P0A959 P77727 ALAA_ECOLI Glutamate-pyruvate aminotransferase AlaA 2.6.1.2 alaA yfbQ b2290 JW2287 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION AS AN AMINOTRANSFERASE AND IN ALANINE BIOSYNTHESIS BIOPHYSICOCHEMICAL PROPERTIES SUBUNIT INDUCTION NOMENCLATURE Involved in the biosynthesis of alanine. 2-oxoglutarate + L-alanine = L-glutamate + pyruvate pyridoxal 5'-phosphate 0.55 mM for pyruvate (at 37 degrees Celsius and pH 8.5) 4.9 mM for alanine (at 37 degrees Celsius and pH 8.5) Homodimer. Cytoplasm Modestly repressed by alanine and leucine via Lrp. Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. 3D-structure Aminotransferase Complete proteome Cytoplasm Pyridoxal phosphate Reference proteome Transferase MSPIEKSSKLENVCYDIRGPVLKEAKRLEEEGNKVLKLNIGNPAPFGFDAPDEILVDVIR NLPTAQGYCDSKGLYSARKAIMQHYQARGMRDVTVEDIYIGNGVSELIVQAMQALLNSGD EMLVPAPDYPLWTAAVSLSSGKAVHYLCDESSDWFPDLDDIRAKITPRTRGIVIINPNNP TGAVYSKELLMEIVEIARQHNLIIFADEIYDKILYDDAEHHSIAPLAPDLLTITFNGLSK TYRVAGFRQGWMVLNGPKKHAKGYIEGLEMLASMRLCANVPAQHAIQTALGGYQSISEFI TPGGRLYEQRNRAWELINDIPGVSCVKPRGALYMFPKIDAKRFNIHDDQKMVLDFLLQEK VLLVQGTAFNWPWPDHFRIVTLPRVDDIELSLSKFARFLSGYHQL P31224 Q2MBW5 ACRB_ECOLI Multidrug efflux pump subunit AcrB AcrAB-TolC multidrug efflux pump subunit AcrB Acridine resistance protein B acrB acrE b0462 JW0451 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 / W4573 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 CHARACTERIZATION INTERACTION WITH ACRA INTERACTION WITH ACRA AND TOLC SUBUNIT SUBCELLULAR LOCATION K12 / MC1061 / ATCC 53338 / DSM 7140 SUBUNIT SUBCELLULAR LOCATION BL21-DE3 TOPOLOGY [LARGE SCALE ANALYSIS] K12 / MG1655 / ATCC 47076 FUNCTION (MICROBIAL INFECTION) DISRUPTION PHENOTYPE K12 / MC4100 FUNCTION INTERACTION WITH ACRZ SUBUNIT INDUCTION MUTAGENESIS OF HIS-526 K12 / MG1655 / ATCC 47076 X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) SUBUNIT X-RAY CRYSTALLOGRAPHY (3.48 ANGSTROMS) IN COMPLEXES WITH SUBSTRATES SUBUNIT X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH SUBSTRATE SUBUNIT FUNCTION X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) SUBUNIT FUNCTION X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) FUNCTION SUBUNIT AcrA-AcrB-AcrZ-TolC is a drug efflux protein complex with broad substrate specificity that uses the proton motive force to export substrates. (Microbial infection) Involved in contact-dependent growth inhibition (CDI), acts downstream of BamA, the receptor for CDI. Its role in CDI is independent of the AcrA-AcrB-TolC efflux pump complex. Homotrimer, with large domains that extend into the periplasm, interacts with AcrA and TolC. AcrA may be required to stably link this protein and TolC. Interacts with AcrZ. Part of the AcrA-AcrB-AcrZ-TolC efflux pump. false 9 P0AAW9 acrZ false 7 P0ADZ7 yajC false 2 Cell inner membrane Multi-pass membrane protein Positively regulated by MarA, Rob and SoxS transcriptional regulators (at protein level). Loss of susceptibility to contact-dependent growth inhibition (CDI); inhibiting cells still contact the target. Belongs to the resistance-nodulation-cell division (RND) (TC 2.A.6) family. 3D-structure Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix Transport H Y MPNFFIDRPIFAWVIAIIIMLAGGLAILKLPVAQYPTIAPPAVTISASYPGADAKTVQDT VTQVIEQNMNGIDNLMYMSSNSDSTGTVQITLTFESGTDADIAQVQVQNKLQLAMPLLPQ EVQQQGVSVEKSSSSFLMVVGVINTDGTMTQEDISDYVAANMKDAISRTSGVGDVQLFGS QYAMRIWMNPNELNKFQLTPVDVITAIKAQNAQVAAGQLGGTPPVKGQQLNASIIAQTRL TSTEEFGKILLKVNQDGSRVLLRDVAKIELGGENYDIIAEFNGQPASGLGIKLATGANAL DTAAAIRAELAKMEPFFPSGLKIVYPYDTTPFVKISIHEVVKTLVEAIILVFLVMYLFLQ NFRATLIPTIAVPVVLLGTFAVLAAFGFSINTLTMFGMVLAIGLLVDDAIVVVENVERVM AEEGLPPKEATRKSMGQIQGALVGIAMVLSAVFVPMAFFGGSTGAIYRQFSITIVSAMAL SVLVALILTPALCATMLKPIAKGDHGEGKKGFFGWFNRMFEKSTHHYTDSVGGILRSTGR YLVLYLIIVVGMAYLFVRLPSSFLPDEDQGVFMTMVQLPAGATQERTQKVLNEVTHYYLT KEKNNVESVFAVNGFGFAGRGQNTGIAFVSLKDWADRPGEENKVEAITMRATRAFSQIKD AMVFAFNLPAIVELGTATGFDFELIDQAGLGHEKLTQARNQLLAEAAKHPDMLTSVRPNG LEDTPQFKIDIDQEKAQALGVSINDINTTLGAAWGGSYVNDFIDRGRVKKVYVMSEAKYR MLPDDIGDWYVRAADGQMVPFSAFSSSRWEYGSPRLERYNGLPSMEILGQAAPGKSTGEA MELMEQLASKLPTGVGYDWTGMSYQERLSGNQAPSLYAISLIVVFLCLAALYESWSIPFS VMLVVPLGVIGALLAATFRGLTNDVYFQVGLLTTIGLSAKNAILIVEFAKDLMDKEGKGL IEATLDAVRMRLRPILMTSLAFILGVMPLVISTGAGSGAQNAVGTGVMGGMVTATVLAIF FVPVFFVVVRRRFSRKNEDIEHSHTVDHH P0A6E1 P08329 Q2MC37 AROL_ECOLI Shikimate kinase 2 SK 2 2.7.1.71 Shikimate kinase II SKII aroL b0388 JW0379 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] PROTEIN SEQUENCE OF 2-25 FUNCTION SUBUNIT K12 NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 PROTEIN SEQUENCE OF 2-9 FUNCTION COFACTOR KINETIC PARAMETERS K12 INDUCTION K12 INDUCTION K12 INDUCTION K12 Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate. ATP + shikimate = 3-phosphoshikimate + ADP + H(+) Mg(2+) Binds 1 Mg(2+) ion per subunit. 200 uM for shikimate 160 uM for ATP Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. Monomer. Cytoplasm Expressed under the control of TyrR and TrpR repressors. The LID domain closes over the active site upon ATP binding. Two isozymes have been found in E.coli. AroK has 100-fold lower affinity for shikimate than AroL, suggesting that AroL is the dominant enzyme in the biosynthesis of the aromatic amino acids, with AroK playing a secondary role and possibly participating in an as yet unidentified cellular process. Belongs to the shikimate kinase family. AroL subfamily. Amino-acid biosynthesis Aromatic amino acid biosynthesis ATP-binding Complete proteome Cytoplasm Direct protein sequencing Kinase Magnesium Metal-binding Nucleotide-binding Reference proteome Transferase MTQPLFLIGPRGCGKTTVGMALADSLNRRFVDTDQWLQSQLNMTVAEIVEREEWAGFRAR ETAALEAVTAPSTVIATGGGIILTEFNRHFMQNNGIVVYLCAPVSVLVNRLQAAPEEDLR PTLTGKPLSEEVQEVLEERDALYREVAHIIIDATNEPSQVISEIRSALAQTINC P75980 A0A385XJE3 BEEE_ECOLI Protein BeeE beeE ymfO b1151 JW1137 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Encoded by the e14 prophage. Missing up to 260 C-terminal residues compared to orthologs. Belongs to the phage portal family. Complete proteome Reference proteome MFFSGLFQRKSDAPVTTPAELADAIGLSYDTYTGKQISSQRAMRLTAVFSCVRVLAESVG MLPCNLYHLNGSLKQRATGERLHKLISTHPNGYMTPQEFWELVVTCLCLRGNFYAYKVKA FGEVAELLPVDPGCVVYALGRCQRWPEGDRRECYSAR P31469 Q2M835 CBRC_ECOLI UPF0167 protein CbrC CreB-regulated gene C protein cbrC yieJ b3717 JW3695 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 INDUCTION BY CREBC MUTANT STUDIES Induced by the two-component regulatory system CreC/CreB. Disruption of this gene leads to hypersensibility to nitrofurazone. Belongs to the UPF0167 family. Complete proteome Reference proteome MTQNIRPLPQFKYHPKPLETGAFEQDKTVECDCCEQQTSVYYSGPFYCVDEVEHLCPWCI ADGSAAEKFAGSFQDDASIEGVEFEYDEEDEFAGIKNTYPDEMLKELVERTPGYHGWQQE FWLAHCGDFCVFIGYVGWNDIKDRLDEFANLEEDCENFGIRNSDLAKCLQKGGHCQGYLF RCLHCGKLRLWGDFS P07639 Q2M754 AROB_ECOLI 3-dehydroquinate synthase DHQS 4.2.3.4 aroB b3389 JW3352 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 357-362 K12 FUNCTION CATALYTIC ACTIVITY COFACTOR KINETIC PARAMETERS SUBUNIT Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate NAD(+) Co(2+) Zn(2+) Binds 1 divalent metal cation per subunit. Displays higher activity with Co(2+), however, Zn(2+) may be the physiological metal cofactor. 0.6 uM for 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate (at pH 6.5) 5.5 uM for 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate (at pH 8.5) Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. Monomer. P68646 fixX false 2 Cytoplasm Belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family. Amino-acid biosynthesis Aromatic amino acid biosynthesis Cobalt Complete proteome Cytoplasm Lyase Metal-binding NAD Nucleotide-binding Reference proteome Zinc MERIVVTLGERSYPITIASGLFNEPASFLPLKSGEQVMLVTNETLAPLYLDKVRGVLEQA GVNVDSVILPDGEQYKSLAVLDTVFTALLQKPHGRDTTLVALGGGVVGDLTGFAAASYQR GVRFIQVPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQPASVVVDLDCLKTLPPRELAS GLAEVIKYGIILDGAFFNWLEENLDALLRLDGPAMAYCIRRCCELKAEVVAADERETGLR ALLNLGHTFGHAIEAEMGYGNWLHGEAVAAGMVMAARTSERLGQFSSAETQRIITLLKRA GLPVNGPREMSAQAYLPHMLRDKKVLAGEMRLILPLAIGKSEVRSGVSHELVLNAIADCQ SA P0A6G5 P77563 Q2MBK2 CITX_ECOLI Apo-citrate lyase phosphoribosyl-dephospho-CoA transferase 2.7.7.61 Apo-ACP nucleodityltransferase Holo-ACP synthase Holo-citrate lyase synthase citX ybdU b0614 JW0606 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 GENE NAME K12 FUNCTION CATALYTIC ACTIVITY FUNCTION CATALYTIC ACTIVITY BL21-DE3 K12 / DH5-alpha OPERON STRUCTURE INDUCTION K12 / BW25113 Transfers 2-(5''-triphosphoribosyl)-3'-dephosphocoenzyme-A on a serine residue to the apo-acyl carrier protein (gamma chain) of the citrate lyase to yield holo-acyl carrier protein. 2'-(5''-triphospho-alpha-D-ribosyl)-3'-dephospho-CoA + apo-[citrate lyase ACP] = diphosphate + holo-[citrate lyase ACP] Repressed by H-NS. Part of the citCDEFXG operon. Belongs to the CitX family. Complete proteome Nucleotidyltransferase Reference proteome Transferase MHLLPELASHHAVSIPELLVSRDERQARQHVWLKRHPVPLVSFTVVAPGPIKDSEVTRRI FNHGVTALRALAAKQGWQIQEQAALVSASGPEGMLSIAAPARDLKLATIELEHSHPLGRL WDIDVLTPEGEILSRRDYSLPPRRCLLCEQSAAVCARGKTHQLTDLLNRMEALLNDVDAC NVN P0A9Q7 P17547 ADHE_ECOLI Aldehyde-alcohol dehydrogenase Alcohol dehydrogenase ADH 1.1.1.1 Acetaldehyde dehydrogenase [acetylating] ACDH 1.2.1.10 Pyruvate-formate-lyase deactivase PFL deactivase adhE ana b1241 JW1228 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] PROTEIN SEQUENCE OF 2-11 NUCLEOTIDE SEQUENCE [GENOMIC DNA] PROTEIN SEQUENCE OF 2-7 CHARACTERIZATION K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 849-891 K12 PROTEIN SEQUENCE OF 2-21 IDENTIFICATION BY 2D-GEL ANTIOXIDANT ROLE OF ADHE K12 / MC4100 / ATCC 35695 / DSM 6574 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-358 IDENTIFICATION BY MASS SPECTROMETRY K12 / JW1106 K12 / MG1655 / ATCC 47076 This enzyme has three activities: ADH, ACDH, and PFL-deactivase. In aerobic conditions it acts as a hydrogen peroxide scavenger. The PFL deactivase activity catalyzes the quenching of the pyruvate-formate-lyase catalyst in an iron, NAD, and CoA dependent reaction. a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH a secondary alcohol + NAD(+) = a ketone + H(+) + NADH acetaldehyde + CoA + NAD(+) = acetyl-CoA + H(+) + NADH Fe cation Seems to form a rod shaped polymer composed of about 40 identical subunits. false 2 P0A7V0 rpsB false 2 Under anaerobic conditions in the absence of nitrate. In the N-terminal section; belongs to the aldehyde dehydrogenase family. In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase family. Acetylation Complete proteome Direct protein sequencing Iron Multifunctional enzyme NAD Oxidoreductase Reference proteome MAVTNVAELNALVERVKKAQREYASFTQEQVDKIFRAAALAAADARIPLAKMAVAESGMG IVEDKVIKNHFASEYIYNAYKDEKTCGVLSEDDTFGTITIAEPIGIICGIVPTTNPTSTA IFKSLISLKTRNAIIFSPHPRAKDATNKAADIVLQAAIAAGAPKDLIGWIDQPSVELSNA LMHHPDINLILATGGPGMVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVASVLMSKTF DNGVICASEQSVVVVDSVYDAVRERFATHGGYLLQGKELKAVQDVILKNGALNAAIVGQP AYKIAELAGFSVPENTKILIGEVTVVDESEPFAHEKLSPTLAMYRAKDFEDAVEKAEKLV AMGGIGHTSCLYTDQDNQPARVSYFGQKMKTARILINTPASQGGIGDLYNFKLAPSLTLG CGSWGGNSISENVGPKHLINKKTVAKRAENMLWHKLPKSIYFRRGSLPIALDEVITDGHK RALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLSIVRKGAELANSFKPDVI IALGGGSPMDAAKIMWVMYEHPETHFEELALRFMDIRKRIYKFPKMGVKAKMIAVTTTSG TGSEVTPFAVVTDDATGQKYPLADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAME AYVSVLASEFSDGQALQALKLLKEYLPASYHEGSKNPVARERVHSAATIAGIAFANAFLG VCHSMAHKLGSQFHIPHGLANALLICNVIRYNANDNPTKQTAFSQYDRPQARRRYAEIAD HLGLSAPGDRTAAKIEKLLAWLETLKAELGIPKSIREAGVQEADFLANVDKLSEDAFDDQ CTGANPRYPLISELKQILLDTYYGRDYVEGETAAKKEAAPAKAEKKAKKSA P76290 O07982 CMOA_ECOLI Carboxy-S-adenosyl-L-methionine synthase Cx-SAM synthase 2.1.3.- cmoA yecO b1870 JW1859 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 19-247 IN COMPLEX WITH CARBOXY-S-ADENOSYL-METHIONINE SUBUNIT X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH CARBOXY-S-ADENOSYL-METHIONINE FUNCTION CATALYTIC ACTIVITY MUTAGENESIS OF ASP-89 Catalyzes the conversion of S-adenosyl-L-methionine (SAM) to carboxy-S-adenosyl-L-methionine (Cx-SAM). prephenate + S-adenosyl-L-methionine = 3-phenylpyruvate + carboxy-S-adenosyl-L-methionine + H2O Homodimer. Mechanistic analyses show the involvement of a unique ylide intermediate as the carboxyl acceptor in the conversion of SAM to Cx-SAM. Belongs to the class I-like SAM-binding methyltransferase superfamily. Cx-SAM synthase family. 3D-structure Complete proteome Reference proteome S-adenosyl-L-methionine Transferase D L MSHRDTLFSAPIARLGDWTFDERVAEVFPDMIQRSVPGYSNIISMIGMLAERFVQPGTQV YDLGCSLGAATLSVRRNIHHDNCKIIAIDNSPAMIERCRRHIDAYKAPTPVDVIEGDIRD IAIENASMVVLNFTLQFLEPSERQALLDKIYQGLNPGGALVLSEKFSFEDAKVGELLFNM HHDFKRANGYSELEISQKRSMLENVMLTDSVETHKARLHNAGFEHSELWFQCFNFGSLVA LKAEDAA P33647 Q2M680 CHPB_ECOLI Endoribonuclease toxin ChpB 3.1.-.- Toxin ChpB mRNA interferase ChpB chpB chpBK yjfE b4225 JW4184 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] FUNCTION PROBABLE OPERON STRUCTURE K12 / MC1000 / ATCC 39531 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30 K12 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-116 K12 GENE MAPPING DISRUPTION PHENOTYPE K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION RNA CLEAVAGE DISRUPTION PHENOTYPE K12 / MG1655 / ATCC 47076 FUNCTION AS AN RNA ENDORIBONUCLEASE SUBUNIT INTERACTION WITH CHPS FUNCTION ACTIVITY REGULATION FUNCTION IN PERSISTENCE DISRUPTION PHENOTYPE K12 / MG1655 / ATCC 47076 Toxic component of a type II toxin-antitoxin (TA) system. ChpB is a sequence-specific mRNA and (weak) tmRNA endoribonuclease that inhibits protein synthesis and induces bacterial stasis. Cleavage is independent of the ribosome. Cleavage occurs at ACY sequences where Y is not C. The endoribonuclease activity is not as strong as that of MazF. The endoribonuclease activity (a toxin) is inhibited by its labile cognate antitoxin ChpS. Toxicity results when the levels of ChpS decrease in the cell, leading to mRNA degradation. Both ChpS and ChpB probably bind to the promoter region of the chpS-chpB operon to autoregulate their synthesis. mRNA interferases play a role in bacterial persistence to antibiotics (PubMed:21788497). Stimulated in vitro in a concentration-dependent fashion by extracellular death factor (EDF, a quorum sensing pentapeptide sequence NNWNN, probably produced from the zwf gene product glucose-6-phosphate 1-dehydrogenase), which is able to overcome inhibition by cognate antitoxin ChpS. Homodimer, interacts with ChpS, which inhibits the endoribonuclease activity. Part of the chpS-chpB operon. No visible phenotype (PubMed:8083180, PubMed:12972253). mRNA interferases play a role in bacterial persistence to antibiotics; as 10 mRNA interferases are successively deleted reduced levels of persisters are generated (PubMed:21788497). Belongs to the PemK/MazF family. Complete proteome DNA-binding Endonuclease Hydrolase Nuclease Reference proteome RNA-binding Toxin-antitoxin system MVKKSEFERGDIVLVGFDPASGHEQQGAGRPALVLSVQAFNQLGMTLVAPITQGGNFARY AGFSVPLHCEEGDVHGVVLVNQVRMMDLHARLAKRIGLAADEVVEEALLRLQAVVE P76541 Q2MAJ1 EUTL_ECOLI Ethanolamine utilization protein EutL eutL yffJ b2439 JW2432 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 May be involved in the formation of a specific microcompartment in the cell in which the metabolism of potentially toxic by-products takes place. Amine and polyamine degradation; ethanolamine degradation. false 2 Belongs to the EutL/PduB family. 3D-structure Complete proteome Reference proteome MPALDLIRPSVTAMRVIASVNADFARELKLPPHIRSLGLISADSDDVTYIAADEATKQAM VEVVYGRSLYAGAAHGPSPTAGEVLIMLGGPNPAEVRAGLDAMIAHIENGAAFQWANDAQ DTAFLAHVVSRTGSYLSSTAGITLGDPMAYLVAPPLEATYGIDAALKSADVQLATYVPPP SETNYSAAFLTGSQAACKAACNAFTDAVLEIARNPIQRA P46859 P78116 Q2M7A0 Q59404 GNTK_ECOLI Thermoresistant gluconokinase 2.7.1.12 Gluconate kinase 2 gntK b3437 JW3400 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 PROTEIN SEQUENCE OF 2-20 CHARACTERIZATION CRYSTALLIZATION ATP + D-gluconate = 6-phospho-D-gluconate + ADP + H(+) Carbohydrate acid metabolism; D-gluconate degradation. Belongs to the gluconokinase GntK/GntV family. 3D-structure ATP-binding Complete proteome Direct protein sequencing Kinase Nucleotide-binding Reference proteome Transferase MSTTNHDHHIYVLMGVSGSGKSAVASEVAHQLHAAFLDGDFLHPRRNIEKMASGEPLNDD DRKPWLQALNDAAFAMQRTNKVSLIVCSALKKHYRDLLREGNPNLSFIYLKGDFDVIESR LKARKGHFFKTQMLVTQFETLQEPGADETDVLVVDIDQPLEGVVASTIEVIKKGK P68699 P00844 Q2M855 ATPL_ECOLI ATP synthase subunit c ATP synthase F(0) sector subunit c Dicyclohexylcarbodiimide-binding protein F-type ATPase subunit c F-ATPase subunit c Lipid-binding protein atpE papH uncE b3737 JW3715 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia PROTEIN SEQUENCE NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] PROTEIN SEQUENCE MUTAGENESIS OF ILE-28 AND ASP-61 K12 NUCLEOTIDE SEQUENCE [GENOMIC DNA] MUTAGENESIS OF GLY-23 AND LEU-31 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 SUBUNIT SUBUNIT C FUSIONS SUBCELLULAR LOCATION K12 / MG1655 / ATCC 47076 STRUCTURE BY NMR SITE STRUCTURE BY NMR STRUCTURE BY NMR STRUCTURE BY NMR 3D-STRUCTURE MODELING F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of 10 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Cell inner membrane Multi-pass membrane protein Dicyclohexylcarbodiimide (DCDD) binding to the reversibly protonated aspartate residue inhibits ATPase in vitro. In this organism c-rings of between c(8) and c(12) can be isolated in vivo following experimental manipulations, however only c(8) and c(9), in addition to c(10), are partially functional. Belongs to the ATPase C chain family. 3D-structure ATP synthesis Cell inner membrane Cell membrane CF(0) Complete proteome Direct protein sequencing Formylation Hydrogen ion transport Ion transport Lipid-binding Membrane Reference proteome Transmembrane Transmembrane helix Transport G D I V L F D G F S MENLNMDLLYMAAAVMMGLAAIGAAIGIGILGGKFLEGAARQPDLIPLLRTQFFIVMGLV DAIPMIAVGLGLYVMFAVA P23908 Q2M8Q2 ARGE_ECOLI Acetylornithine deacetylase AO Acetylornithinase 3.5.1.16 N-acetylornithinase NAO argE b3957 JW3929 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 / DH5-alpha K12 / JM101 / ATCC 33876 / DSM 3948 / NCIMB 11926 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11 K12 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11 CHARACTERIZATION Displays a broad specificity and can also deacylate substrates such as acetylarginine, acetylhistidine or acetylglutamate semialdehyde. H2O + N(2)-acetyl-L-ornithine = acetate + L-ornithine Zn(2+) Co(2+) Binds 2 Zn(2+) or Co(2+) ions per subunit. glutathione Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine from N(2)-acetyl-L-ornithine (linear): step 1/1. Homodimer. Cytoplasm Belongs to the peptidase M20A family. ArgE subfamily. Amino-acid biosynthesis Arginine biosynthesis Cobalt Complete proteome Cytoplasm Hydrolase Metal-binding Reference proteome Zinc MKNKLPPFIEIYRALIATPSISATEEALDQSNADLITLLADWFKDLGFNVEVQPVPGTRN KFNMLASIGQGAGGLLLAGHTDTVPFDDGRWTRDPFTLTEHDGKLYGLGTADMKGFFAFI LDALRDVDVTKLKKPLYILATADEETSMAGARYFAETTALRPDCAIIGEPTSLQPVRAHK GHISNAIRIQGQSGHSSDPARGVNAIELMHDAIGHILQLRDNLKERYHYEAFTVPYPTLN LGHIHGGDASNRICACCELHMDIRPLPGMTLNELNGLLNDALAPVSERWPGRLTVDELHP PIPGYECPPNHQLVEVVEKLLGAKTEVVNYCTEAPFIQTLCPTLVLGPGSINQAHQPDEY LETRFIKPTRELITQVIHHFCWH P07363 P76302 CHEA_ECOLI Chemotaxis protein CheA 2.7.13.3 cheA b1888 JW1877 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 430-654 PHOSPHORYLATION AT HIS-48 DOMAINS SUBUNIT STRUCTURE BY NMR OF 1-233 STRUCTURE BY NMR OF 124-257 STRUCTURE BY NMR OF 1-134 X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 158-228 X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 158-226 Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to either CheB or CheY. ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. An in vitro complex of CheW/CheA(L)/CheA(S) in a 1:1:1 ratio increases the autophosphorylation of CheA and is required for the binding of CheY, the phosphorylation substrate. This complex accounts for 10% of the total number of molecules. P07330 cheB false 3 P0AE67 cheY false 7 P0A9H9 cheZ false 3 P07017 tar false 4 Cytoplasm P07363-1 cheA(L) long large P07363-2 cheA(S) short May have three functional domains: one for interaction with CheB and CheY, a second for regulating phosphorylation and controlling the stability of the protein, and a third for receiving input signals regulating CheA activity. 3D-structure Alternative initiation ATP-binding Chemotaxis Complete proteome Cytoplasm Kinase Nucleotide-binding Phosphoprotein Reference proteome Transferase Two-component regulatory system R P GERVLEVRGEYLPIVELW ASGCWKCGVNICPSSNCG V A MSMDISDFYQTFFDEADELLADMEQHLLVLQPEAPDAEQLNAIFRAAHSIKGGAGTFGFS VLQETTHLMENLLDEARRGEMQLNTDIINLFLETKDIMQEQLDAYKQSQEPDAASFDYIC QALRQLALEAKGETPSAVTRLSVVAKSEPQDEQSRSQSPRRIILSRLKAGEVDLLEEELG HLTTLTDVVKGADSLSAILPGDIAEDDITAVLCFVIEADQITFETVEVSPKISTPPVLKL AAEQAPTGRVEREKTTRSNESTSIRVAVEKVDQLINLVGELVITQSMLAQRSSELDPVNH GDLITSMGQLQRNARDLQESVMSIRMMPMEYVFSRYPRLVRDLAGKLGKQVELTLVGSST ELDKSLIERIIDPLTHLVRNSLDHGIELPEKRLAAGKNSVGNLILSAEHQGGNICIEVTD DGAGLNRERILAKAASQGLTVSENMSDDEVAMLIFAPGFSTAEQVTDVSGRGVGMDVVKR NIQKMGGHVEIQSKQGTGTTIRILLPLTLAILDGMSVRVADEVFILPLNAVMESLQPREA DLHPLAGGERVLEVRGEYLPIVELWKVFNVAGAKTEATQGIVVILQSGGRRYALLVDQLI GQHQVVVKNLESNYRKVPGISAATILGDGSVALIVDVSALQAINREQRMANTAA P0ADP5 P27849 Q2M8D2 Q8X5G7 BIOP_ECOLI Biotin transporter Plasmamembrane biotin transport protein bioP yigM b3827 JW3803 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 DISRUPTION PHENOTYPE GENE NAME FUNCTION ACTIVITY REGULATION BIOPHYSICOCHEMICAL PROPERTIES SUBCELLULAR LOCATION INDUCTION DISRUPTION PHENOTYPE DISRUPTION PHENOTYPE Uptake of biotin. Acts probably by facilitated diffusion. Biotin uptake is weakly inhibited by CCCP and FCCP protonophores and by the respiratory chain blocker NaN(3). 74 nM for biotin Cell inner membrane Multi-pass membrane protein Expression is repressed by biotin. Deletion of the gene abolishes biotin uptake (Ref.5, PubMed:1091631). BioH-bioP double mutant is unable to grow on trace levels of biotin (PubMed:24256712). Belongs to the drug/metabolite transporter (DMT) superfamily. 10 TMS drug/metabolite exporter (DME) (TC 2.A.7.3) family. Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Repeat Transmembrane Transmembrane helix Transport MALLIITTILWAFSFSFYGEYLAGHVDSYFAVLVRVGLAALVFLPFLRTRGNSLKTVGLY MLVGAMQLGVMYMLSFRAYLYLTVSELLLFTVLTPLYITLIYDIMSKRRLRWGYAFSALL AVIGAGIIRYDQVTDHFWTGLLLVQLSNITFAIGMVGYKRLMETRPMPQHNAFAWFYLGA FLVAVIAWFLLGNAQKMPQTTLQWGILVFLGVVASGIGYFMWNYGATQVDAGTLGIMNNM HVPAGLLVNLAIWHQQPHWPTFITGALVILASLWVHRKWVAPRSSQTADDRRRDCALSE P69330 O54336 P77618 CITD_ECOLI Citrate lyase acyl carrier protein Citrate lyase gamma chain citD ybdX b0617 JW0609 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 OPERON STRUCTURE INDUCTION K12 / BW25113 Covalent carrier of the coenzyme of citrate lyase. Oligomer with a subunit composition of (alpha,beta, gamma)6. Cytoplasm Repressed by H-NS. Part of the citCDEFXG operon. Belongs to the CitD family. Complete proteome Cytoplasm Phosphoprotein Reference proteome PWEDCQ HGRIANDFRFAATT MKINQPAVAGTLESGDVMIRIAPLDTQDIDLQINSSVEKQFGDAIRTTILDVLARYNVRG VQLNVDDKGALDCILRARLEALLARASGIPALPWEDCQ P33234 Q2M6I8 ADIY_ECOLI HTH-type transcriptional regulator AdiY adiY b4116 JW4077 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Complete proteome DNA-binding Reference proteome Transcription Transcription regulation MRICSDQPCIVLLTEKDVWIRVNGKEPISLKANHMALLNCENNIIDVSSLNNTLVAHISH DIIKDYLRFLNKDLSQIPVWQRSATPILTLPCLTPDVFRVAAQHSMMPAETESEKERTRA LLFTVLSRFLDSKKFVSLMMYMLRNCVSDSVYQIIESDIHKDWNLSMVASCLCLSPSLLK KKLKSENTSYSQIITTCRMRYAVNELMMDGKNISQVSQSCGYNSTSYFISVFKDFYGMTP LHYVSQHRERTVA P0AE08 P26427 AHPC_ECOLI Alkyl hydroperoxide reductase C 1.11.1.15 Alkyl hydroperoxide reductase protein C22 Peroxiredoxin SCRP-23 Sulfate starvation-induced protein 8 SSI8 Thioredoxin peroxidase ahpC b0605 JW0598 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 PROTEIN SEQUENCE OF 2-31 PROTEIN SEQUENCE OF 2-28 AND 70-81 K12 / EMG2 PROTEIN SEQUENCE OF 2-21 SUBCELLULAR LOCATION K12 PROTEIN SEQUENCE OF 2-14 K12 / W3110 / ATCC 27325 / DSM 5911 PROTEIN SEQUENCE OF 2-11 K12 / MC4100 / ATCC 35695 / DSM 6574 PROTEIN SEQUENCE OF 2-5 K12 / W3110 / ATCC 27325 / DSM 5911 IDENTIFICATION BY 2D-GEL FUNCTION ROLE IN HYDROXYUREA RESISTANCE DISRUPTION PHENOTYPE K12 / MC4100 / ATCC 35695 / DSM 6574 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-17; LYS-93; LYS-153; LYS-169 AND LYS-171 IDENTIFICATION BY MASS SPECTROMETRY K12 / JW1106 K12 / MG1655 / ATCC 47076 SUBUNIT X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 162-186 DISULFIDE BONDS Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides. Is the primary scavenger for endogenously generated hydrogen peroxides. [protein]-dithiol + a hydroperoxide = [protein]-disulfide + an alcohol + H2O Homodimer; disulfide-linked, upon oxidation. 5 homodimers assemble to form a ring-like decamer (PubMed:7499381). false 2 Cytoplasm Repressed by sulfate or cysteine. Increased sensitivity to hydroxyurea, probably because more reactive oxygen species accumulate. The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this typical 2-Cys peroxiredoxin, C(R) is provided by the other dimeric subunit to form an intersubunit disulfide. The disulfide is subsequently reduced by AhpF. Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily. 3D-structure Acetylation Antioxidant Complete proteome Cytoplasm Direct protein sequencing Disulfide bond Oxidoreductase Peroxidase Redox-active center Reference proteome MSLINTKIKPFKNQAFKNGEFIEITEKDTEGRWSVFFFYPADFTFVCPTELGDVADHYEE LQKLGVDVYAVSTDTHFTHKAWHSSSETIAKIKYAMIGDPTGALTRNFDNMREDEGLADR ATFVVDPQGIIQAIEVTAEGIGRDASDLLRKIKAAQYVASHPGEVCPAKWKEGEATLAPS LDLVGKI P43533 P77520 FLGN_ECOLI Flagella synthesis protein FlgN flgN b1070 JW1057 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-38 Required for the efficient initiation of filament assembly. P33235 flgK false 3 Cytoplasm Belongs to the FlgN family. Bacterial flagellum biogenesis Complete proteome Cytoplasm Reference proteome MTRLAEILDQMSAVLNDLKTVMDQEQQHLSMGQINGSQLQWITEQKSSLLATLDYLEQLR RKEPNTANSVDISQRWQEITVKTQQLRQMNQHNGWLLEGQIERNQQALEMLKPHQEPTLY GANGQTSTTHRGGKKISI P0A6S0 P75940 Q9R7P0 FLGH_ECOLI Flagellar L-ring protein Basal body L-ring protein flgH fla FVIII flaY b1079 JW5153 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. The basal body constitutes a major portion of the flagellar organelle and consists of four rings (L,P,S, and M) mounted on a central rod. Cell outer membrane Lipid-anchor Bacterial flagellum basal body Belongs to the FlgH family. Bacterial flagellum Cell outer membrane Complete proteome Lipoprotein Membrane Palmitate Reference proteome Signal MQKNAAHTYAISSLLVLSLTGCAWIPSTPLVQGATSAQPVPGPTPVANGSIFQSAQPINY GYQPLFEDRRPRNIGDTLTIVLQENVSASKSSSANASRDGKTNFGFDTVPRYLQGLFGNA RADVEASGGNTFNGKGGANASNTFSGTLTVTVDQVLVNGNLHVVGEKQIAINQGTEFIRF SGVVNPRTISGSNTVPSTQVADARIEYVGNGYINEAQNMGWLQRFFLNLSPM P77218 EUTD_ECOLI Ethanolamine utilization protein EutD eutD eutI ypfA b2458 JW2442 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Amine and polyamine degradation; ethanolamine degradation. Belongs to the phosphate acetyltransferase and butyryltransferase family. 3D-structure Acyltransferase Complete proteome Reference proteome Transferase MIIERCRELALRAPARVVFPDALDQRVLKAAQYLHQQGLATPILVANPFELRQFALSHGV AMDGLQVIDPHGNLAMREEFAHRWLARAGEKTPPDALEKLTDPLMFAAAMVSAGKADVCI AGNLSSTANVLRAGLRIIGLQPGCKTLSSIFLMLPQYSGPALGFADCSVVPQPTAAQLAD IALASAETWRAITGEEPRVAMLSFSSNGSARHPCVANVQQATEIVRERAPKLVVDGELQF DAAFVPEVAAQKAPASPLQGKANVMVFPSLEAGNIGYKIAQRLGGYRAVGPLIQGLAAPM HDLSRGCSVQEIIELALVAAVPRQTEVNRESSLQTLVE P77445 EUTE_ECOLI Ethanolamine utilization protein EutE eutE yffX b2455 JW2439 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 May act as an acetaldehyde dehydrogenase that converts acetaldehyde into acetyl-CoA. Amine and polyamine degradation; ethanolamine degradation. Complete proteome Oxidoreductase Reference proteome MNQQDIEQVVKAVLLKMQSSDTPSAAVHEMGVFASLDDAVAAAKVAQQGLKSVAMRQLAI AAIREAGEKHARDLAELAVSETGMGRVEDKFAKNVAQARGTPGVECLSPQVLTGDNGLTL IENAPWGVVASVTPSTNPAATVINNAISLIAAGNSVIFAPHPAAKKVSQRAITLLNQAIV AAGGPENLLVTVANPDIETAQRLFKFPGIGLLVVTGGEAVVEAARKHTNKRLIAAGAGNP PVVVDETADLARAAQSIVKGASFDNNIICADEKVLIVVDSVADELMRLMEGQHAVKLTAE QAQQLQPVLLKNIDERGKGTVSRDWVGRDAGKIAAAIGLKVPQETRLLFVETTAEHPFAV TELMMPVLPVVRVANVADAIALAVKLEGGCHHTAAMHSRNIENMNQMANAIDTSIFVKNG PCIAGLGLGGEGWTTMTITTPTGEGVTSARTFVRLRRCVLVDAFRIV P0AEL8 P21502 P77080 Q2MBP4 FIMZ_ECOLI Fimbriae Z protein fimZ ybcA b0535 JW5073 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Cytoplasm Complete proteome Cytoplasm DNA-binding Phosphoprotein Reference proteome Transcription Transcription regulation Two-component regulatory system MKPTSVIIMDTHPIIRMSIEVLLQKNSELQIVLKTDDYRITIDYLRTRPVDLIIMDIDLP GTDGFTFLKRIKQIQSTVKVLFLSSKSECFYAGRAIQAGANGFVSKCNDQNDIFHAVQMI LSGYTFFPSETLNYIKSNKCSTNSSTVTVLSNREVTILRYLVSGLSNKEIADKLLLSNKT VSAHKSNIYGKLGLHSIVELIDYAKLYELI P15286 P77706 Q9JN62 FLK_ECOLI Flagellar regulator flk Fluke flk div b2321 JW2318 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39 K12 / W3110 / ATCC 27325 / DSM 5911 Acts as a regulator of flagellar gene expression by modulating the protein level of the anti sigma factor FlgM upon sensing ring completion or hook elongation. Flk could inhibit FlgM secretion by acting as a braking system for the flagellar-associated type III secretion (T3S) system. Plays a role in hindering to flip the flagellar T3S specificity switch from the rod and hook-type substrates to filament-type substrates prior to hook-basal body (HBB) completion possibly by preventing interaction of FliK with FlhB (By similarity). Cell inner membrane Single-pass membrane protein Belongs to the flk family. Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MIQPISGPPPGQPPGQGDNLPSGTGNQPLSSQQRTSLESLMTKVTSLTQQQRAELWAGIR HDIGLSGDSPLLSRHFPAAEHNLAQRLLAAQKSHSARQLLAQLGEYLRLGNNRQAVTDYI RHNFGQTPLNQLSPEQLKTILTLLQEGKMVIPQPQQREATDRPLLPAEHNALKQLVTKLA AATGEPSKQIWQSMLELSGVKDGELIPAKLFNHLVTWLQARQTLSQQNTPTLESLQMTLK QPLDASELAALSAYIQQKYGLSAQSSLSSAQAEDILNQLYQRRVKGIDPRVMQPLLNPFP PMMDTLQNMATRPALWILLVAIILMLVWLVR P0ABP3 Q47134 Q9ZBC9 Q9ZBD0 DCUC_ECOLI Anaerobic C4-dicarboxylate transporter DcuC dcuC b0621 JW0613/JW0616 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 / AN387 NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION K12 / AN387 SUBCELLULAR LOCATION K12 / MG1655 / ATCC 47076 Responsible for the transport of C4-dicarboxylates during anaerobic growth. Cell inner membrane Multi-pass membrane protein Belongs to the DcuC/DcuD transporter (TC 2.A.61) family. PubMed:8905232 and PubMed:16738553 sequences differ from that shown due to the presence of an IS5 insertion element between codons 327 and 328. Strain W3110A but not W3110B harbors this IS5 insertion. Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix Transport MLTFIELLIGVVVIVGVARYIIKGYSATGVLFVGGLLLLIISAIMGHKVLPSSQASTGYS ATDIVEYVKILLMSRGGDLGMMIMMLCGFAAYMTHIGANDMVVKLASKPLQYINSPYLLM IAAYFVACLMSLAVSSATGLGVLLMATLFPVMVNVGISRGAAAAICASPAAIILAPTSGD VVLAAQASEMSLIDFAFKTTLPISIAAIIGMAIAHFFWQRYLDKKEHISHEMLDVSEITT TAPAFYAILPFTPIIGVLIFDGKWGPQLHIITILVICMLIASILEFLRSFNTQKVFSGLE VAYRGMADAFANVVMLLVAAGVFAQGLSTIGFIQSLISIATSFGSASIILMLVLVILTML AAVTTGSGNAPFYAFVEMIPKLAHSSGINPAYLTIPMLQASNLGRTLSPVSGVVVAVAGM AKISPFEVVKRTSVPVLVGLVIVIVATELMVPGTAAAVTGK P0A6W5 P21346 P78111 Q2M931 Q8X9K9 GREA_ECOLI Transcription elongation factor GreA Transcript cleavage factor GreA greA b3181 JW3148 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 IDENTIFICATION BY 2D-GEL X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) Necessary for efficient RNA polymerase transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by cleavage factors such as GreA or GreB allows the resumption of elongation from the new 3'terminus. GreA releases sequences of 2 to 3 nucleotides. Belongs to the GreA/GreB family. Translation N-terminally extended. 3D-structure Complete proteome DNA-binding Reference proteome Transcription Transcription regulation MQAIPMTLRGAEKLREELDFLKSVRRPEIIAAIAEAREHGDLKENAEYHAAREQQGFCEG RIKDIEAKLSNAQVIDVTKMPNNGRVIFGATVTVLNLDSDEEQTYRIVGDDEADFKQNLI SVNSPIARGLIGKEEDDVVVIKTPGGEVEFEVIKVEYL P0AC55 P38504 P77118 Q2MBX6 GLNK_ECOLI Nitrogen regulatory protein P-II 2 glnK ybaI b0450 JW0440 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 IDENTIFICATION CHARACTERIZATION X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) P-II indirectly controls the transcription of the glutamine synthetase gene (glnA). P-II prevents NR-II-catalyzed conversion of NR-I to NR-I-phosphate, the transcriptional activator of GlnA. When P-II is uridylylated to P-II-UMP, these events are reversed. When the ratio of Gln to 2-ketoglutarate decreases, P-II is uridylylated to P-II-UMP, which causes the deadenylation of glutamine synthetase by GlnE, so activating the enzyme (By similarity). Homotrimer. false 3 P69681 amtB false 3 P0A9Z1 glnB false 3 P27249 glnD false 3 P0AFB5 glnL false 5 Uridylylated/deuridylylated by GlnD. Belongs to the P(II) protein family. 3D-structure Complete proteome Nucleotide-binding Phosphoprotein Reference proteome Transcription Transcription regulation MKLVTVIIKPFKLEDVREALSSIGIQGLTVTEVKGFGRQKGHAELYRGAEYSVNFLPKVK IDVAIADDQLDEVIDIVSKAAYTGKIGDGKIFVAELQRVIRIRTGEADEAAL P04036 DAPB_ECOLI 4-hydroxy-tetrahydrodipicolinate reductase HTPA reductase 1.17.1.8 dapB b0031 JW0029 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 269-273 PROTEIN SEQUENCE OF 1-18 FUNCTION KINETIC PARAMETERS SUBSTRATE SPECIFICITY SUBUNIT MASS SPECTROMETRY K12 INDUCTION K12 / MG1655 / ATCC 47076 FUNCTION CATALYTIC ACTIVITY IDENTIFICATION OF HTPA AS REACTION SUBSTRTATE ACTIVE SITE X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH NADPH K12 X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH NAD OR NUCLEOTIDE SUBSTRATE ANALOGS K12 X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH NAD AND A SUBSTRATE ANALOG INHIBITOR ACTIVITY REGULATION KINETIC PARAMETERS REACTION MECHANISM ACTIVE SITE SITE MUTAGENESIS OF HIS-159 AND LYS-163 K12 Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. Can use both NADH and NADPH as a reductant, with NADH being twice as effective as NADPH. (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NAD(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADH (S)-2,3,4,5-tetrahydrodipicolinate + H2O + NADP(+) = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H(+) + NADPH Is inhibited by 2,6-pyridine dicarboxylate (2,6-PDC or picolinate). 1.6 uM for NADH 8 uM for NADPH Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. Homotetramer. Cytoplasm Expression of dapB is up-regulated by ArgP and is repressed by lysine that prevents the binding of the ArgP activator. Thus, ArgP contributes to enhanced transcription of dapB when lysine becomes limiting. Belongs to the DapB family. Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction (PubMed:20503968). 3D-structure Amino-acid biosynthesis Complete proteome Cytoplasm Diaminopimelate biosynthesis Direct protein sequencing Lysine biosynthesis NAD NADP Oxidoreductase Reference proteome H A Q K A C Q MHDANIRVAIAGAGGRMGRQLIQAALALEGVQLGAALEREGSSLLGSDAGELAGAGKTGV TVQSSLDAVKDDFDVFIDFTRPEGTLNHLAFCRQHGKGMVIGTTGFDEAGKQAIRDAAAD IAIVFAANFSVGVNVMLKLLEKAAKVMGDYTDIEIIEAHHRHKVDAPSGTALAMGEAIAH ALDKDLKDCAVYSREGHTGERVPGTIGFATVRAGDIVGEHTAMFADIGERLEITHKASSR MTFANGAVRSALWLSGKESGLFDMRDVLDLNNL P39334 P76809 Q2M658 BDCR_ECOLI HTH-type transcriptional repressor BdcR bdcR yjgJ b4251 JW4208 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 SEQUENCE REVISION K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION AS A REGULATOR GENE NAME K12 / BW25113 Negatively regulates expression of bdcA. Complete proteome DNA-binding Reference proteome Repressor Transcription Transcription regulation MVTKKQSRVPGRPRRFAPEQAISAAKVLFHQKGFDAVSVAEVTDYLGINPPSLYAAFGSK AGLFSRVLNEYVGTEAIPLADILRDDRPVGECLVEVLKEAARRYSQNGGCAGCMVLEGIH SHDPQARDIAVQYYHAAETTIYDYIARRHPQRAQCVTDFMSTVMSGLSAKAREGHSIEQL CATAAMAGEAIKTILEE P69490 P33928 Q2MAP6 CCME_ECOLI Cytochrome c-type biogenesis protein CcmE Cytochrome c maturation protein E Heme chaperone CcmE ccmE yejS b2197 JW2185 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / BHB2600 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 PROTEIN SEQUENCE OF 131-140 HEME-BINDING CHARACTERIZATION GENE NAME INTERACTION WITH CCMC INTERACTION WITH CCMF HEME-BINDING MUTAGENESIS OF HIS-130 INTERACTION WITH CCMD STRUCTURE BY NMR OF 30-159 Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH. Forms a ternary complex with CcmC and CcmD. Interacts with CcmF. Shuttles between CcmC and CcmF for heme delivery. P0ABM1 ccmC false 7 Cell inner membrane Single-pass type II membrane protein Periplasmic side Stabilized by CcmD in the membrane. Belongs to the CcmE/CycJ family. 3D-structure Cell inner membrane Cell membrane Complete proteome Cytochrome c-type biogenesis Direct protein sequencing Heme Iron Membrane Metal-binding Reference proteome Signal-anchor Transmembrane Transmembrane helix H A H C MNIRRKNRLWIACAVLAGLALTIGLVLYALRSNIDLFYTPGEILYGKRETQQMPEVGQRL RVGGMVMPGSVQRDPNSLKVTFTIYDAEGSVDVSYEGILPDLFREGQGVVVQGELEKGNH ILAKEVLAKHDENYTPPEVEKAMEANHRRPASVYKDPAS P76205 P77764 ARPB_ECOLI Putative ankyrin repeat protein B arpB b4494 JW5278/JW1710 b1720/b1721 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Could be the product of a pseudogene, it is missing the C-terminus compared to orthologs. A full-length version has several ankyrin repeats (see for example AC A0A0H3JEK5). Complete proteome Reference proteome MSQNDIIIRTHYKSPHRLHIDSDIPTPSSEPINQFARQLITLLDTSDLSSMLSYCVTQEF TANCRKISQNCYSTALFTINFATSPIHTENILITLHYKKEIISLLLETTPIKANHLRSIL DYIEQEQLTAEDRNHCMKLSKKIHREKNYTPNSKSQW P0AFP2 P75707 P77119 Q2MBX2 ATL_ECOLI DNA base-flipping protein Alkyltransferase-like protein ATL atl ybaZ b0454 JW0444 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION DNA-BINDING MUTAGENESIS OF TRP-83 FUNCTION DNA-BINDING INTERACTION WITH HELD K12 FUNCTION DNA-BINDING INTERACTION WITH UVRA K12 / AB1157 FUNCTION Involved in DNA damage recognition. Binds DNA containing O(6)-methylguanine and larger O(6)-alkylguanine adducts, and to double-stranded DNA that contains an AP (apurinic/apyrimidinic) site (PubMed:16027108, PubMed:18084297, PubMed:19269902, PubMed:20921378). Binds to the damaged base and flips the base out of the DNA duplex into an extrahelical conformation, which allows processing by repair proteins (PubMed:18084297). Works in partnership with the nucleotide excision repair (NER) pathway to enhance the repair of the O(6)-alkylguanine adducts larger than the methyl adduct (PubMed:19269902, PubMed:20921378). Also prevents methyl-directed mismatch repair (MMR)-mediated attack of the O(6)-alkylguanine:T mispairs for the larger alkyl groups (PubMed:20921378). Interacts with HelD and UvrA. P0A698 uvrA false 2 Does not have alkyltransferase activity. A tryptophan residue replaces the cysteine at the known active site of MGMT. Belongs to the MGMT family. ATL subfamily. Complete proteome DNA damage DNA-binding Reference proteome W C MLVSCAMRLHSGVFPDYAEKLPQEEKMEKEDSFPQRVWQIVAAIPEGYVTTYGDVAKLAG SPRAARQVGGVLKRLPEGSTLPWHRVVNRHGTISLTGPDLQRQRQALLAEGVMVSGSGQI DLQRYRWNY P31551 P75623 CAID_ECOLI Carnitinyl-CoA dehydratase 4.2.1.149 Crotonobetainyl-CoA hydratase caiD yaaL b0036 JW0035 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] CHARACTERIZATION O44:K74 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] SEQUENCE REVISION TO 108 K12 / W3110 / ATCC 27325 / DSM 5911 PROTEIN SEQUENCE OF 2-11 FUNCTION CATALYTIC ACTIVITY BIOPHYSICOCHEMICAL PROPERTIES SUBUNIT O44:K74 Catalyzes the reversible dehydration of L-carnitinyl-CoA to crotonobetainyl-CoA. (R)-carnitinyl-CoA = crotonobetainyl-CoA + H2O 12 uM for crotonobetainyl-CoA 38 uM for crotonyl-CoA 186 umol/min/mg enzyme with crotonobetainyl-CoA as substrate 0.3 umol/min/mg enzyme with crotonyl-CoA as substrate Amine and polyamine metabolism; carnitine metabolism. Homotrimer. Belongs to the enoyl-CoA hydratase/isomerase family. Translation N-terminally shortened. Translation N-terminally shortened. Complete proteome Direct protein sequencing Lyase Reference proteome P L MSESLHLTRNGSILEITLDRPKANAIDAKTSFEMGEVFLNFRDDPQLRVAIITGAGEKFF SAGWDLKAAAEGEAPDADFGPGGFAGLTEIFNLDKPVIAAVNGYAFGGGFELALAADFIV CADNASFALPEAKLGIVPDSGGVLRLPKILPPAIVNEMVMTGRRMGAEEALRWGIVNRVV SQAELMDNARELAQQLVNSAPLAIAALKEIYRTTSEMPVEEAYRYIRSGVLKHYPSVLHS EDAIEGPLAFAEKRDPVWKGR P0ACJ8 P03020 Q2M723 CRP_ECOLI cAMP-activated global transcriptional regulator CRP Catabolite activator protein CAP Catabolite gene activator cAMP receptor protein CRP cAMP regulatory protein crp cap csm b3357 JW5702 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] CAMP-BINDING K12 NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 PROTEIN SEQUENCE OF 2-10 K12 DISRUPTION PHENOTYPE INDUCTION NEGATIVE AUTOREGULATION DNA-BINDING FUNCTION AS A TRANSCRIPTIONAL REPRESSOR AUTOREGULATION DNA-BINDING DNA-BINDING MUTAGENESIS OF SER-129; ARG-181 AND ARG-186 CAMP-BINDING MUTAGENESIS OF SER-63; ARG-83; SER-84; THR-128 AND SER-129 CAMP-BINDING INTERACTION WITH RNA POLYMERASE SUBUNIT MRE-600 FUNCTION AS AN ACTIVATOR FUNCTION AS A REPRESSOR PROBABLE INTERACTION WITH RPOA SUBUNIT INDUCTION POSITIVE AUTOREGULATION MUTAGENESIS OF ASP-139 FUNCTION CHARACTERIZATION OF ACTIVATING REGION 1 (AR1) DNA-BINDING MUTAGENESIS OF ALA-157; THR-159; HIS-160 AND GLY-163 FUNCTION CHARACTERIZATION OF ACTIVATING REGION 1 (AR1) DNA-BINDING MUTAGENESIS OF ALA-157; THR-159; HIS-160 AND GLY-163 K12 FUNCTION CHARACTERIZATION OF ACTIVATING REGION 2 (AR2) INTERACTION WITH RPOA DNA-BINDING DNA-BENDING MUTAGENESIS OF HIS-20; HIS-22; LYS-53; GLU-97; LYS-102; THR-159; HIS-160 AND GLY-163 IDENTIFICATION BY 2D-GEL FUNCTION CHARACTERIZATION OF ACTIVATING REGION 3 (AR3) MUTAGENESIS OF 54-ASP--GLU-56 AND GLU-59 FUNCTION CHARACTERIZATION OF ACTIVATING REGION 3 (AR3) PROBABLE INTERACTION WITH SIGMA-70 (RPOD) MUTAGENESIS OF GLU-59 MUTAGENESIS OF ASP-139 FUNCTION REGULON DISRUPTION PHENOTYPE MUTAGENESIS OF LYS-102 AND HIS-160 K12 / MG1655 / ATCC 47076 FUNCTION REGULON K12 / MG1655 / ATCC 47076 FUNCTION MUTAGENESIS OF 128-THR-SER-129 INDUCTION DISRUPTION PHENOTYPE K12 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-101 IDENTIFICATION BY MASS SPECTROMETRY K12 / JW1106 K12 / MG1655 / ATCC 47076 REVIEW REVIEW REVIEW REVIEW ON ROLE IN CARBON CATABOLITE REPRESSION AND OTHER PROCESSES X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH CAMP SUBUNIT DOMAIN X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH CAMP SUBUNIT DOMAIN X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 2-206 IN COMPLEX WITH CAMP AND DNA SUBUNIT DNA-BINDING DNA-BENDING X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-210 IN COMPLEX WITH CAMP AND DNA SUBUNIT DNA-BINDING DNA-BENDING X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH 2 CAMP PER MONOMER AND DNA SUBUNIT DNA-BINDING X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH CAMP SUBUNIT X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 2-210 IN COMPLEX WITH CAMP; DNA AND RNAP INTERACTION WITH RPOA DNA-BINDING SUBUNIT STRUCTURE BY NMR OF 2-210 OF APO-CRP ACTIVITY REGULATION SUBUNIT X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF APO-CRP ACTIVITY REGULATION SUBUNIT MUTAGENESIS OF ASP-139 STRUCTURE BY ELECTRON MICROSCOPY (19.80 ANGSTROMS) OF 2-210 IN COMPLEX WITH RPOA; RPOB; RPOC; RPOD; RPOZ AND DNA INTERACTION WITH ROPA DNA-BINDING SUBUNIT X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 2-210 IN COMPLEX WITH 2 CAMP PER MONOMER SUBUNIT STRUCTURE BY NMR OF 2-210 OF APO-CRP MUTAGENESIS OF 128-THR-SER-129 A global transcription regulator. Complexes with cyclic AMP (cAMP) which allosterically activates DNA binding (to consensus sequence 5'-AAATGTGATCTAGATCACATTT-3') to directly regulate the transcription of about 300 genes in about 200 operons and indirectly regulate the expression of about half the genome. There are 3 classes of CRP promoters; class I promoters have a single CRP-binding site upstream of the RNA polymerase (RNAP)-binding site, whereas in class II promoters the single CRP- and RNAP-binding site overlap, CRP making multiple contacts with RNAP. Class III promoters require multiple activator molecules, including at least one CRP dimer. It can act as an activator, repressor, coactivator or corepressor. Induces a severe bend in DNA (about 87 degrees), bringing upstream promoter elements into contact with RNAP. Acts as a negative regulator of its own synthesis as well as for adenylate cyclase (cyaA), which generates cAMP. High levels of active CRP are detrimental to growth (PubMed:16260780). Plays a major role in carbon catabolite repression (CCR). CCR involves cAMP, adenylate cyclase (cyaA), CRP and the EIIA-Glc component of the PTS (crr). In the presence of glucose EIIA-Glc is dephosphorylated, and does not activate adenylate cyclase, leading to reduced cAMP and thus decreased CRP activity. Also plays a role in many other processes (see PubMed:22573269). In the apo-form the DNA-binding helices form a rigid body in which their DNA recognitions helices are buried. cAMP binding causes a coil-to helix transition, stabilizing the active DNA binding conformation by reorienting and elongating these helices, which precludes a return to the inactive state. Homodimer, which upon binding cAMP is able to bind DNA. AR1 of the upstream subunit binds to the C-terminus of RNAP subunit RpoA, AR2 of the downstream subunit binds to the N-terminus of RpoA while AR3 binds to sigma-70 (RpoD). false 5 P0AFG0 nusG false 2 P23862 priC false 2 P0A7K2 rplL false 2 P0A8E5 yacL false 4 Constitutively expressed, levels decrease in stationary phase; more strongly induced in an rnlA deletion mutant, levels remain high even in stationary phase (at protein level). Both positively (PubMed:1328816) and negatively autoregulated (PubMed:6297782). The N-terminal domain binds cAMP and is responsible for homodimerization, while the C-terminal domain binds DNA when cAMP is bound. Not essential (on rich medium), greatly increased levels of cAMP. Eliminates the NaCl sensitivity of an rnlA deletion mutant. Binds 2 cAMP; cAMP 1 is in the anti conformation, while cAMP 2 is in the syn conformation. 3D-structure Acetylation Activator cAMP cAMP-binding Complete proteome Direct protein sequencing DNA-binding Nucleotide-binding Reference proteome Repressor Transcription Transcription regulation H A L Y H A L K N DEE AAA E A E G K S A R L S A K E A K E TS LI T A S A D L A D P T A I N S V H A K L N P Q R Y G A C D R S V R K R L R K R L T K MVLGKPQTDPTLEWFLSHCHIHKYPSKSTLIHQGEKAETLYYIVKGSVAVLIKDEEGKEM ILSYLNQGDFIGELGLFEEGQERSAWVRAKTACEVAEISYKKFRQLIQVNPDILMRLSAQ MARRLQVTSEKVGNLAFLDVTGRIAQTLLNLAKQPDAMTHPDGMQIKITRQEIGQIVGCS RETVGRILKMLEDQNLISAHGKTIVVYGTR P0AD99 P37011 P77112 P77492 Q2MC25 BRNQ_ECOLI Branched-chain amino acid transport system 2 carrier protein LIV-II brnQ b0401 JW0391 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-70 K12 IDENTIFICATION TOPOLOGY [LARGE SCALE ANALYSIS] K12 / MG1655 / ATCC 47076 Component of the LIV-II transport system for branched-chain amino acids. This LIV-II transport system may be H(+)-coupled. P08312 pheS false 5 Cell inner membrane Multi-pass membrane protein Belongs to the branched chain amino acid transporter family. Amino-acid transport Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix Transport MTHQLRSRDIIALGFMTFALFVGAGNIIFPPMVGLQAGEHVWTAAFGFLITAVGLPVLTV VALAKVGGGVDSLSTPIGKVAGVLLATVCYLAVGPLFATPRTATVSFEVGIAPLTGDSAL PLFIYSLVYFAIVILVSLYPGKLLDTVGNFLAPLKIIALVILSVAAIVWPAGSISTATEA YQNAAFSNGFVNGYLTMDTLGAMVFGIVIVNAARSRGVTEARLLTRYTVWAGLMAGVGLT LLYLALFRLGSDSASLVDQSANGAAILHAYVQHTFGGGGSFLLAALIFIACLVTAVGLTC ACAEFFAQYVPLSYRTLVFILGGFSMVVSNLGLSQLIQISVPVLTAIYPPCIALVVLSFT RSWWHNSSRVIAPPMFISLLFGILDGIKASAFSDILPSWAQRLPLAEQGLAWLMPTVVMV VLAIIWDRAAGRQVTSSAH P13518 Q2M8W2 CSRD_ECOLI RNase E specificity factor CsrD Regulator of CsrB and CsrC decay CsrD csrD yhdA b3252 JW3221 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 545-646 K12 FUNCTION IN REGULATION OF CARBON STORAGE REGULATION SYSTEM DISRUPTION PHENOTYPE K12 / MG1655 / CF7789 FUNCTION MUTAGENESIS OF LEU-584 DOMAIN EAL AND GGDEF DISRUPTION PHENOTYPE K12 / MG1655 / CF7789 FUNCTION IN CURLI EXPRESSION INDUCTION DISRUPTION PHENOTYPE K12 / W3110 / ATCC 27325 / DSM 5911 Serves as a specificity factor required for RNase E-mediated decay of the small global regulatory RNAs CsrB and CsrC, it is probably not a nuclease. Nor does its activity involve c-di-GMP, despite its domain composition. Positively modulates motility gene expression, is also required for curli expression. Cell membrane Multi-pass membrane protein Expressed at low levels at both 28 and 37 degrees Celsius. Removal of the transmembrane regions (residues 1-156) has no effect on csrB translation, however removal of either the HAMP-like region, EAL or GGDEF domains obviates the activity of CsrD. Dramatically stabilizes CsrB and CsrC RNAs, small RNAs that sequester the global carbon storage regulator CsrA; also decreased transcription of CsrB/C (PubMed:16980588). Decreased biofilm formation, decreased expression of DgcC, a probable diguanylate cyclase and of the curli regulator CsgD. Decreased expression of the curlin subunit CsgB, decreased curli expression at 28 degrees Celsius (PubMed:19332833). Although this protein contains both EAL and GGDEF domains it is unlikely to have either c-di-GMP phosphodiesterase or diguanylate cyclase activities as amino acids known to be important to these activities are not conserved. Cell membrane Coiled coil Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix L A MRLTTKFSAFVTLLTGLTIFVTLLGCSLSFYNAIQYKFSHRVQAVATAIDTHLVSNDFSV LRPQITELMMSADIVRVDLLHGDKQVYTLARNGSYRPVGSSDLFRELSVPLIKHPGMSLR LVYQDPMGNYFHSLMTTAPLTGAIGFIIVMLFLAVRWLQRQLAGQELLETRATRILNGER GSNVLGTIYEWPPRTSSALDTLLREIQNAREQHSRLDTLIRSYAAQDVKTGLNNRLFFDN QLATLLEDQEKVGTHGIVMMIRLPDFNMLSDTWGHSQVEEQFFTLTNLLSTFMMRYPGAL LARYHRSDFAALLPHRTLKEAESIAGQLIKAVDTLPNNKMLDRDDMIHIGICAWRSGQDT EQVMEHAESATRNAGLQGGNSWAIYDDSLPEKGRGNVRWRTLIEQMLSRGGPRLYQKPAV TREGQVHHRELMCRIFDGNEEVSSAEYMPMVLQFGLSEEYDRLQISRLIPLLRYWPEENL AIQVTVESLIRPRFQRWLRDTLMQCEKSQRKRIIIELAEADVGQHISRLQPVIRLVNALG VRVAVNQAGLTLVSTSWIKELNVELLKLHPGLVRNIEKRTENQLLVQSLVEACSGTSTQV YATGVRSRSEWQTLIQRGVTGGQGDFFASSQPLDTNVKKYSQRYSV P52086 P77109 COBC_ECOLI Adenosylcobalamin/alpha-ribazole phosphatase 3.1.3.73 Adenosylcobalamin phosphatase Alpha-ribazole-5'-phosphate phosphatase cobC phpB b0638 JW0633 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Catalyzes the conversion of adenosylcobalamin 5'-phosphate to adenosylcobalamin (vitamin B12); involved in the assembly of the nucleotide loop of cobalamin. Also catalyzes the hydrolysis of the phospho group from alpha-ribazole 5'-phosphate to form alpha-ribazole. adenosylcob(III)alamin 5'-phosphate + H2O = adenosylcob(III)alamin + phosphate alpha-ribazole 5'-phosphate + H2O = alpha-ribazole + phosphate Nucleoside biosynthesis; alpha-ribazole biosynthesis; alpha-ribazole from 5,6-dimethylbenzimidazole: step 2/2. Belongs to the phosphoglycerate mutase family. Translation N-terminally shortened. 3D-structure Cobalamin biosynthesis Complete proteome Hydrolase Reference proteome MRLWLIRHGETQANIDGLYSGHAPTPLTARGIEQAQNLHTLLHGVSFDLVLCSELERAQH TARLVLSDRQLPVQIIPELNEMFFGDWEMRHHRDLMQEDAENYSAWCNDWQHAIPTNGEG FQAFSQRVERFIARLSEFQHYQNILVVSHQGVLSLLIARLIGMPAEAMWHFRVDQGCWSA IDINQKFATLRVLNSRAIGVENA P0AA84 P75771 CLSB_ECOLI Cardiolipin synthase B CL synthase 2.7.8.- clsB ybhO b0789 JW0772 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION AS A CL SYNTHASE CATALYTIC ACTIVITY ACTIVITY REGULATION SUBCELLULAR LOCATION ATCC 33694 / HB101 FUNCTION DISRUPTION PHENOTYPE GENE NAME Catalyzes the phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol. Can also catalyze phosphatidyl group transfer to water to form phosphatidate. 2 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) = a cardiolipin + glycerol Activated by phosphate. Inhibited by cardiolipin and phosphatidate. Cell membrane Peripheral membrane protein Triple deletion of clsA, clsB and clsC results in a complete lack of cardiolipin, regardless of growth phase or growth conditions. All three cardiolipin synthases (ClsA, ClsB and ClsC) contribute to CL synthesis in stationary phase. Only ClsA contributes to synthesis during logarithmic growth phase. Belongs to the phospholipase D family. Cardiolipin synthase subfamily. ClsB sub-subfamily. Cell membrane Complete proteome Lipid biosynthesis Lipid metabolism Membrane Phospholipid biosynthesis Phospholipid metabolism Reference proteome Repeat Transferase MKCSWREGNKIQLLENGEQYYPAVFKAIGEAQERIILETFIWFEDDVGKQLHAALLAAAQ RGVKAEVLLDGYGSPDLSDEFVNELTAAGVVFRYYDPRPRLFGMRTNVFRRMHRKIVVID ARIAFIGGLNYSAEHMSSYGPEAKQDYAVRLEGPIVEDILQFELENLPGQSAARRWWRRH HKAEENRQPGEAQVLLVWRDNEEHRDDIERHYLKMLTQARREVIIANAYFFPGYRFLHAL RKAARRGVRIKLIIQGEPDMPIVRVGARLLYNYLVKGGVQVFEYRRRPLHGKVALMDDHW ATVGSSNLDPLSLSLNLEANVIIHDRHFNQTLRDNLNGIIAADCQQVDETMLPKRTWWNL TKSVLAFHFLRHFPALVGWLPAHTPRLAQVDPPAQPTMETQDRVETENTGVKP P06720 Q2M6I5 AGAL_ECOLI Alpha-galactosidase 3.2.1.22 Melibiase melA mel-7 b4119 JW4080 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52 PROTEIN SEQUENCE OF 1-20 COFACTOR SUBUNIT Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids. NAD(+) Binds 1 NAD(+) per subunit. Mn(2+) Binds 1 Mn(2+) ion per subunit. Homodimer. Belongs to the glycosyl hydrolase 4 family. Carbohydrate metabolism Complete proteome Direct protein sequencing Glycosidase Hydrolase Manganese Metal-binding NAD Reference proteome MMSAPKITFIGAGSTIFVKNILGDVFHREALKTAHIALMDIDPTRLEESHIVVRKLMDSA GASGKITCHTQQKEALEDADFVVVAFQIGGYEPCTVTDFEVCKRHGLEQTIADTLGPGGI MRALRTIPHLWQICEDMTEVCPDATMLNYVNPMAMNTWAMYARYPHIKQVGLCHSVQGTA EELARDLNIDPATLRYRCAGINHMAFYLELERKTADGSYVNLYPELLAAYEAGQAPKPNI HGNTRCQNIVRYEMFKKLGYFVTESSEHFAEYTPWFIKPGREDLIERYKVPLDEYPKRCV EQLANWHKELEEYKKASRIDIKPSREYASTIMNAIWTGEPSVIYGNVRNDGLIDNLPQGC CVEVACLVDANGIQPTKVGTLPSHLAALMQTNINVQTLLTEAILTENRDRVYHAAMMDPH TAAVLGIDEIYALVDDLIAAHGDWLPGWLHR P0AE82 P08336 Q2M8K8 CPXA_ECOLI Sensor histidine kinase CpxA 2.7.13.3 cpxA ecfB eup ssd b3911 JW3882 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] SUBCELLULAR LOCATION TOPOLOGY K12 NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 CHARACTERIZATION DISRUPTION PHENOTYPE K12 / AE2000 FUNCTION K12 FUNCTION ACTIVITY REGULATION DISRUPTION PHENOTYPE K12 / MC4100 ACTIVITY REGULATION FUNCTION AS A KINASE AND PHOSPHATASE CATALYTIC ACTIVITY COFACTOR DOMAIN PHOSPHORYLATION AT HIS-248 MUTAGENESIS OF ARG-33; 93-ARG--GLY-124 AND THR-252 K12 / MC4100 FUNCTION ACTIVITY REGULATION DISRUPTION PHENOTYPE K12 / MC4100 ACTIVITY REGULATION DISRUPTION PHENOTYPE K12 / MC4100 FUNCTION IN BIOFILM FORMATION DISRUPTION PHENOTYPE K12 / MC4100 / ATCC 35695 / DSM 6574 SUBCELLULAR LOCATION TOPOLOGY [LARGE SCALE ANALYSIS] K12 / MG1655 / ATCC 47076 FUNCTION ACTIVITY REGULATION PROBABLE SUBUNIT K12 / MC4100 FUNCTION ACTIVITY REGULATION ROLE IN HYDROXYUREA RESISTANCE DISRUPTION PHENOTYPE K12 / MC4100 / ATCC 35695 / DSM 6574 SUBUNIT K12 / MC4100 SUBUNIT FUNCTION ACTIVITY REGULATION INTERACTION WITH CPXP AND CPXR SUBCELLULAR LOCATION K12 / MG1655 / ATCC 47076 X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 188-457 IN COMPLEX WITH ADP; ATP AND ATP ANALOG FUNCTION SUBUNIT ACTIVE SITE REACTION MECHANISM DOMAIN PHOSPHORYLATION AT HIS-248 MUTAGENESIS OF SER-185; LEU-186; ALA-197; ASN-204; GLY-222; MET-228 AND ASN-356 Histidine kinase member of the two-component regulatory system CpxA/CpxR which responds to envelope stress response by activating expression of downstream genes including cpxP, degP, dsbA and ppiA (PubMed:7883164, PubMed:9401031, PubMed:9473036). Activates CpxR by phosphorylation; has autokinase, phosphotransferase and (in the presence of Mg(2+) and/or ATP or ADP) phosphatase activity (PubMed:9401031, PubMed:17259177, PubMed:24492262). The kinase activity is inhibited by periplasmic accessory protein CpxP; proteolysis of CpxP relieves inhibition (PubMed:16166523, PubMed:17259177, PubMed:25207645). Involved in several diverse cellular processes, including the functioning of acetohydroxyacid synthetase I, the biosynthesis of isoleucine and valine, the TraJ protein activation activity for tra gene expression in F plasmid (PubMed:8432716), and the synthesis, translocation, or stability of cell envelope proteins (PubMed:7883164). Activates transcription of periplasmic protease degP, probably by phosphorylating the cognate response protein CpxR; overexpression of an outer membrane lipoprotein NlpE also leads to transcription of degP via CpxRA (PubMed:7883164). Required for efficient binding of stationary phase cells to hydrophobic surfaces, part of the process of biofilm formation (PubMed:11830644). ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. Mg(2+) Phosphotransfer to CpxR is stimulated by Mg(2+) and/or Mn(2+). The two-component system is activated by envelope stress such as overexpression of some (misfolded) periplasmic proteins (PubMed:7883164, PubMed:9351822). Activated by spheroplasting (which removes the periplasm) in an autoregulatory cpxA-cpxR-dependent fashion (PubMed:10972835). Cpx two-component system is induced at pH 8.0; in a degP deletion mutant induction is halved (PubMed:9473036, PubMed:16166523). The kinase activity is inhibited by periplasmic accessory protein CpxP; proteolysis of CpxP relieves inhibition (PubMed:16166523, PubMed:17259177, PubMed:25207645). Autokinase activity reconstituted in liposomes is 50% inhibited by periplasmic accessory protein CpxP, but CpxP has no effect on phosphatase activity; autokinase stimulated by KCl, NH(4)Cl, RbCl, pH 7.5 and 8.0, inhibited by sensor kinase inhibitors tetrachlorosalicylanilid and ethodin (PubMed:17259177). The isolated cytoplasmic domain (residues 188-457) crystallizes as a homodimer, and forms dimers of dimers in solution which may be catalytically important (PubMed:24492262). Interacts with periplasmic accessory protein CpxP (PubMed:16166523, PubMed:21317318, PubMed:21239493, PubMed:25207645); interaction with CpxP is not seen in vivo when cells are grown in 0.3 M NaCl, or if the misfolded P pili protein PapE is overexpressed (PubMed:25207645). Interacts with cognate response regulator CpxR (PubMed:25207645). false 3 P0AE88 cpxR false 3 P76086 paaX false 3 Cell inner membrane Multi-pass membrane protein The periplasmic segment (residues 30-163) defines the sensory domain (PubMed:9401031). Conformational changes in the cytoplasmic HAMP domain modulate the mobility of the central alpha-helices (which bend at Ser-238 and Pro-253) that allows formation of 1 kinase-active state. Autophosphorylated (PubMed:9401031, PubMed:24492262). Maximal phosphorylation of the dimeric isolated cytoplasmic domain (residues 188-457) is about 70%, suggesting the protein may be hemiphosphorylated in vivo; probably occurs via a trans-autophosphorylation mechanism, i.e. one subunit phosphorylates the other (PubMed:24492262). Loss of the Cpx envelope stress response (PubMed:10972835). Decreased resistance to the antibiotic amnikacin (PubMed:2185221). Single cpxA and double cpxR-cpxA mutant decrease transcription of degP (PubMed:7883164). Decreased transcription of cpxP (PubMed:9473036). Hypersensitive to alkaline pH (greater than pH 8.8) (PubMed:9473036). Decreased numbers of stationary phase cells bind to hydrophobic surfaces (PubMed:11830644). Greatly increased resistance to hydroxyurea, probably due to decreased recognition of mis-folded proteins which eventually leads to decreased OH radical formation (PubMed:20005847). Translation N-terminally extended. 3D-structure ATP-binding Cell adhesion Cell inner membrane Cell membrane Complete proteome Kinase Membrane Nucleotide-binding Phosphoprotein Reference proteome Transferase Transmembrane Transmembrane helix Two-component regulatory system R C S R L Q A V N Y G D G R M V T P N Y W WW K R MIGSLTARIFAIFWLTLALVLMLVLMLPKLDSRQMTELLDSEQRQGLMIEQHVEAELAND PPNDLMWWRRLFRAIDKWAPPGQRLLLVTTEGRVIGAERSEMQIIRNFIGQADNADHPQK KKYGRVELVGPFSVRDGEDNYQLYLIRPASSSQSDFINLLFDRPLLLLIVTMLVSTPLLL WLAWSLAKPARKLKNAADEVAQGNLRQHPELEAGPQEFLAAGASFNQMVTALERMMTSQQ RLLSDISHELRTPLTRLQLGTALLRRRSGESKELERIETEAQRLDSMINDLLVMSRNQQK NALVSETIKANQLWSEVLDNAAFEAEQMGKSLTVNFPPGPWPLYGNPNALESALENIVRN ALRYSHTKIEVGFAVDKDGITITVDDDGPGVSPEDREQIFRPFYRTDEARDRESGGTGLG LAIVETAIQQHRGWVKAEDSPLGGLRLVIWLPLYKRS P77330 Q2MBM3 BORD_ECOLI Prophage lipoprotein Bor homolog Lipoprotein Bor homolog from lambdoid prophage DLP12 borD ybcU b0557 JW0546 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Cell membrane Lipid-anchor Encoded by the cryptic lambdoid prophage DLP12. Belongs to the lambda phage bor family. Cell membrane Complete proteome Lipoprotein Membrane Palmitate Reference proteome Signal MKKMLLATALALLITGCAQQTFTVQNKQTAVAPKETITHHFFVSGIGQKKTVDAAKICGG AENVVKTETQQTFVNGLLGFITLGIYTPLEARVYCSK P0C0V0 P09376 P15724 DEGP_ECOLI Periplasmic serine endoprotease DegP 3.4.21.107 Heat shock protein DegP Protease Do degP htrA ptd b0161 JW0157 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] INDUCTION K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50 K12 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16 PROTEIN SEQUENCE OF 27-39 FUNCTION AS A SERINE PROTEASE ACTIVITY REGULATION K12 PROTEIN SEQUENCE OF 27-30 K12 / W3110 / ATCC 27325 / DSM 5911 IDENTITY OF HTRA AND PROTEASE DO FUNCTION MUTAGENESIS OF HIS-131 AND SER-236 INDUCTION K12 / MC4100 BIOPHYSICOCHEMICAL PROPERTIES FUNCTION AS A SERINE PROTEASE CATALYTIC ACTIVITY SUBSTRATE SPECIFICITY SUBUNIT SUBCELLULAR LOCATION INDUCTION FUNCTION AS A CHAPERONE AND AS A SERINE PROTEASE SUBSTRATE SPECIFICITY DISULFIDE BOND K12 / W3110 / ATCC 27325 / DSM 5911 DISRUPTION PHENOTYPE K12 / MC4100 FUNCTION DISRUPTION PHENOTYPE K12 / MC4100 FUNCTION IN PREVENTION OF PROTEIN MISFOLDING SUBUNIT ROLE IN HYDROXYUREA RESISTANCE DISRUPTION PHENOTYPE K12 / MC4100 / ATCC 35695 / DSM 6574 MUTAGENESIS OF ILE-254; LEU-255; ASP-258; ASN-261; ILE-262 AND ILE-264 OLIGOMERIZATION SUBSTRATE SPECIFICITY SUBUNIT X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 27-474 OF MUTANT SER-236 SUBUNIT FUNCTION IN PREVENTION OF PROTEIN MISFOLDING MUTAGENESIS OF SER-236 STRUCTURE BY ELECTRON MICROSCOPY (28.0 ANGSTROMS) OF 27-474 OF MUTANT SER-236 IN COMPLEX WITH ANALOG SUBSTRATE FUNCTION AS A CHAPERONE AND AS A SERINE PROTEASE OLIGOMERIZATION SUBUNIT X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 27-474 IN COMPLEX WITH ANALOG SUBSTRATE OLIGOMERIZATION SUBUNIT ACTIVE SITE X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 27-474 IN COMPLEX WITH ANALOG SUBSTRATE OLIGOMERIZATION SUBUNIT DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures (PubMed:10319814). Degrades transiently denatured and unfolded or misfolded proteins which accumulate in the periplasm following heat shock or other stress conditions (PubMed:16303867). DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids (PubMed:8830688). Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins (PubMed:8830688). Its proteolytic activity is essential for the survival of cells at elevated temperatures (PubMed:7557477). It can degrade IciA, Ada, casein, globin and PapA. DegP shares specificity with DegQ (PubMed:8830688). DegP is also involved in the biogenesis of partially folded outer-membrane proteins (OMP). Acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-|-Val. Inhibited by diisopropylfluorophosphate (DFP). Optimum temperature is around 55 degrees Celsius. In the range from 37 to 55 degrees Celsius, the proteolytic activity rapidly increases with temperature. DegP can reversibly switch between different oligomeric forms that represent inactive (6-mer) and active (12-and 24-mer) protease states. Substrate binding triggers the conversion of the resting DegP trimer and hexamer into catalytically active 12- and 24-mers. The conversion of 6-mer (DegP6) into 12-mer (DegP12) or 24-mer (DegP24) is crucial in regulating protease activity. false 16 P02666 CSN2 true 8 P00698 LYZ true 11 P0A910 ompA false 8 P06996 ompC false 7 Cell inner membrane Peripheral membrane protein Cytoplasmic side By heat shock (PubMed:3057437). Transcriptionally up-regulated by sigma-E factor and the Cpx two-component signal transduction pathway (PubMed:7883164, PubMed:9351822). Decreased induction of Cpx two-component regulatory system (PubMed:16166523). Increased accumulation of periplasmic accessory protein CpxP, increased accumulation and toxicity of overexpressed, misfolded periplasmic proteins (PubMed:16303867). Increased resistance to hydroxyurea, probably due to decreased degradation of misfolded proteins which eventually leads to decreased OH radical formation (PubMed:20005847). DegP is indispensable for bacterial survival at temperatures above 42 degrees Celsius, however is also able to digest its natural substrates in a reducing environment at temperatures as low as 20 degrees Celsius. Belongs to the peptidase S1C family. 3D-structure Cell inner membrane Cell membrane Complete proteome Direct protein sequencing Disulfide bond Hydrolase Membrane Protease Reference proteome Repeat Serine protease Signal Stress response H R S A I N L N D V N I I N I N A R E Q A G STIYLLMQ RHLPVNAVISLNPFLKTGRGSPYNL MKKTTLALSALALSLGLALSPLSATAAETSSATTAQQMPSLAPMLEKVMPSVVSINVEGS TTVNTPRMPRNFQQFFGDDSPFCQEGSPFQSSPFCQGGQGGNGGGQQQKFMALGSGVIID ADKGYVVTNNHVVDNATVIKVQLSDGRKFDAKMVGKDPRSDIALIQIQNPKNLTAIKMAD SDALRVGDYTVAIGNPFGLGETVTSGIVSALGRSGLNAENYENFIQTDAAINRGNSGGAL VNLNGELIGINTAILAPDGGNIGIGFAIPSNMVKNLTSQMVEYGQVKRGELGIMGTELNS ELAKAMKVDAQRGAFVSQVLPNSSAAKAGIKAGDVITSLNGKPISSFAALRAQVGTMPVG SKLTLGLLRDGKQVNVNLELQQSSQNQVDSSSIFNGIEGAEMSNKGKDQGVVVNNVKTGT PAAQIGLKKGDVIIGANQQAVKNIAELRKVLDSKPSVLALNIQRGDSTIYLLMQ P0AEF8 P37316 Q2M7K5 DPPB_ECOLI Dipeptide transport system permease protein DppB dppB b3543 JW3512 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 / MM500 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 TOPOLOGY [LARGE SCALE ANALYSIS] K12 / MG1655 / ATCC 47076 Part of the binding-protein-dependent transport system for dipeptides; probably responsible for the translocation of the substrate across the membrane. Cell inner membrane Multi-pass membrane protein Belongs to the binding-protein-dependent transport system permease family. OppBC subfamily. Cell inner membrane Cell membrane Complete proteome Membrane Peptide transport Protein transport Reference proteome Transmembrane Transmembrane helix Transport MLQFILRRLGLVIPTFIGITLLTFAFVHMIPGDPVMIMAGERGISPERHAQLLAELGLDK PMWQQYLHYIWGVMHGDLGISMKSRIPVWEEFVPRFQATLELGVCAMIFATAVGIPVGVL AAVKRGSIFDHTAVGLALTGYSMPIFWWGMMLIMLVSVHWNLTPVSGRVSDMVFLDDSNP LTGFMLIDTAIWGEDGNFIDAVAHMILPAIVLGTIPLAVIVRMTRSSMLEVLGEDYIRTA RAKGLTRMRVIIVHALRNAMLPVVTVIGLQVGTLLAGAILTETIFSWPGLGRWLIDALQR RDYPVVQGGVLLVATMIILVNLLVDLLYGVVNPRIRHKK P0AE06 P31223 Q2MBW4 ACRA_ECOLI Multidrug efflux pump subunit AcrA AcrAB-TolC multidrug efflux pump subunit AcrA Acridine resistance protein A acrA lir mtcA b0463 JW0452 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 / W4573 NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 CHARACTERIZATION FUNCTION IN EFFLUX SUBUNIT PALMITOYLATION AT CYS-25 DISRUPTION PHENOTYPE PROTEOLYTIC PROCESSING INTERACTION WITH ACRB INTERACTION WITH ACRB AND TOLC SUBUNIT SUBCELLULAR LOCATION K12 / MC1061 / ATCC 53338 / DSM 7140 HOMOTRIMERIZATION SUBCELLULAR LOCATION BL21-DE3 SUBUNIT K12 / MG1655 / ATCC 47076 X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF 45-312 MUTAGENESIS OF 223-MET-MET-224 AND 287-LEU-LEU-288 K12 / JM101 / ATCC 33876 / DSM 3948 / NCIMB 11926 AcrA-AcrB-AcrZ-TolC is a drug efflux protein complex with broad substrate specificity that uses the proton motive force to export substrates. This subunit may act as an adapter protein that links AcrB and TolC stably together. It is elongated in shape, being long enough to span the periplasm. Monomeric in solution. Homotrimeric; interacts indpendently with AcrB and TolC as well as AcrZ. Part of the AcrA-AcrB-TolC efflux pump. Complex assembly is independent of an efflux substrate and appears to be constitutive. false 6 P02930 tolC false 2 Cell inner membrane Lipid-anchor An unlipidated version of this protein (directed to the periplasm by the OmpA signal sequence) functions normally. Cannot grow on efflux substrates novobiocin or fusidic acid. Belongs to the membrane fusion protein (MFP) (TC 8.A.1) family. 3D-structure Antibiotic resistance Cell inner membrane Cell membrane Coiled coil Complete proteome Lipoprotein Membrane Palmitate Reference proteome Signal Transport MNKNRGFTPLAVVLMLSGSLALTGC MKKTAIAIAVALAGFATVAQA FL MM LL MM MNKNRGFTPLAVVLMLSGSLALTGCDDKQAQQGGQQMPAVGVVTVKTEPLQITTELPGRT SAYRIAEVRPQVSGIILKRNFKEGSDIEAGVSLYQIDPATYQATYDSAKGDLAKAQAAAN IAQLTVNRYQKLLGTQYISKQEYDQALADAQQANAAVTAAKAAVETARINLAYTKVTSPI SGRIGKSNVTEGALVQNGQATALATVQQLDPIYVDVTQSSNDFLRLKQELANGTLKQENG KAKVSLITSDGIKFPQDGTLEFSDVTVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEEG LNPNAILVPQQGVTRTPRGDATVLVVGADDKVETRPIVASQAIGDKWLVTEGLKAGDRVV ISGLQKVRPGVQVKAQEVTADNNQQAASGAQPEQSKS P0A6E9 P77201 Q8X788 BIOD2_ECOLI ATP-dependent dethiobiotin synthetase BioD 2 6.3.3.3 DTB synthetase 2 DTBS 2 Dethiobiotin synthase 2 bioD2 ynfK b1593 JW5264 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA) to form an ureido ring. 7,8-diaminononanoate + ATP + CO2 = ADP + dethiobiotin + 3 H(+) + phosphate Mg(2+) Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2. Homodimer. Cytoplasm Belongs to the dethiobiotin synthetase family. ATP-binding Biotin biosynthesis Complete proteome Cytoplasm Ligase Magnesium Metal-binding Nucleotide-binding Reference proteome MLKRFFITGTDTSVGKTVVSRALLQALASQGKTVAGYKPVAKGSKETPEGLRNKDALVLQ SVSTIELPYEAVNPIALSEEESSVAHSCPINYTLISNGLANLTEKVDHVVVEGTGGWRSL MNDLRPLSEWVVQEQLPVLMVVGIQEGCINHALLTAQAIANDGLPLIGWVANRINPGLAH YAEIIDVLGKKLPAPLIGELPYLPRAEQRELGQYIRLAMLRSVLAVDRVTV P0AE52 P23480 BCP_ECOLI Peroxiredoxin Bcp 1.11.1.15 Bacterioferritin comigratory protein Thioredoxin peroxidase bcp b2480 JW2465 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32 K12 PROTEIN SEQUENCE OF 1-15 K12 / EMG2 PROTEIN SEQUENCE OF 1-11 K12 / W3110 / ATCC 27325 / DSM 5911 ACTIVE SITE ACTIVE SITE DISULFIDE BOND FUNCTION CATALYTIC ACTIVITY BIOPHYSICOCHEMICAL PROPERTIES SUBUNIT Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. [protein]-dithiol + a hydroperoxide = [protein]-disulfide + an alcohol + H2O 76.1 uM for H(2)O(2) (using glutathione Grx1 as electron donor) 99.5 uM for cumene hydroperoxide (using glutathione Grx1 as electron donor) 6800 uM for tert-butyl hydroperoxide (using glutathione Grx1 as electron donor) 14.6 uM for H(2)O(2) (using thioredoxin Trx1 as electron donor) 21.6 uM for cumene hydroperoxide (using thioredoxin Trx1 as electron donor) 574 uM for tert-butyl hydroperoxide (using thioredoxin Trx1 as electron donor) Monomer. The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this atypical 2-Cys peroxiredoxin, C(R) is present in the same subunit to form an intramolecular disulfide. The disulfide is subsequently reduced by thioredoxin. Belongs to the peroxiredoxin family. BCP/PrxQ subfamily. Antioxidant Complete proteome Direct protein sequencing Disulfide bond Oxidoreductase Peroxidase Redox-active center Reference proteome MNPLKAGDIAPKFSLPDQDGEQVNLTDFQGQRVLVYFYPKAMTPGCTVQACGLRDNMDEL KKAGVDVLGISTDKPEKLSRFAEKELLNFTLLSDEDHQVCEQFGVWGEKSFMGKTYDGIH RISFLIDADGKIEHVFDDFKTSNHHDVVLNWLKEHA P28246 Q2MAQ9 BCR_ECOLI Bicyclomycin resistance protein Sulfonamide resistance protein bcr bicA bicR sur suxA b2182 JW5363 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 60-396 K12 / C600 / ATCC 23724 / DSM 3925 / LMG 3041 / NCIB 10222 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / BHB2600 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION SUBCELLULAR LOCATION TOPOLOGY [LARGE SCALE ANALYSIS] K12 / MG1655 / ATCC 47076 FUNCTION K12 / JM101 / ATCC 33876 / DSM 3948 / NCIMB 11926 Involved in sulfonamide (sulfathiazole) and bicyclomycin resistance (PubMed:2694948). Probable membrane translocase. A transporter able to export peptides. When overexpressed, allows cells deleted for multiple peptidases (pepA, pepB, pepD and pepN) to grow in the presence of dipeptides Ala-Gln or Gly-Tyr which otherwise inhibit growth (PubMed:20067529). Cells overexpressing this protein have decreased intracellular levels of Ala-Gln dipeptide, and in a system that produces the Ala-Gln dipeptide overproduction of this protein increases export of the dipeptide (PubMed:20067529). Cell inner membrane Multi-pass membrane protein Belongs to the major facilitator superfamily. Bcr/CmlA family. Translation N-terminally extended. Translation N-terminally extended. Antibiotic resistance Cell inner membrane Cell membrane Complete proteome Membrane Peptide transport Protein transport Reference proteome Transmembrane Transmembrane helix Transport D V V I MTTRQHSSFAIVFILGLLAMLMPLSIDMYLPALPVISAQFGVPAGSTQMTLSTYILGFAL GQLIYGPMADSFGRKPVVLGGTLVFAAAAVACALANTIDQLIVMRFFHGLAAAAASVVIN ALMRDIYPKEEFSRMMSFVMLVTTIAPLMAPIVGGWVLVWLSWHYIFWILALAAILASAM IFFLIKETLPPERRQPFHIRTTIGNFAALFRHKRVLSYMLASGFSFAGMFSFLSAGPFVY IEINHVAPENFGYYFALNIVFLFVMTIFNSRFVRRIGALNMFRSGLWIQFIMAAWMVISA LLGLGFWSLVVGVAAFVGCVSMVSSNAMAVILDEFPHMAGTASSLAGTFRFGIGAIVGAL LSLATFNSAWPMIWSIAFCATSSILFCLYASRPKKR P76459 P94762 ATOA_ECOLI Acetate CoA-transferase subunit beta 2.8.3.8 Acetyl-CoA:acetoacetate CoA-transferase subunit beta atoA b2222 JW2216 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 acetate + an acyl-CoA = a fatty acid + acetyl-CoA Lipid metabolism; short-chain fatty acid metabolism. Heterodimer. P0AC02 bamD false 2 Belongs to the 3-oxoacid CoA-transferase subunit B family. 3D-structure Complete proteome Fatty acid metabolism Lipid metabolism Reference proteome Transferase MDAKQRIARRVAQELRDGDIVNLGIGLPTMVANYLPEGIHITLQSENGFLGLGPVTTAHP DLVNAGGQPCGVLPGAAMFDSAMSFALIRGGHIDACVLGGLQVDEEANLANWVVPGKMVP GMGGAMDLVTGSRKVIIAMEHCAKDGSAKILRRCTMPLTAQHAVHMLVTELAVFRFIDGK MWLTEIADGCDLATVRAKTEARFEVAADLNTQRGDL P0AAF3 P08531 ARAG_ECOLI Arabinose import ATP-binding protein AraG 7.5.2.12 araG b1900 JW1888 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] BEK 180 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION IN ARABINOSE TRANSPORT SUBCELLULAR LOCATION K12 FUNCTION IN ARABINOSE TRANSPORT BEK 180 INDUCTION Part of the ABC transporter complex AraFGH involved in arabinose import. Responsible for energy coupling to the transport system (Probable). ATP + H2O + L-arabinose(out) = ADP + H(+) + L-arabinose(in) + phosphate The complex is composed of two ATP-binding proteins (AraG), two transmembrane proteins (AraH) and a solute-binding protein (AraF). P28635 metQ false 3 Cell inner membrane Peripheral membrane protein Induced by arabinose. Transcription is dependent on the transcription factor AraC, the cAMP receptor protein (CRP) and cAMP. Belongs to the ABC transporter superfamily. Arabinose importer (TC 3.A.1.2.2) family. ATP-binding Cell inner membrane Cell membrane Complete proteome Membrane Nucleotide-binding Reference proteome Repeat Sugar transport Translocase Transport MQQSTPYLSFRGIGKTFPGVKALTDISFDCYAGQVHALMGENGAGKSTLLKILSGNYAPT TGSVVINGQEMSFSDTTAALNAGVAIIYQELHLVPEMTVAENIYLGQLPHKGGIVNRSLL NYEAGLQLKHLGMDIDPDTPLKYLSIGQWQMVEIAKALARNAKIIAFDEPTSSLSAREID NLFRVIRELRKEGRVILYVSHRMEEIFALSDAITVFKDGRYVKTFTDMQQVDHDALVQAM VGRDIGDIYGWQPRSYGEERLRLDAVKAPGVRTPISLAVRSGEIVGLFGLVGAGRSELMK GMFGGTQITAGQVYIDQQPIDIRKPSHAIAAGMMLCPEDRKAEGIIPVHSVRDNINISAR RKHVLGGCVINNGWEENNADHHIRSLNIKTPGAEQLIMNLSGGNQQKAILGRWLSEEMKV ILLDEPTRGIDVGAKHEIYNVIYALAAQGVAVLFASSDLPEVLGVADRIVVMREGEIAGE LLHEQADERQALSLAMPKVSQAVA P76473 Q2MAN2 ARNT_ECOLI Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase 2.4.2.43 4-amino-4-deoxy-L-arabinose lipid A transferase Lipid IV(A) 4-amino-4-deoxy-L-arabinosyltransferase Polymyxin resistance protein PmrK Undecaprenyl phosphate-alpha-L-Ara4N transferase arnT pmrK yfbI b2257 JW2251 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 CATALYTIC ACTIVITY FUNCTION K12 / W3110 / ATCC 27325 / DSM 5911 SUBCELLULAR LOCATION Catalyzes the transfer of the L-Ara4N moiety of the glycolipid undecaprenyl phosphate-alpha-L-Ara4N to lipid A. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. 4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + lipid IV(A) = lipid II(A) + di-trans,octa-cis-undecaprenyl phosphate. Lipopolysaccharide metabolism; 4-amino-4-deoxy-beta-L-arabinose-lipid A biosynthesis. Cell inner membrane Multi-pass membrane protein Induced by BasR. Belongs to the glycosyltransferase 83 family. Cell inner membrane Cell membrane Complete proteome Glycosyltransferase Lipid A biosynthesis Lipid biosynthesis Lipid metabolism Lipopolysaccharide biosynthesis Membrane Reference proteome Transferase Transmembrane Transmembrane helix MKSVRYLIGLFAFIACYYLLPISTRLLWQPDETRYAEISREMLASGDWIVPHLLGLRYFE KPIAGYWINSIGQWLFGANNFGVRAGVIFATLLTAALVTWFTLRLWRDKRLALLATVIYL SLFIVYAIGTYAVLDPFIAFWLVAGMCSFWLAMQAQTWKGKSAGFLLLGITCGMGVMTKG FLALAVPVLSVLPWVATQKRWKDLFIYGWLAVISCVLTVLPWGLAIAQREPNFWHYFFWV EHIQRFALDDAQHRAPFWYYVPVIIAGSLPWLGLLPGALYTGWKNRKHSATVYLLSWTIM PLLFFSVAKGKLPTYILSCFASLAMLMAHYALLAAKNNPLALRINGWINIAFGVTGIIAT FVVSPWGPMNTPVWQTFESYKVFCAWSIFSLWAFFGWYTLTNVEKTWPFAALCPLGLALL VGFSIPDRVMEGKHPQFFVEMTQESLQPSRYILTDSVGVAAGLAWSLQRDDIIMYRQTGE LKYGLNYPDAKGRFVSGDEFANWLNQHRQEGIITLVLSVDRDEDINSLAIPPADAIDRQE RLVLIQYRPK P00963 Q2M862 ASNA_ECOLI Aspartate--ammonia ligase 6.3.1.1 Asparagine synthetase A asnA b3744 JW3722 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-252 PROTEIN SEQUENCE OF 1-5 K12 FUNCTION IN PRODUCTION OF EXTRACELLULAR DEATH FACTOR (EDF) DISRUPTION PHENOTYPE X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) K12 May amidate Asp of the extracellular death factor precursor Asn-Asn-Trp-Asp-Asn to generate Asn-Asn-Trp-Asn-Asn. ATP + L-aspartate + NH4(+) = AMP + diphosphate + H(+) + L-asparagine Amino-acid biosynthesis; L-asparagine biosynthesis; L-asparagine from L-aspartate (ammonia route): step 1/1. Homodimer. false 2 Cytoplasm Loss of production of extracellular death factor. Belongs to the class-II aminoacyl-tRNA synthetase family. AsnA subfamily. 3D-structure Amino-acid biosynthesis Asparagine biosynthesis ATP-binding Complete proteome Cytoplasm Direct protein sequencing Ligase Nucleotide-binding Reference proteome MKTAYIAKQRQISFVKSHFSRQLEERLGLIEVQAPILSRVGDGTQDNLSGCEKAVQVKVK ALPDAQFEVVHSLAKWKRQTLGQHDFSAGEGLYTHMKALRPDEDRLSPLHSVYVDQWDWE RVMGDGERQFSTLKSTVEAIWAGIKATEAAVSEEFGLAPFLPDQIHFVHSQELLSRYPDL DAKGRERAIAKDLGAVFLVGIGGKLSDGHRHDVRAPDYDDWSTPSELGHAGLNGDILVWN PVLEDAFELSSMGIRVDADTLKHQLALTGDEDRLELEWHQALLRGEMPQTIGGGIGQSRL TMLLLQLPHIGQVQCGVWPAAVRESVPSLL P0A9H5 P13040 BTUR_ECOLI Corrinoid adenosyltransferase 2.5.1.17 Cob(II)alamin adenosyltransferase Cob(II)yrinic acid a,c-diamide adenosyltransferase Cobinamide/cobalamin adenosyltransferase btuR cobA b1270 JW1262 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Required for both de novo synthesis of the corrin ring for the assimilation of exogenous corrinoids. Participates in the adenosylation of a variety of incomplete and complete corrinoids (By similarity). 2 ATP + 2 cob(II)yrinate a,c diamide + reduced [electron-transfer flavoprotein] = 2 adenosylcob(III)yrinate a,c-diamide + 3 H(+) + oxidized [electron-transfer flavoprotein] + 2 triphosphate 2 ATP + 2 cob(II)alamin + reduced [electron-transfer flavoprotein] = 2 adenosylcob(III)alamin + 3 H(+) + oxidized [electron-transfer flavoprotein] + 2 triphosphate Cofactor biosynthesis; adenosylcobalamin biosynthesis; adenosylcobalamin from cob(II)yrinate a,c-diamide: step 2/7. Cytoplasm Belongs to the Cob(I)alamin adenosyltransferase family. ATP-binding Cobalamin biosynthesis Complete proteome Cytoplasm Nucleotide-binding Porphyrin biosynthesis Reference proteome Transferase MSDERYQQRQQRVKEKVDARVAQAQDERGIIIVFTGNGKGKTTAAFGTATRAVGHGKKVG VVQFIKGTWPNGERNLLEPHGVEFQVMATGFTWDTQNRESDTAACREVWQHAKRMLADSS LDMVLLDELTYMVAYDYLPLEEVVQALNERPHQQTVIITGRGCHRDILELADTVSELRPV KHAFDAGVKAQIGIDY P60061 P39268 P39269 Q2M6I9 ADIC_ECOLI Arginine/agmatine antiporter adiC aniC yjdD yjdE b4115 JW4076 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] SEQUENCE REVISION K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION INDUCTION K12 FUNCTION K12 / MG1655 / ATCC 47076 TOPOLOGY [LARGE SCALE ANALYSIS] K12 / MG1655 / ATCC 47076 Major component of the acid-resistance (AR) system allowing enteric pathogens to survive the acidic environment in the stomach (By similarity). Exchanges extracellular arginine for its intracellular decarboxylation product agmatine (Agm) thereby expelling intracellular protons. Cell inner membrane Multi-pass membrane protein By acidic conditions. Belongs to the amino acid-polyamine-organocation (APC) superfamily. Basic amino acid/polyamine antiporter (APA) (TC 2.A.3.2) family. 3D-structure Amino-acid transport Antiport Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix Transport MSSDADAHKVGLIPVTLMVSGNIMGSGVFLLPANLASTGGIAIYGWLVTIIGALGLSMVY AKMSFLDPSPGGSYAYARRCFGPFLGYQTNVLYWLACWIGNIAMVVIGVGYLSYFFPILK DPLVLTITCVVVLWIFVLLNIVGPKMITRVQAVATVLALIPIVGIAVFGWFWFRGETYMA AWNVSGLGTFGAIQSTLNVTLWSFIGVESASVAAGVVKNPKRNVPIATIGGVLIAAVCYV LSTTAIMGMIPNAALRVSASPFGDAARMALGDTAGAIVSFCAAAGCLGSLGGWTLLAGQT AKAAADDGLFPPIFARVNKAGTPVAGLIIVGILMTIFQLSSISPNATKEFGLVSSVSVIF TLVPYLYTCAALLLLGHGHFGKARPAYLAVTTIAFLYCIWAVVGSGAKEVMWSFVTLMVI TAMYALNYNRLHKNPYPLDAPISKD P22333 P78163 P78240 ADD_ECOLI Adenosine deaminase 3.5.4.4 Adenosine aminohydrolase add b1623 JW1615 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 adenosine + H(+) + H2O = inosine + NH4(+) Zn(2+) Binds 1 zinc ion per subunit. Belongs to the metallo-dependent hydrolases superfamily. Adenosine and AMP deaminases family. Adenosine deaminase subfamily. Complete proteome Hydrolase Metal-binding Nucleotide metabolism Reference proteome Zinc MIDTTLPLTDIHRHLDGNIRPQTILELGRQYNISLPAQSLETLIPHVQVIANEPDLVSFL TKLDWGVKVLASLDACRRVAFENIEDAARHGLHYVELRFSPGYMAMAHQLPVAGVVEAVI DGVREGCRTFGVQAKLIGIMSRTFGEAACQQELEAFLAHRDQITALDLAGDELGFPGSLF LSHFNRARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAIEDRALMDFLAEQQI GIESCLTSNIQTSTVAELAAHPLKTFLEHGIRASINTDDPGVQGVDIIHEYTVAAPAAGL SREQIRQAQINGLEMAFLSAEEKRALREKVAAK P0AGF2 Q2MA23 Q46926 CSDE_ECOLI Sulfur acceptor protein CsdE csdE ygdK b2811 JW2782 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION GENE NAME INTERACTION WITH CSDA SUBUNIT SULFHYDRATION AT CYS-61 MUTAGENESIS OF CYS-61 K12 / MG1655 / ATCC 47076 FUNCTION INTERACTION WITH CSDA AND TCDA DISRUPTION PHENOTYPE K12 / MG1655 / ATCC 47076 FUNCTION ROLE IN CT(6)A37 FORMATION DISRUPTION PHENOTYPE STRUCTURE BY NMR Stimulates the cysteine desulfurase activity of CsdA. Contains a cysteine residue (Cys-61) that acts to accept sulfur liberated via the desulfurase activity of CsdA. May be able to transfer sulfur to TcdA/CsdL. Seems to support the function of TcdA in the generation of cyclic threonylcarbamoyladenosine at position 37 (ct(6)A37) in tRNAs that read codons beginning with adenine. Does not appear to participate in Fe/S biogenesis. Homodimer. Forms a heterodimer with CsdA. Interacts with CsdA and with TcdA/CsdL. Q46925 csdA false 8 Q46927 tcdA false 3 Cells lacking this gene display a high decrease in the level of ct(6)A modification in tRNAs, and show the t(6)A modification instead. They also show no defects in motility, fitness or antibiotic sensitivity, in contrast to csdA mutants. Belongs to the SufE family. 3D-structure Complete proteome Reference proteome C S MTNPQFAGHPFGTTVTAETLRNTFAPLTQWEDKYRQLIMLGKQLPALPDELKAQAKEIAG CENRVWLGYTVAENGKMHFFGDSEGRIVRGLLAVLLTAVEGKTAAELQAQSPLALFDELG LRAQLSASRSQGLNALSEAIIAATKQV P0AEM4 P43532 FLGM_ECOLI Negative regulator of flagellin synthesis Anti-sigma-28 factor flgM b1071 JW1058 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 STRUCTURE BY NMR Responsible for the coupling of flagellin expression to flagellar assembly by preventing expression of the flagellin genes when a component of the middle class of proteins is defective. It negatively regulates flagellar genes by inhibiting the activity of FliA by directly binding to FliA. P0AEM6 fliA false 4 Belongs to the FlgM family. Bacterial flagellum biogenesis Complete proteome Reference proteome Repressor Transcription Transcription regulation MSIDRTSPLKPVSTVQPRETTDAPVTNSRAAKTTASTSTSVTLSDAQAKLMQPGSSDINL ERVEALKLAIRNGELKMDTGKIADALINEAQQDLQSN P77694 Q2MCD2 ECPD_ECOLI Fimbria adhesin EcpD ecpD matE yagW b0290 JW0284 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 EXPRESSION K12 Part of the ecpRABCDE operon, which encodes the E.coli common pilus (ECP). ECP is found in both commensal and pathogenic strains and plays a dual role in early-stage biofilm development and host cell recognition. Tip pilus adhesin, which is required for assembly of EcpA into fibers (By similarity). Forms polymers. Interacts with EcpA. Fimbrium Negatively regulated by H-NS. Positively regulated by IHF and EcpR (By similarity). Not expressed under classical laboratory conditions, but is functional when constitutively expressed. Belongs to the EcpD/MatE family. Complete proteome Fimbrium Reference proteome Signal MRVNLLITMIIFALIWPVTALRAAVSKTTWADAPAREFVFVENNSDDNFFVTPGGALDPR LTGANRWTGLKYTGSGTIYQQSLGYIDNGYNTGLYTNWKFDMWLENSPVSSPLTGLRCIN WYAGCNMTTSLILPQTTDASGFYGATVTSGGAKWMHGMLSDAFYQYMQQMPVGSSFTMTI NACQTSVNYDASSGARCKDQASGNWYVRNVTHTKAANLRLINTHSLAEVFINSDGVPTLG EGNADCRTQTIGSRSGLSCKMVNYTLQTNGLSNTSIHIFPAIANSSLASAVGAYDMQFSL NGSSWKPVSNTAYYYTFNEMKSADSIYVFFSSNFFKQMVNLGISDINTKDLFNFRFQNTT SPESGWYEFSTSNTLIIKPRDFSISIISDEYTQTPSREGYVGSGESALDFGYIVTTSGKT AADEVLIKVTGPAQVIGGRSYCVFSSDDGKAKVPFPATLSFITRNGATKTYDAGCDDSWR DMTDALWLTTPWTDISGEVGQMDKTTVKFSIPMDNAISLRTVDDNGWFGEVSASGEIHVQ ATWRNIN P77395 Q2MBT5 CNOX_ECOLI Chaperedoxin Heat shock protein CnoX Trxsc cnoX ybbN b0492 JW5067 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION SUBUNIT IDENTIFICATION BY MASS SPECTROMETRY FUNCTION INTERACTION WITH DNAK AND GROEL DISRUPTION PHENOTYPE DISRUPTION PHENOTYPE FUNCTION ACTIVITY REGULATION DISRUPTION PHENOTYPE MUTAGENESIS OF CYS-38 AND CYS-63 X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) FUNCTION SUBUNIT DOMAIN Chaperedoxin that combines a chaperone activity with a redox-protective function (PubMed:16563353, PubMed:18657513, PubMed:29754824). Involved in the protection against hypochlorous acid (HOCl), the active ingredient of bleach, which kills bacteria by causing protein aggregation (PubMed:29754824). Functions as an efficient holdase chaperone that protects the substrates of the major folding systems GroEL/GroES and DnaK/DnaJ/GrpE from aggregation. In addition, it prevents the irreversible oxidation of its substrates through the formation of mixed disulfide complexes (PubMed:29754824). After bleach stress, it transfers its substrates to the GroEL/GroES and DnaK/DnaJ/GrpE foldases (PubMed:29754824). Lacks oxidoreductase activity (PubMed:21498507, PubMed:29754824). The holdase activity is activated by HOCl, via the reversible chlorination of several residues in the TPR domain. Chorination probably increases the hydrophobicity of CnoX and enables it to bind a variety of substrates. Reduced glutathione (GSH) is required to resolve CnoX-substrate complexes. Interacts with a variety of proteins, including multiple ribosomal protein subunits, DnaK and GroEL (PubMed:18657513, PubMed:21498507). The reduced protein is monomeric in solution (PubMed:21498507). Upon oxidation, its oligomeric state changes to tetramers and higher oligomers (PubMed:16563353). P0A988 dnaN false 2 Contains an N-terminal mobile Trx domain and four atypical tetratricopeptide repeat (TPR) motifs in the C-terminal region. The Trx domain lacks the canonical Cys-x-x-Cys active site of thioredoxins and is not a functional oxidoreductase. Mutant is highly sensitive to HOCl (PubMed:29754824). Disruption mutant displays increased sensitivity to heat stress, but not to oxidative, UV, osmotic and pH stresses. Mutation does not affect the redox state of cytoplasmic, membrane and periplasmic proteins, but mutant shows a decreased expression of several cytoplasmic proteins (PubMed:18657513). Mutant displays overinitiation, hypermutator and filamentation phenotypes with the occurrence of anucleated cells (PubMed:21195694). Translation N-terminally shortened. 3D-structure Chaperone Complete proteome Disulfide bond Reference proteome Stress response C A C A MSVENIVNINESNLQQVLEQSMTTPVLFYFWSERSQHCLQLTPILESLAAQYNGQFILAK LDCDAEQMIAAQFGLRAIPTVYLFQNGQPVDGFQGPQPEEAIRALLDKVLPREEELKAQQ AMQLMQESNYTDALPLLKDAWQLSNQNGEIGLLLAETLIALNRSEDAEAVLKTIPLQDQD TRYQGLVAQIELLKQAADTPEIQQLQQQVAENPEDAALATQLALQLHQVGRNEEALELLF GHLRKDLTAADGQTRKTFQEILAALGTGDALASKYRRQLYALLY P0A6S3 P75941 FLGI_ECOLI Flagellar P-ring protein Basal body P-ring protein flgI fla FIX flaM b1080 JW1067 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. The basal body constitutes a major portion of the flagellar organelle and consists of four rings (L,P,S, and M) mounted on a central rod. Periplasm Bacterial flagellum basal body Belongs to the FlgI family. Bacterial flagellum Complete proteome Periplasm Reference proteome Signal MIKFLSALILLLVTTAAQAERIRDLTSVQGVRQNSLIGYGLVVGLDGTGDQTTQTPFTTQ TLNNMLSQLGITVPTGTNMQLKNVAAVMVTASLPPFGRQGQTIDVVVSSMGNAKSLRGGT LLMTPLKGVDSQVYALAQGNILVGGAGASAGGSSVQVNQLNGGRITNGAVIERELPSQFG VGNTLNLQLNDEDFSMAQQIADTINRVRGYGSATALDARTIQVRVPSGNSSQVRFLADIQ NMQVNVTPQDAKVVINSRTGSVVMNREVTLDSCAVAQGNLSVTVNRQANVSQPDTPFGGG QTVVTPQTQIDLRQSGGSLQSVRSSASLNNVVRALNALGATPMDLMSILQSMQSAGCLRA KLEII P76553 P76969 EUTG_ECOLI Ethanolamine utilization protein EutG 1.1.-.- eutG yffV b2453 JW2437 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 May act on the acetaldehyde produced from the degradation of ethanolamine. Amine and polyamine degradation; ethanolamine degradation. Belongs to the iron-containing alcohol dehydrogenase family. Complete proteome NAD Oxidoreductase Reference proteome MQNELQTALFQAFDTLNLQRVKTFSVPPVTLCGPGSVSSCGQQAQTRGLKHLFVMADSFL HQAGMTAGLTRSLTVKGIAMTLWPCPVGEPCITDVCAAVAQLRESGCDGVIAFGGGSVLD AAKAVTLLVTNPDSTLAEMSETSVLQPRLPLIAIPTTAGTGSETTNVTVIIDAVSGRKQV LAHASLMPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSALNATPFTDSLAIGAIAM IGKSLPKAVGYGHDLAARESMLLASCMAGMAFSSAGLGLCHAMAHQPGAALHIPHGLANA MLLPTVMEFNRMVCRERFSQIGRALRTKKSDDRDAINAVSELIAEVGIGKRLGDVGATSA HYGAWAQAALEDICLRSNPRTASLEQIVGLYAAAQ P09549 DEDD_ECOLI Cell division protein DedD dedD b2314 JW5378 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION SUBCELLULAR LOCATION DISRUPTION PHENOTYPE K12 / MG1655 / ATCC 47076 SUBCELLULAR LOCATION DOMAIN K12 / BW25113 Non-essential cell division protein that could be required for efficient cell constriction. Cell inner membrane Single-pass membrane protein Localizes at the septal ring. The SPOR domain binds septal peptidoglycans and is required to target DedD to the septal ring. Deletion causes a mild cell chaining phenotype. Belongs to the DedD family. Translation N-terminally extended. Cell cycle Cell division Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MASKFQNRLVGTIVLVALGVIVLPGLLDGQKKHYQDEFAAIPLVPKAGDRDEPDMMPAAT QALPTQPPEGAAEEVRAGDAAAPSLDPATIAANNTEFEPEPAPVAPPKPKPVEPPKPKVE APPAPKPEPKPVVEEKAAPTGKAYVVQLGALKNADKVNEIVGKLRGAGYRVYTSPSTPVQ GKITRILVGPDASKDKLKGSLGELKQLSGLSGVVMGYTPN P0DQD7 GNDA_ECOLI Protein GndA gndA Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 PROTEIN SEQUENCE OF 39-51 INDENTIFICATION SUBCELLULAR LOCATION INDUCTION BY HEAT SHOCK K12 / MG1655 / ATCC 47076 Cell inner membrane Single-pass membrane protein By heat shock (shift from 30 to 45 degrees Celsius) (at protein level). Entirely encoded within the coding gene for gnd (AC P00350), on the same strand within another reading frame. This protein is produced independently of gnd. It is uncertain whether Met-1 or Met-19 is the initiator. Cell inner membrane Cell membrane Complete proteome Direct protein sequencing Membrane Reference proteome Stress response Transmembrane Transmembrane helix MLLLIPSNHISIKETSSLMVVTPSSRTLFVVIVSFQQRALTSSVPVFLAVKRGR P0DSF9 EVGL_ECOLI Protein EvgL evgL b4781 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 IDENTIFICATION INDUCTION K12 / MG1655 / ATCC 47076 Expressed in both exponential and stationary phase in rich medium; expression is higher in stationary phase (at protein level). Complete proteome Reference proteome MLHCKGNNL P30843 Q2M6J1 Q5MNC7 Q5MNC9 Q5MNE0 Q5MNE5 Q5MNF2 Q5MNH0 BASR_ECOLI Transcriptional regulatory protein BasR basR pmrA b4113 JW4074 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [GENOMIC DNA] REGULATION BY PMRD ECOR 1 ECOR 10 ECOR 11 ECOR 12 ECOR 13 ECOR 14 ECOR 15 ECOR 16 ECOR 17 ECOR 18 ECOR 19 ECOR 2 ECOR 20 ECOR 21 ECOR 22 ECOR 24 ECOR 25 ECOR 26 ECOR 27 ECOR 3 ECOR 30 ECOR 33 ECOR 34 ECOR 35 ECOR 36 ECOR 37 ECOR 38 ECOR 4 ECOR 40 ECOR 41 ECOR 42 ECOR 43 ECOR 44 ECOR 45 ECOR 46 ECOR 47 ECOR 48 ECOR 5 ECOR 51 ECOR 52 ECOR 53 ECOR 54 ECOR 55 ECOR 56 ECOR 57 ECOR 59 ECOR 6 ECOR 60 ECOR 61 ECOR 62 ECOR 63 ECOR 64 ECOR 65 ECOR 66 ECOR 67 ECOR 68 ECOR 69 ECOR 7 ECOR 70 ECOR 71 ECOR 72 ECOR 8 ECOR 9 O2:HN / ECOR 50 / P97 / UPEC NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 PHOSPHORYLATION K12 / W3110 / ATCC 27325 / DSM 5911 Member of the two-component regulatory system BasS/BasR. BasR induces the transcription of the ugd, ais, arnBCADTEF and eptA-basRS loci, all involved in resistance to polymyxin (By similarity). Homodimer. Cytoplasm The eptA-basRS operon is positively autoregulated by BasR under high iron or aluminum concentration conditions. Phosphorylated by BasS. The activity of the BasR protein is in some natural isolates, but not in strain K12, controlled at a post-transcriptional level by the PmrD protein under low Mg(2+) concentration conditions. Activator Antibiotic resistance Complete proteome Cytoplasm DNA-binding Phosphoprotein Reference proteome Transcription Transcription regulation Two-component regulatory system S G T S I N V L G S R P Y F S T MKILIVEDDTLLLQGLILAAQTEGYACDSVTTARMAEQSLEAGHYSLVVLDLGLPDEDGL HFLARIRQKKYTLPVLILTARDTLTDKIAGLDVGADDYLVKPFALEELHARIRALLRRHN NQGESELIVGNLTLNMGRRQVWMGGEELILTPKEYALLSRLMLKAGSPVHREILYNDIYN WDNEPSTNTLEVHIHNLRDKVGKARIRTVRGFGYMLVANEEN P17445 Q2MCB1 BETB_ECOLI NAD/NADP-dependent betaine aldehyde dehydrogenase BADH 1.2.1.8 betB b0312 JW0304 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] PROTEIN SEQUENCE OF 2-29 K12 NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION CATALYTIC ACTIVITY BIOPHYSICOCHEMICAL PROPERTIES INDUCTION FUNCTION CATALYTIC ACTIVITY BIOPHYSICOCHEMICAL PROPERTIES ACTIVITY REGULATION SUBSTRATE SPECIFICITY SUBUNIT INDUCTION Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the reversible oxidation of betaine aldehyde to the corresponding acid. It is highly specific for betaine and has a significantly higher affinity for NAD than for NADP. betaine aldehyde + H2O + NAD(+) = betaine + 2 H(+) + NADH K(+) Binds 2 potassium ions per subunit. Aldehydes with apolar groups are the most effective inhibitors. N-Methylated compounds are also inhibitory, but to a much lesser degree than the aldehydes. The alcohols are more inhibitory than the corresponding acids, and the inhibitory effect increases with the degree of methylation from ethanolamine to choline. 99 uM for NAD (at pH 7.5 and 25 degrees Celsius) 160 uM for betaine aldehyde (at pH 7.5 and 25 degrees Celsius) 400 uM for NADP (at pH 7.5 and 25 degrees Celsius) 66 umol/min/mg enzyme (at pH 7.5 and 25 degrees Celsius) Optimum pH is between 7.5 and 9.5. Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1. Dimer of dimers. By osmotic stress. Choline is required for full expression. Oxygen and choline exert their control via the transacting DNA-binding proteins ArcA and BetI, respectively. Belongs to the aldehyde dehydrogenase family. Translation N-terminally shortened. Translation N-terminally shortened. Complete proteome Direct protein sequencing Metal-binding NAD NADP Oxidation Oxidoreductase Potassium Reference proteome Stress response A R R P MSRMAEQQLYIHGGYTSATSGRTFETINPANGNVLATVQAAGREDVDRAVKSAQQGQKIW ASMTAMERSRILRRAVDILRERNDELAKLETLDTGKAYSETSTVDIVTGADVLEYYAGLI PALEGSQIPLRETSFVYTRREPLGVVAGIGAWNYPIQIALWKSAPALAAGNAMIFKPSEV TPLTALKLAEIYSEAGLPDGVFNVLPGVGAETGQYLTEHPGIAKVSFTGGVASGKKVMAN SAASSLKEVTMELGGKSPLIVFDDADLDLAADIAMMANFFSSGQVCTNGTRVFVPAKCKA AFEQKILARVERIRAGDVFDPQTNFGPLVSFPHRDNVLRYIAKGKEEGARVLCGGDVLKG DGFDNGAWVAPTVFTDCSDDMTIVREEIFGPVMSILTYESEDEVIRRANDTDYGLAAGIV TADLNRAHRVIHQLEAGICWINTWGESPAEMPVGGYKHSGIGRENGVMTLQSYTQVKSIQ VEMAKFQSIF P77398 Q56VX0 ARNA_ECOLI Bifunctional polymyxin resistance protein ArnA Polymyxin resistance protein PmrI UDP-4-amino-4-deoxy-L-arabinose formyltransferase 2.1.2.13 ArnAFT UDP-L-Ara4N formyltransferase UDP-glucuronic acid oxidase, UDP-4-keto-hexauronic acid decarboxylating 1.1.1.305 ArnADH UDP-GlcUA decarboxylase UDP-glucuronic acid dehydrogenase arnA pmrI yfbG b2255 JW2249 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] FUNCTION OF C-TERMINAL DOMAIN CHARACTERIZATION K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 INDUCTION BY BASR K12 / MG1655 / ATCC 47076 FUNCTION OF N-TERMINAL DOMAIN CATALYTIC ACTIVITY CHARACTERIZATION K12 / W3110 / ATCC 27325 / DSM 5911 PATHWAY K12 / W3110 / ATCC 27325 / DSM 5911 X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 306-660 CATALYTIC ACTIVITY OF C-TERMINAL DOMAIN BIOPHYSICOCHEMICAL PROPERTIES X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-300 MUTAGENESIS OF ASN-102; HIS-104 AND ASP-140 REACTION MECHANISM X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) IN COMPLEX WITH UMP AND N-5-FTHF MUTAGENESIS OF SER-433 AND GLU-434 X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) IN COMPLEX WITH UDP-GLCUA AND NAD ANALOG AND OF 306-660 OF MUTANTS ALA-433; GLU-619; MET-619 AND TYR-619 MUTAGENESIS OF SER-433 AND ARG-619 SUBUNIT REACTION MECHANISM Bifunctional enzyme that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O) and the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. NAD(+) + UDP-alpha-D-glucuronate = CO2 + NADH + UDP-beta-L-threo-pentopyranos-4-ulose (6S)-10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinose = (6S)-5,6,7,8-tetrahydrofolate + H(+) + UDP-4-deoxy-4-formamido-beta-L-arabinose 0.76 mM for NAD 0.086 mM for UDP-GlcUA Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose from UDP-alpha-D-glucuronate: step 1/3. Nucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose from UDP-alpha-D-glucuronate: step 3/3. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Homohexamer, formed by a dimer of trimers. false 3 P76092 ynbC false 2 Induced by BasR. In the N-terminal section; belongs to the Fmt family. UDP-L-Ara4N formyltransferase subfamily. In the C-terminal section; belongs to the NAD(P)-dependent epimerase/dehydratase family. UDP-glucuronic acid decarboxylase subfamily. 3D-structure Antibiotic resistance Complete proteome Lipid A biosynthesis Lipid biosynthesis Lipid metabolism Lipopolysaccharide biosynthesis Multifunctional enzyme NAD Oxidoreductase Reference proteome Transferase N A H A H K D A N S A S T E A E Q R E Y R M MKTVVFAYHDMGCLGIEALLAAGYEISAIFTHTDNPGEKAFYGSVARLAAERGIPVYAPD NVNHPLWVERIAQLSPDVIFSFYYRHLIYDEILQLAPAGAFNLHGSLLPKYRGRAPLNWV LVNGETETGVTLHRMVKRADAGAIVAQLRIAIAPDDIAITLHHKLCHAARQLLEQTLPAI KHGNILEIAQRENEATCFGRRTPDDSFLEWHKPASVLHNMVRAVADPWPGAFSYVGNQKF TVWSSRVHPHASKAQPGSVISVAPLLIACGDGALEIVTGQAGDGITMQGSQLAQTLGLVQ GSRLNSQPACTARRRTRVLILGVNGFIGNHLTERLLREDHYEVYGLDIGSDAISRFLNHP HFHFVEGDISIHSEWIEYHVKKCDVVLPLVAIATPIEYTRNPLRVFELDFEENLRIIRYC VKYRKRIIFPSTSEVYGMCSDKYFDEDHSNLIVGPVNKPRWIYSVSKQLLDRVIWAYGEK EGLQFTLFRPFNWMGPRLDNLNAARIGSSRAITQLILNLVEGSPIKLIDGGKQKRCFTDI RDGIEALYRIIENAGNRCDGEIINIGNPENEASIEELGEMLLASFEKHPLRHHFPPFAGF RVVESSSYYGKGYQDVEHRKPSIRNAHRCLDWEPKIDMQETIDETLDFFLRTVDLTDKPS P77357 P76847 ABGA_ECOLI p-aminobenzoyl-glutamate hydrolase subunit A 3.5.1.- PABA-GLU hydrolase PGH abgA ydaJ b1338 JW5205 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 PROTEIN SEQUENCE OF 1-10 FUNCTION AS A PABA-GLU HYDROLASE BIOPHYSICOCHEMICAL PROPERTIES SUBUNIT COFACTOR INDUCTION FUNCTION AS A PABA-GLU HYDROLASE Component of the p-aminobenzoyl-glutamate hydrolase multicomponent enzyme system which catalyzes the cleavage of p-aminobenzoyl-glutamate (PABA-GLU) to form p-aminobenzoate (PABA) and glutamate. AbgAB does not degrade dipeptides and the physiological role of abgABT should be clarified. Mn(2+) 60 uM for PABA-GLU (at pH 8.5) Forms a heterodimer with AbgB. P76052 abgB false 2 Could be transcriptionally regulated by AbgR. Belongs to the peptidase M20 family. Complete proteome Direct protein sequencing Hydrolase Reference proteome MESLNQFVNSLAPKLSHWRRDFHHYAESGWVEFRTATLVAEELHQLGYSLALGREVVNES SRMGLPDEFTLQREFERARQQGALAQWIAAFEGGFTGIVATLDTGRPGPVMAFRVDMDAL DLSEEQDVSHRPYRDGFASCNAGMMHACGHDGHTAIGLGLAHTLKQFESGLHGVIKLIFQ PAEEGTRGARAMVDAGVVDDVDYFTAVHIGTGVPAGTVVCGSDNFMATTKFDAHFTGTAA HAGAKPEDGHNALLAAAQATLALHAIAPHSEGASRVNVGVMQAGSGRNVVPASALLKVET RGASDVINQYVFDRAQQAIQGAATMYGVGVETRLMGAATASSPSPQWVAWLQSQAAQVAG VNQAIERVEAPAGSEDATLMMARVQQHQGQASYVVFGTQLAAGHHNEKFDFDEQVLAIAV ETLARTALNFPWTRGI P0ABA4 P00831 Q2M853 ATPD_ECOLI ATP synthase subunit delta ATP synthase F(1) sector subunit delta F-type ATPase subunit delta F-ATPase subunit delta atpH papE uncH b3735 JW3713 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 SUBUNIT SUBCELLULAR LOCATION BL21-DE3 STRUCTURE BY NMR OF 1-135 F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. F-type ATPases have 2 components, F(1) - the catalytic core - and F(0) - the membrane proton channel. F(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. F(1) is attached to F(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. Cell inner membrane Peripheral membrane protein Belongs to the ATPase delta chain family. 3D-structure ATP synthesis Cell inner membrane Cell membrane CF(1) Complete proteome Hydrogen ion transport Ion transport Membrane Reference proteome Transport E D MSEFITVARPYAKAAFDFAVEHQSVERWQDMLAFAAEVTKNEQMAELLSGALAPETLAES FIAVCGEQLDENGQNLIRVMAENGRLNALPDVLEQFIHLRAVSEATAEVDVISAAALSEQ QLAKISAAMEKRLSRKVKLNCKIDKSVMAGVIIRAGDMVIDGSVRGRLERLADVLQS P56262 Q2M8D5 Q6BEY8 DLHH_ECOLI Putative carboxymethylenebutenolidase 3.1.1.45 Dienelactone hydrolase DLH ysgA b3830 JW5853 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 SEQUENCE REVISION NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 2-(5-oxo-2,5-dihydrofuran-2-ylidene)acetate + H2O = 4-oxohex-2-enedioate + H(+) Belongs to the dienelactone hydrolase family. Complete proteome Hydrolase Reference proteome MATTQQSGFAPAASPLASTIVQTPDDAIVAGFTSIPSQGDNMPAYHARPKQSDGPLPVVI VVQEIFGVHEHIRDICRRLALEGYLAIAPELYFREGDPNDFADIPTLLSGLVAKVPDSQV LADLDHVASWASRNGGDVHRLMITGFCWGGRITWLYAAHNPQLKAAVAWYGKLTGDKSLN SPKQPVDIATDLNAPILGLYGGQDNSIPQESVETMRQALRAANAKAEIIVYPDAGHAFNA DYRPSYHAASAEDGWQRMLEWFKQYGGKKSL P52599 P76517 P76944 P76945 EMRK_ECOLI Probable multidrug resistance protein EmrK emrK b2368 JW2365 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 INDUCTION K12 / MC4100 / ATCC 35695 / DSM 6574 DISRUPTION PHENOTYPE K12 Part of the tripartite efflux system EmrYK-TolC, which confers resistance to various drugs. Part of the tripartite efflux system EmrYK-TolC, which is composed of an inner membrane transporter, EmrY, a membrane fusion protein, EmrK, and an outer membrane component, TolC. The complex forms a large protein conduit and can translocate molecules across both the inner and outer membranes (By similarity). Cell inner membrane Single-pass membrane protein Periplasmic side Growth phase-dependent transcription is induced by tetracycline. Expression may be controlled by both RpoS and the Mar system. Mutants are more sensitive to nalidixic acid, mitomycin C and other stresses such as hydrogen peroxide or UV irradiation. Belongs to the membrane fusion protein (MFP) (TC 8.A.1) family. Translation N-terminally extended. Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix Transport MEQINSNKKHSNRRKYFSLLAVVLFIAFSGAYAYWSMELEDMISTDDAYVTGNADPISAQ VSGSVTVVNHKDTNYVRQGDILVSLDKTDATIALNKAKNNLANIVRQTNKLYLQDKQYSA EVASARIQYQQSLEDYNRRVPLAKQGVISKETLEHTKDTLISSKAALNAAIQAYKANKAL VMNTPLNRQPQVVEAADATKEAWLALKRTDIKSPVTGYIAQRSVQVGETVSPGQSLMAVV PARQMWVNANFKETQLTDVRIGQSVNIISDLYGENVVFHGRVTGINMGTGNAFSLLPAQN ATGNWIKIVQRVPVEVSLDPKELMEHPLRIGLSMTATIDTKNEDIAEMPELASTVTSMPA YTSKALVIDTSPIEKEISNIISHNGQL P00816 Q2MC84 CYNS_ECOLI Cyanate hydratase Cyanase 4.2.1.104 Cyanate hydrolase Cyanate lyase cynS cnt b0340 JW0331 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia PROTEIN SEQUENCE NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 CHARACTERIZATION IDENTIFICATION BY 2D-GEL X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide. cyanate + 3 H(+) + hydrogencarbonate = 2 CO2 + NH4(+) Homodecamer composed of five homodimers. Belongs to the cyanase family. 3D-structure Complete proteome Direct protein sequencing Lyase Reference proteome D N D N L S N D MIQSQINRNIRLDLADAILLSKAKKDLSFAEIADGTGLAEAFVTAALLGQQALPADAARL VGAKLDLDEDSILLLQMIPLRGCIDDRIPTDPTMYRFYEMLQVYGTTLKALVHEKFGDGI ISAINFKLDVKKVADPEGGERAVITLDGKYLPTKPF P76127 Q2MBA3 BDM_ECOLI Protein bdm Biofilm-dependent modulation protein bdm yddX b1481 JW5239 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 INDUCTION K12 / MC4100 / PHL644 Expression is reduced in biofilms and is repressed by a high salt concentration. Complete proteome Reference proteome MFTYYQAENSTAEPALVNAIEQGLRAQHGVVTEDDILMELTKWVEASDNDILSDIYQQTI NYVVSGQHPTL P17444 P77861 Q2MCB2 BETA_ECOLI Oxygen-dependent choline dehydrogenase CDH CHD 1.1.99.1 Betaine aldehyde dehydrogenase BADH 1.2.1.8 betA b0311 JW0303 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION CATALYTIC ACTIVITY BIOPHYSICOCHEMICAL PROPERTIES INDUCTION ACTIVITY REGULATION SUBCELLULAR LOCATION FUNCTION DISRUPTION PHENOTYPE NOMENCLATURE INDUCTION Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the oxidation of choline to betaine aldehyde and betaine aldehyde to glycine betaine at the same rate. A + choline = AH2 + betaine aldehyde betaine aldehyde + H2O + NAD(+) = betaine + 2 H(+) + NADH FAD Activated by high osmotic strength. 0.06 mM for NAD (at pH 7.5 and 37 degrees Celsius) 0.13 mM for glycine betaine aldehyde (at pH 7.5 and 37 degrees Celsius) 0.5 mM for NADP (at pH 7.5 and 37 degrees Celsius) 1.5 mM for choline (at pH 7.5 and 37 degrees Celsius) 1.6 mM for glycine betaine aldehyde (at pH 7.5 and 37 degrees Celsius) Optimum pH is 7.5 for choline dehydrogenase and is between 7.5 and 9.5 for glycine betaine-aldehyde dehydrogenase. Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine aldehyde from choline (cytochrome c reductase route): step 1/1. Cell membrane Peripheral membrane protein By osmotic stress. Choline is required for full expression. Oxygen and choline exert their control via the transacting DNA-binding proteins ArcA and BetI, respectively. Cells lacking this gene do not grow at high osmotic strength in the presence of choline, but are able to grow when the medium is supplemented with glycine betaine. Belongs to the GMC oxidoreductase family. Translation N-terminally extended. Cell membrane Complete proteome FAD Flavoprotein Membrane NAD Oxidoreductase Reference proteome Stress response MQFDYIIIGAGSAGNVLATRLTEDPNTSVLLLEAGGPDYRFDFRTQMPAALAFPLQGKRY NWAYETEPEPFMNNRRMECGRGKGLGGSSLINGMCYIRGNALDLDNWAQEPGLENWSYLD CLPYYRKAETRDMGENDYHGGDGPVSVTTSKPGVNPLFEAMIEAGVQAGYPRTDDLNGYQ QEGFGPMDRTVTPQGRRASTARGYLDQAKSRPNLTIRTHAMTDHIIFDGKRAVGVEWLEG DSTIPTRATANKEVLLCAGAIASPQILQRSGVGNAELLAEFDIPLVHELPGVGENLQDHL EMYLQYECKEPVSLYPALQWWNQPKIGAEWLFGGTGVGASNHFEAGGFIRSREEFAWPNI QYHFLPVAINYNGSNAVKEHGFQCHVGSMRSPSRGHVRIKSRDPHQHPAILFNYMSHEQD WQEFRDAIRITREIMHQPALDQYRGREISPGVECQTDEQLDEFVRNHAETAFHPCGTCKM GYDEMSVVDGEGRVHGLEGLRVVDASIMPQIITGNLNATTIMIGEKIADMIRGQEALPRS TAGYFVANGMPVRAKK P23910 Q2MC30 ARAJ_ECOLI Putative transporter AraJ araJ b0396 JW0386 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] DISRUPTION PHENOTYPE NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 INDUCTION SUBCELLULAR LOCATION TOPOLOGY [LARGE SCALE ANALYSIS] K12 / MG1655 / ATCC 47076 May be involved in either the transport or processing of arabinose polymers. Cell inner membrane Multi-pass membrane protein Induced by arabinose (PubMed:2231717) (Probable). Transcription is dependent on the transcription factor AraC, the cAMP receptor protein (CRP) and cAMP (PubMed:2231717). No visible effect on arabinose uptake or growth on arabinose. Belongs to the major facilitator superfamily. Translation N-terminally shortened. Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix Transport MKKVILSLALGTFGLGMAEFGIMGVLTELAHNVGISIPAAGHMISYYALGVVVGAPIIAL FSSRYSLKHILLFLVALCVIGNAMFTLSSSYLMLAIGRLVSGFPHGAFFGVGAIVLSKII KPGKVTAAVAGMVSGMTVANLLGIPLGTYLSQEFSWRYTFLLIAVFNIAVMASVYFWVPD IRDEAKGNLREQFHFLRSPAPWLIFAATMFGNAGVFAWFSYVKPYMMFISGFSETAMTFI MMLVGLGMVLGNMLSGRISGRYSPLRIAAVTDFIIVLALLMLFFCGGMKTTSLIFAFICC AGLFALSAPLQILLLQNAKGGELLGAAGGQIAFNLGSAVGAYCGGMMLTLGLAYNYVALP AALLSFAAMSSLLLYGRYKRQQAADTPVLAKPLG P0A6E4 P22767 Q2M939 ASSY_ECOLI Argininosuccinate synthase 6.3.4.5 Citrulline--aspartate ligase argG b3172 JW3140 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] PROTEIN SEQUENCE OF 2-11 K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 PROTEIN SEQUENCE OF 2-13 K12 / EMG2 CHARACTERIZATION CRYSTALLIZATION X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) UNCOMPLEXED AND IN COMPLEX WITH ASPARTATE AND CITRULLINE X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ATP AND CITRULLINE ATP + L-aspartate + L-citrulline = 2-(N(omega)-L-arginino)succinate + AMP + diphosphate + H(+) Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. Homotetramer. false 2 P24228 dacB false 2 Cytoplasm The monomer is composed of two major structural domains: a nucleotide-binding domain and a catalytic/multimerization domain. Binding of ATP results in a large rigid body conformational change of the nucleotide binding domain. Belongs to the argininosuccinate synthase family. Type 2 subfamily. 3D-structure Amino-acid biosynthesis Arginine biosynthesis ATP-binding Complete proteome Cytoplasm Direct protein sequencing Ligase Nucleotide-binding Reference proteome I N G D MTTILKHLPVGQRIGIAFSGGLDTSAALLWMRQKGAVPYAYTANLGQPDEEDYDAIPRRA MEYGAENARLIDCRKQLVAEGIAAIQCGAFHNTTGGLTYFNTTPLGRAVTGTMLVAAMKE DGVNIWGDGSTYKGNDIERFYRYGLLTNAELQIYKPWLDTDFIDELGGRHEMSEFMIACG FDYKMSVEKAYSTDSNMLGATHEAKDLEYLNSSVKIVNPIMGVKFWDESVKIPAEEVTVR FEQGHPVALNGKTFSDDVEMMLEANRIGGRHGLGMSDQIENRIIEAKSRGIYEAPGMALL HIAYERLLTGIHNEDTIEQYHAHGRQLGRLLYQGRWFDSQALMLRDSLQRWVASQITGEV TLELRRGNDYSILNTVSENLTYKPERLTMEKGDSVFSPDDRIGQLTMRNLDITDTREKLF GYAKTGLLSSSAASGVPQVENLENKGQ P15078 P23517 P77740 CSTA_ECOLI Peptide transporter CstA Carbon starvation protein A cstA ybdC b0598 JW0590 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] FUNCTION INDUCTION K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-200 TOPOLOGY [LARGE SCALE ANALYSIS] SUBCELLULAR LOCATION K12 / MG1655 / ATCC 47076 TRANSLATION REGULATION Involved in peptide utilization during carbon starvation. Cell inner membrane Multi-pass membrane protein Induced by carbon starvation. Induction requires the cAMP-cAMP receptor protein (CRP) complex (PubMed:1848300). The carbon storage regulator CsrA regulates translation of cstA by sterically interfering with ribosome binding (PubMed:12867454). Belongs to the peptide transporter carbon starvation (CstA) (TC 2.A.114) family. Cell inner membrane Cell membrane Complete proteome Membrane Peptide transport Protein transport Reference proteome Stress response Transmembrane Transmembrane helix Transport A G MNKSGKYLVWTVLSVMGAFALGYIALNRGEQINALWIVVASVCIYLIAYRFYGLYIAKNV LAVDPTRMTPAVRHNDGLDYVPTDKKVLFGHHFAAIAGAGPLVGPVLAAQMGYLPGMIWL LAGVVLAGAVQDFMVLFVSTRRDGRSLGELVKEEMGPTAGVIALVACFMIMVIILAVLAM IVVKALTHSPWGTYTVAFTIPLALFMGIYLRYLRPGRIGEVSVIGLVFLIFAIISGGWVA ESPTWAPYFDFTGVQLTWMLVGYGFVAAVLPVWLLLAPRDYLSTFLKIGTIVGLAVGILI MRPTLTMPALTKFVDGTGPVWTGNLFPFLFITIACGAVSGFHALISSGTTPKMLANEGQA CFIGYGGMLMESFVAIMALVSACIIDPGVYFAMNSPMAVLAPAGTADVVASAAQVVSSWG FSITPDTLNQIASEVGEQSIISRAGGAPTLAVGMAYILHGALGGMMDVAFWYHFAILFEA LFILTAVDAGTRAARFMLQDLLGVVSPGLKRTDSLPANLLATALCVLAWGYFLHQGVVDP LGGINTLWPLFGIANQMLAGMALMLCAVVLFKMKRQRYAWVALVPTAWLLICTLTAGWQK AFSPDAKVGFLAIANKFQAMIDSGNIPSQYTESQLAQLVFNNRLDAGLTIFFMVVVVVLA LFSIKTALAALKDPKPTAKETPYEPMPENVEEIVAQAKGAH P0AE12 P15272 P78074 AMN_ECOLI AMP nucleosidase 3.2.2.4 amn b1982 JW1963 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] PARTIAL PROTEIN SEQUENCE INDUCTION NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-159 K12 FUNCTION CATALYTIC ACTIVITY ACTIVITY REGULATION BIOPHYSICOCHEMICAL PROPERTIES K12 IDENTIFICATION BY 2D-GEL DISRUPTION PHENOTYPE X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH FORMYCIN-5'-MONOPHOSPHATE AND PHOSPHATE SUBUNIT DOMAIN Catalyzes the hydrolysis of the N-glycosidic bond of AMP to form adenine and ribose 5-phosphate. Involved in regulation of AMP concentrations. AMP + H2O = adenine + D-ribose 5-phosphate Allosterically activated by Mg-ATP. Inhibited by inorganic phosphate and formycin monophosphate. 15 mM for AMP (in the absence of Mg-ATP) 0.09 mM for AMP (in the presence of saturating Mg-ATP) Homohexamer. Trimer of dimers. By cAMP at limiting phosphate concentrations. Repressed by phosphate. Each monomer consists of two domains: a C-terminal catalytic domain and a putative N-terminal regulatory domain. Knockout elevates intracellular ATP levels and increases cold tolerance. AMP nucleosidase binds AMP at the catalytic site, Mg-ATP at an allosteric regulatory site, and inorganic phosphate also at a regulatory site. Belongs to the AMP nucleosidase family. 3D-structure Allosteric enzyme Complete proteome Direct protein sequencing Hydrolase Reference proteome WLM CY ESQAIG KVRPLA MNNKGSGLTPAQALDKLDALYEQSVVALRNAIGNYITSGELPDENARKQGLFVYPSLTVT WDGSTTNPPKTRAFGRFTHAGSYTTTITRPTLFRSYLNEQLTLLYQDYGAHISVQPSQHE IPYPYVIDGSELTLDRSMSAGLTRYFPTTELAQIGDETADGIYHPTEFSPLSHFDARRVD FSLARLRHYTGTPVEHFQPFVLFTNYTRYVDEFVRWGCSQILDPDSPYIALSCAGGNWIT AETEAPEEAISDLAWKKHQMPAWHLITADGQGITLVNIGVGPSNAKTICDHLAVLRPDVW LMIGHCGGLRESQAIGDYVLAHAYLRDDHVLDAVLPPDIPIPSIAEVQRALYDATKLVSG RPGEEVKQRLRTGTVVTTDDRNWELRYSASALRFNLSRAVAIDMESATIAAQGYRFRVPY GTLLCVSDKPLHGEIKLPGQANRFYEGAISEHLQIGIRAIDLLRAEGDRLHSRKLRTFNE PPFR P13039 P77094 FES_ECOLI Enterochelin esterase Ferric enterobactin esterase fes b0585 JW0576 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] PROTEIN SEQUENCE OF 27-31 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-307 K12 / W3110 / ATCC 27325 / DSM 5911 PROTEIN SEQUENCE OF 6-15 K12 / BW25113 Upon internalization, ferric enterobactin is processed via an exquisitely specific pathway that is dependent on FES activity, making iron available for metabolic use. Cytoplasm Belongs to the Fes family. Translation N-terminally extended. Translation N-terminally extended. Complete proteome Cytoplasm Direct protein sequencing Ion transport Iron Iron transport Reference proteome Transport MTALKVGSESWWQSKHGPEWQRLNDEMFEVTFWWRDPQGSEEYSTIKRVWVYITGVTDHH QNSQPQSMQRIAGTNVWQWTTQLNANWRGSYCFIPTERDDIFSVPSPDRLELREGWRKLL PQAIADPLNLQSWKGGRGHAVSALEMPQAPLQPGWDCPQAPEIPAKEIIWKSERLKKSRR VWIFTTGDATAEERPLAVLLDGEFWAQSMPVWPVLTSLTHRQQLPPAVYVLIDAIDTTHR AHELPCNADFWLAVQQELLPLVKAIAPFSDRADRTVVAGQSFGGLSALYAGLHWPERFGC VLSQSGSYWWPHRGGQQEGVLLEKLKAGEVSAEGLRIVLEAGIREPMIMRANQALYAQLH PIKESIFWRQVDGGHDALCWRGGLMQGLIDLWQPLFHDRS P06968 Q2M7V4 DUT_ECOLI Deoxyuridine 5'-triphosphate nucleotidohydrolase dUTPase 3.6.1.23 dUTP pyrophosphatase dut dnaS sof b3640 JW3615 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 PROTEIN SEQUENCE OF 1-5 FUNCTION CATALYTIC ACTIVITY BIOPHYSICOCHEMICAL PROPERTIES SUBCELLULAR LOCATION SUBUNIT DOMAIN MASS SPECTROMETRY IDENTIFICATION BY 2D-GEL X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) SUBUNIT SUBCELLULAR LOCATION X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS AND SUBSTRATE COFACTOR MUTAGENESIS OF ASP-90 SUBUNIT This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. dUTP + H2O = diphosphate + dUMP + H(+) Mg(2+) 0.28 uM for dUTP kcat is 5.15 s(-1). Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2. Homotrimer. Cytoplasm The C-terminal 11 residues (motif 5) is important for function; its removal by trypsin decreases kcat about 40-fold with a less than 2-fold increase in KM for dUTP. Belongs to the dUTPase family. Translation N-terminally extended. Translation N-terminally extended. Translation N-terminally extended. Translation N-terminally extended. Translation N-terminally extended. 3D-structure Complete proteome Cytoplasm Direct protein sequencing Hydrolase Magnesium Metal-binding Nucleotide metabolism Reference proteome D N MMKKIDVKILDPRVGKEFPLPTYATSGSAGLDLRACLNDAVELAPGDTTLVPTGLAIHIA DPSLAAMMLPRSGLGHKHGIVLGNLVGLIDSDYQGQLMISVWNRGQDSFTIQPGERIAQM IFVPVVQAEFNLVEDFDATDRGEGGFGHSGRQ P0AFU4 P21712 P77512 GLRR_ECOLI Transcriptional regulatory protein GlrR glrR yfhA b2554 JW2538 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 288-444 K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 404-444 K12 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 419-444 PHOSPHORYLATION K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION DNA-BINDING DISRUPTION PHENOTYPE GENE NAME Member of the two-component regulatory system GlrR/GlrK that up-regulates transcription of the glmY sRNA when cells enter the stationary growth phase. Regulates glmY transcription by binding to three conserved sites in the purL-glmY intergenic region. Cytoplasm Phosphorylated by GlrK. Mutants show decreased amounts of glmY. Not required for the regulation of the glmY-glmZ-glmS regulatory cascade by glucosamine-6-phosphate depletion. ATP-binding Complete proteome Cytoplasm DNA-binding Nucleotide-binding Phosphoprotein Reference proteome Transcription Transcription regulation Two-component regulatory system K N ER DG ER DG MSHKPAHLLLVDDDPGLLKLLGLRLTSEGYSVVTAESGAEGLRVLNREKVDLVISDLRMD EMDGMQLFAEIQKVQPGMPVIILTAHGSIPDAVAATQQGVFSFLTKPVDKDALYQAIDDA LEQSAPATDERWREAIVTRSPLMLRLLEQARLVAQSDVSVLINGQSGTGKEIFAQAIHNA SPRNSKPFIAINCGALPEQLLESELFGHARGAFTGAVSNREGLFQAAEGGTLFLDEIGDM PAPLQVKLLRVLQERKVRPLGSNRDIDINVRIISATHRDLPKAMARGEFREDLYYRLNVV SLKIPALAERTEDIPLLANHLLRQAAERHKPFVRAFSTDAMKRLMTASWPGNVRQLVNVI EQCVALTSSPVISDALVEQALEGENTALPTFVEARNQFELNYLRKLLQITKGNVTHAARM AGRNRTEFYKLLSRHELDANDFKE P77774 BAMB_ECOLI Outer membrane protein assembly factor BamB bamB yfgL b2512 JW2496 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 SUBUNIT SUBCELLULAR LOCATION K12 SUBUNIT INTERACTION WITH BAMA K12 FUNCTION SUBUNIT FUNCTION SUBUNIT X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 21-392 X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 22-392 INTERACTION WITH BAMA SUBUNIT FUNCTION X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 21-392 X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 21-392 FUNCTION SUBUNIT STRUCTURE BY ELECTRON MICROSCOPY (4.90 ANGSTROMS) OF 22-392 IN LATERAL OPEN BAM COMPLEX FUNCTION REACTION MECHANISM SUBUNIT MASS SPECTROMETRY DIACYLGLYCEROL AT CYS-20 PALMITOYLATION AT CYS-20 X-RAY CRYSTALLOGRAPHY (3.56 ANGSTROMS) OF 20-392 IN LATERAL CLOSED BAM COMPLEX SUBUNIT SUBCELLULAR LOCATION K12 / MG1655 / ATCC 47076 X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN LATERAL CLOSED BAM COMPLEX REACTION MECHANISM SUBUNIT SUBCELLULAR LOCATION Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex, which may orient the flexible periplasmic domain of BamA for interaction with other Bam components, chaperones and nascent outer membrane proteins. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits (PubMed:20378773, PubMed:21823654, PubMed:27686148). A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly complete Bam complexes show there is considerable movement of all 5 proteins (PubMed:27686148, PubMed:26900875, PubMed:26901871). Part of the Bam complex, which is composed of the outer membrane protein BamA, and four lipoproteins BamB, BamC, BamD and BamE. Monomer. Interacts directly with BamA. The Bam complex has the shape of a hat, with the BamA beta-barrel crown in the outer membrane and the periplasmic brim formed by the BamA POTRA domains and the 4 lipoproteins (PubMed:27686148, PubMed:26900875, PubMed:26901871). false 2 P0A940 bamA false 23 P0ABZ6 surA false 2 Cell outer membrane Lipid-anchor With 3 palmitic acid (C16) acyl chains. With 2 palmitic (C16) and 1 stearic (C18) acid acyl chains. Belongs to the BamB family. 3D-structure Cell outer membrane Complete proteome Lipoprotein Membrane Palmitate Reference proteome Signal MQLRKLLLPGLLSVTLLSGCSLFNSEEDVVKMSPLPTVENQFTPTTAWSTSVGSGIGNFY SNLHPALADNVVYAADRAGLVKALNADDGKEIWSVSLAEKDGWFSKEPALLSGGVTVSGG HVYIGSEKAQVYALNTSDGTVAWQTKVAGEALSRPVVSDGLVLIHTSNGQLQALNEADGA VKWTVNLDMPSLSLRGESAPTTAFGAAVVGGDNGRVSAVLMEQGQMIWQQRISQATGSTE IDRLSDVDTTPVVVNGVVFALAYNGNLTALDLRSGQIMWKRELGSVNDFIVDGNRIYLVD QNDRVMALTIDGGVTLWTQSDLLHRLLTSPVLYNGNLVVGDSEGYLHWINVEDGRFVAQQ KVDSSGFQTEPVAADGKLLIQAKDGTVYSITR Q46897 Q2MA73 CAS6_ECOLI CRISPR system Cascade subunit CasE 3.1.-.- CasE endoRNase crRNA endonuclease casE cas6e ygcH b2756 JW2726 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION AS AN ENDORIBONUCLEASE SUBUNIT COFACTOR DISRUPTION PHENOTYPE MUTAGENESIS OF HIS-20 K12 / W3110 / ATCC 27325 / DSM 5911 OPERON STRUCTURE INDUCTION BY LEUO K12 / BW25113 INDUCTION BY H-NS K12 FUNCTION AS AN INHIBITOR OF YGBT (CAS1) INTERACTION WITH YGBT K12 FUNCTION AS AN ENDONUCLEASE ROLE IN PLASMID SILENCING SUBUNIT INDUCTION BY BAER MUTAGENESIS OF HIS-20 DISRUPTION PHENOTYPE K12 / BW25113 FUNCTION IN CASCADE MASS SPECTROMETRY SUBUNIT STRUCTURE BY ELECTRON MICROSCOPY INTERACTION WITH CASA AND CASC DISRUPTION PHENOTYPE K12 STRUCTURE BY ELECTRON MICROSCOPY OF CASCADE WITH AND WITHOUT TARGET RNA RNA-BINDING INTERACTION WITH CASB AND CASC K12 FUNCTION IN R-LOOP FORMATION SUBUNIT K12 / MG1655 / ATCC 47076 SUBUNIT CASCADE DNA-BINDING K12 / MG1655 / ATCC 47076 CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain sequences complementary to antecedent mobile elements and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). CasE is required to process the pre-crRNA into single repeat-spacer units, with an 8-nt 5'-repeat DNA tag that may help other proteins recognize the crRNA. This subunit alone will cleave pre-crRNA, as will CasCDE or CasCE; cleavage does not require divalent metals or ATP. CasCDE alone is also able to form R-loops. Partially inhibits the cleavage of Holliday junctions by YgbT (Cas1). Yields a 5'-hydroxy group and a 2',3'-cyclic phosphate terminus. A component of Cascade, which participates in CRISPR interference, the third stage of CRISPR immunity. Cascade binds both crRNA and in a sequence-specific manner negatively supercoiled dsDNA target. This leads to the formation of an R-loop in which the crRNA binds the target DNA, displacing the noncomplementary strand. Cas3 is recruited to Cascade, nicks target DNA and then unwinds and cleaves the target, leading to DNA degradation and invader neutralization. Does not require a metal cofactor. Part of the Cascade ribonucleoprotein complex, with stoichiometry CasA(1),CasB(2),CasC(6),CasD(1),CasE(1)-crRNA(1). Interacts directly with crRNA, CasA, CasB and CasC. Stable subcomplexes of CasBCDE-crRNA and CasCDE-crRNA also form, both of which are able to bind target dsDNA, and CasCDE is able to form R-loops. CasCDE and CasCE complexes have endonuclease activity. Interacts with YgbT (Cas1). Binding of target ssRNA or dsDNA causes a conformational change in the Cascade complex. Repressed by H-NS, activated by LeuO. Activated by the BaeSR two-component regulatory system, possibly due to envelope stress. Part of the casABCDE-ygbT-ygbF operon. Loss of resistance to bacteriophage lambda infection, loss of plasmid silencing. Decreased levels of crRNA, increased levels of pre-crRNA, prevents pre-crRNA cleavage. Belongs to the CRISPR-associated protein Cas6/Cse3/CasE family. Subtype I-E/Ecoli subfamily. 3D-structure Antiviral defense Complete proteome Endonuclease Hydrolase Nuclease Reference proteome RNA-binding H A MYLSKVIIARAWSRDLYQLHQGLWHLFPNRPDAARDFLFHVEKRNTPEGCHVLLQSAQMP VSTAVATVIKTKQVEFQLQVGVPLYFRLRANPIKTILDNQKRLDSKGNIKRCRVPLIKEA EQIAWLQRKLGNAARVEDVHPISERPQYFSGDGKSGKIQTVCFEGVLTINDAPALIDLVQ QGIGPAKSMGCGLLSLAPL P32719 Q2M6L8 ALSE_ECOLI D-allulose-6-phosphate 3-epimerase 5.1.3.- alsE yjcU b4085 JW4046 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION K12 X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS AND D-GLUCITOL-6-PHOSPHATE FUNCTION CATALYTIC ACTIVITY COFACTOR SUBUNIT MUTAGENESIS OF THR-196; SER-197 AND GLY-198 Catalyzes the reversible epimerization of D-allulose 6-phosphate to D-fructose 6-phosphate. Can also catalyze with lower efficiency the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate. Co(2+) Mn(2+) Zn(2+) Binds 1 divalent metal cation per subunit. Activity is highest with Co(2+) > Mn(2+) > Zn(2+). Carbohydrate degradation; D-allose degradation. Homohexamer. Trimer of dimers. Belongs to the ribulose-phosphate 3-epimerase family. 3D-structure Carbohydrate metabolism Cobalt Complete proteome Isomerase Manganese Metal-binding Reference proteome Zinc MKISPSLMCMDLLKFKEQIEFIDSHADYFHIDIMDGHFVPNLTLSPFFVSQVKKLATKPL DCHLMVTRPQDYIAQLARAGADFITLHPETINGQAFRLIDEIRRHDMKVGLILNPETPVE AMKYYIHKADKITVMTVDPGFAGQPFIPEMLDKLAELKAWREREGLEYEIEVDGSCNQAT YEKLMAAGADVFIVGTSGLFNHAENIDEAWRIMTAQILAAKSEVQPHAKTA P0AEC3 P22763 Q2M902 ARCB_ECOLI Aerobic respiration control sensor protein ArcB 2.7.13.3 arcB b3210 JW5536 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 SEQUENCE REVISION TO 469-470 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 CHARACTERIZATION M15 CHARACTERIZATION M15 PHOSPHORYLATION AT HIS-292 AND HIS-717 MUTAGENESIS OF HIS-292; ASP-576 AND HIS-717 K12 / MC4100 / ATCC 35695 / DSM 6574 SUBCELLULAR LOCATION K12 / MG1655 / ATCC 47076 X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) OF 660-778 X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 659-776 IN COMPLEX WITH CHEY X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 659-776 Member of the two-component regulatory system ArcB/ArcA. Sensor-regulator protein for anaerobic repression of the arc modulon. Activates ArcA via a four-step phosphorelay. ArcB can also dephosphorylate ArcA by a reverse phosphorelay involving His-717 and Asp-576. ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. Cell inner membrane Multi-pass membrane protein Activation requires a sequential transfer of a phosphate group from a His in the primary transmitter domain, to an Asp in the receiver domain and to a His in the secondary transmitter domain. 3D-structure ATP-binding Cell inner membrane Cell membrane Complete proteome Kinase Membrane Nucleotide-binding Phosphoprotein Reference proteome Transcription Transcription regulation Transferase Transmembrane Transmembrane helix Two-component regulatory system H Q D A H Q MKQIRLLAQYYVDLMMKLGLVRFSMLLALALVVLAIVVQMAVTMVLHGQVESIDVIRSIF FGLLITPWAVYFLSVVVEQLEESRQRLSRLVQKLEEMRERDLSLNVQLKDNIAQLNQEIA VREKAEAELQETFGQLKIEIKEREETQIQLEQQSSFLRSFLDASPDLVFYRNEDKEFSGC NRAMELLTGKSEKQLVHLKPADVYSPEAAAKVIETDEKVFRHNVSLTYEQWLDYPDGRKA CFEIRKVPYYDRVGKRHGLMGFGRDITERKRYQDALERASRDKTTFISTISHELRTPLNG IVGLSRILLDTELTAEQEKYLKTIHVSAVTLGNIFNDIIDMDKMERRKVQLDNQPVDFTS FLADLENLSALQAQQKGLRFNLEPTLPLPHQVITDGTRLRQILWNLISNAVKFTQQGQVT VRVRYDEGDMLHFEVEDSGIGIPQDELDKIFAMYYQVKDSHGGKPATGTGIGLAVSRRLA KNMGGDITVTSEQGKGSTFTLTIHAPSVAEEVDDAFDEDDMPLPALNVLLVEDIELNVIV ARSVLEKLGNSVDVAMTGKAALEMFKPGEYDLVLLDIQLPDMTGLDISRELTKRYPREDL PPLVALTANVLKDKQEYLNAGMDDVLSKPLSVPALTAMIKKFWDTQDDEESTVTTEENSK SEALLDIPMLEQYLELVGPKLITDGLAVFEKMMPGYVSVLESNLTAQDKKGIVEEGHKIK GAAGSVGLRHLQQLGQQIQSPDLPAWEDNVGEWIEEMKEEWRHDVEVLKAWVAKATKK P0ABB0 P00822 Q2M852 Q47249 ATPA_ECOLI ATP synthase subunit alpha 7.1.2.2 ATP synthase F1 sector subunit alpha F-ATPase subunit alpha atpA papA uncA b3734 JW3712 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50 SEQUENCE REVISION TO 239-244 PROTEIN SEQUENCE OF 1-8 K12 / W3110 / ATCC 27325 / DSM 5911 PROTEIN SEQUENCE OF 1-12 K12 / EMG2 MUTAGENESIS OF LYS-175 IDENTIFICATION BY 2D-GEL SUBUNIT SUBCELLULAR LOCATION BL21-DE3 X-RAY CRYSTALLOGRAPHY (4.4 ANGSTROMS) OF AN ALPHA(3)/BETA (3)/GAMMA/EPSILON COMPLEX Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an alternating ring which encloses part of the gamma chain. CF(1) is attached to CF(0) by a central stalk formed by the gamma and epsilon chains, while a peripheral stalk is formed by the delta and b chains. P0A6E6 atpC false 3 P0ABB4 atpD false 13 Cell inner membrane Peripheral membrane protein Belongs to the ATPase alpha/beta chains family. 3D-structure ATP synthesis ATP-binding Cell inner membrane Cell membrane CF(1) Complete proteome Direct protein sequencing Hydrogen ion transport Ion transport Membrane Nucleotide-binding Reference proteome Translocase Transport K E K I T I PYAGCA RMPVAL RAA MLQ MQLNSTEISELIKQRIAQFNVVSEAHNEGTIVSVSDGVIRIHGLADCMQGEMISLPGNRY AIALNLERDSVGAVVMGPYADLAEGMKVKCTGRILEVPVGRGLLGRVVNTLGAPIDGKGP LDHDGFSAVEAIAPGVIERQSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQTGKTALAI DAIINQRDSGIKCIYVAIGQKASTISNVVRKLEEHGALANTIVVVATASESAALQYLAPY AGCAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLER AARVNAEYVEAFTKGEVKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLETNLF NAGIRPAVNPGISVSRVGGAAQTKIMKKLSGGIRTALAQYRELAAFSQFASDLDDATRKQ LDHGQKVTELLKQKQYAPMSVAQQSLVLFAAERGYLADVELSKIGSFEAALLAYVDRDHA PLMQEINQTGGYNDEIEGKLKGILDSFKATQSW P0A901 P39281 Q2M6F3 BLC_ECOLI Outer membrane lipoprotein Blc blc yjeL b4149 JW4110 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 / CS520 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 23-177 FUNCTION X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 23-177 IN COMPLEX WITH VACCENIC ACID SUBSTRATE SPECIFICITY SUBUNIT Involved in the storage or transport of lipids necessary for membrane maintenance under stressful conditions. Displays a binding preference for lysophospholipids. Homodimer. Cell outer membrane Lipid-anchor By starvation and high osmolarity. Belongs to the calycin superfamily. Lipocalin family. 3D-structure Cell outer membrane Complete proteome Lipid-binding Lipoprotein Membrane Palmitate Reference proteome Signal MRLLPLVAAATAAFLVVACSSPTPPRGVTVVNNFDAKRYLGTWYEIARFDHRFERGLEKV TATYSLRDDGGLNVINKGYNPDRGMWQQSEGKAYFTGAPTRAALKVSFFGPFYGGYNVIA LDREYRHALVCGPDRDYLWILSRTPTISDEVKQEMLAVATREGFDVSKFIWVQQPGS P25550 Q2M8A5 ASLB_ECOLI Anaerobic sulfatase-maturating enzyme homolog AslB AnSME homolog aslB atsB b3800 JW5594 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] SEQUENCE REVISION TO 391 K12 / MG1655 / ATCC 47076 SEQUENCE REVISION TO 116 AND 117 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 MEMBER OF THE RADICAL SAM SUPERFAMILY NON-INVOLVEMENT IN SULFATASE MATURATION K12 / BW25113 [4Fe-4S] cluster Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. iron-sulfur cluster May bind at least one other iron-sulfur cluster. Belongs to the radical SAM superfamily. Anaerobic sulfatase-maturating enzyme family. Despite its homology to the anaerobic sulfatase-maturating enzymes, it is not involved in Cys-type sulfatase maturation in vivo. 4Fe-4S Complete proteome Iron Iron-sulfur Metal-binding Reference proteome S-adenosyl-L-methionine CA WP L C MLQQVPTRAFHVMAKPSGSDCNLNCDYCFYLEKQSLYREKPVTHMDDDTLEAYVRHYIAA SEPQNEVAFTWQGGEPTLLGLAFYRRAVALQAKYGAGRKISNSFQTNGVLLDDEWCAFLA EHHFLVGLSLDGPPEIHNQYRVTKGGRPTHKLVMRALTLLQKHHVDYNVLVCVNRTSAQQ PLQVYDFLCDAGVEFIQFIPVVERLADETTARDGLKLHAPGDIQGELTEWSVRPEEFGEF LVAIFDHWIKRDVGKIFVMNIEWAFANFVGAPGAVCHHQPTCGRSVIVEHNGDVYACDHY VYPQYRLGNMHQQTIAEMIDSPQQQAFGEDKFKQLPAQCRSCNVLKACWGGCPKHRFMLD ASGKPGLNYLCAGYQRYFRHLPPYLKAMADLLAHGRPASDIMHAHLLVVSK P0AE85 O65939 P32158 Q2M8L0 CPXP_ECOLI Periplasmic protein CpxP ORF_o167 Periplasmic accessory protein CpxP cpxP yiiO b4484 JW5558 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 SEQUENCE REVISION NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 INDUCTION FUNCTION SUBCELLULAR LOCATION INDUCTION DISRUPTION PHENOTYPE K12 / MC4100 INDUCTION K12 / MC4100 FUNCTION SUBUNIT INDUCTION BY ALKALI DOMAIN DEGRADATION BY DEGP MUTAGENESIS OF GLN-55; MET-59; ARG-60; ASP-61 AND GLN-128 K12 / MC4100 FUNCTION DEGRADATION BY DEGP DISRUPTION PHENOTYPE K12 / MC4100 INDUCTION IN PERSISTER CELLS K12 FUNCTION FUNCTION K12 / MG1655 / ATCC 47076 FUNCTION INTERACTION WITH CPXA AND PAPE SUBUNIT SUBCELLULAR LOCATION MUTAGENESIS OF ARG-56 AND ALA-108 K12 / MG1655 / ATCC 47076 X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 40-151 FUNCTION SUBUNIT MUTAGENESIS OF GLN-55 AND GLN-128 K12 / MC4100 X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 21-150 FUNCTION SUBUNIT DOMAIN MUTAGENESIS OF ALA-103; ILE-107 AND ALA-108 Acts as an auxiliary protein in the Cpx two-component envelope stress response system, helping modulate the Cpx response systems response to some inducers (PubMed:25207645, PubMed:16303867). Binds the periplasmic domain of sensor histidine kinase CpxA, inhibiting induction of the Cpx envelope stress response in the absence of inducer; overexpression decreases Cpx pathway activity (PubMed:16166523, PubMed:21317318). Some periplasmic stimulii (shown for P pili subunit PapE and probably 0.3 M NaCl) increase CpxP's susceptibility to DegP, leading to CpxP degradation, inducing the Cpx pathway (PubMed:16166523, PubMed:16303867). Aids in combating extracytoplasmic protein-mediated toxicity (PubMed:9473036, PubMed:16303867, PubMed:21239493). Overexpression leads to degradation by DegP of misfolded P pili subunits in the periplasm (tested using PapE) (PubMed:21239493). Inhibits autophosphorylation of CpxA in reconstituted liposomes by 50% but has no effect on phosphatase activity of CpxA (PubMed:17259177, PubMed:21239493). Has mild protein chaperone activity (PubMed:21317898, PubMed:21239493). Homodimer; it might alter shape slightly at pH 8.0 when Cpx is induced (PubMed:21317318, PubMed:21239493). Binds the periplasmic sensor domain of CpxA (PubMed:16166523, PubMed:21317318, PubMed:21239493, PubMed:25207645). Interaction with CpxA is not seen in vivo when cells are grown in 0.3 M NaCl, or if the misfolded P pili protein PapE is overexpressed (PubMed:25207645). false 2 Periplasm Induced by envelope stress such as overexpression of misfolded periplasmic proteins (PubMed:9351822). Induced by alkaine pH (tested up to pH 8.4) (PubMed:9473036, PubMed:16166523). Induction is decreased in a degP deletion (PubMed:16166523). Transcription is stimulated by the Cpx two-component signal transduction pathway; sigma factor E (rpoE) is not involved (PubMed:9351822, PubMed:9473036, PubMed:10972835). Transcription induced by spheroplasting, which removes the periplasm and thus this protein; if the protein is anchored to the outer surface of the inner membrane induction does not occur (PubMed:10972835). Induced in persister cells (PubMed:16768798). A region in the N-terminus (residues 55-61) probably interacts with the periplasmic sensor domain of CpxA to inhibit its kinase activity and is also important for CpxP stability (PubMed:16166523). The homodimer has an elongated cradle shape; a hydrophobic cleft on the convex face may interact with periplasmic protein PapE (PubMed:21239493). Degraded by DegP; some CpxP mutant proteins are more susceptible to the protease than others (PubMed:16166523). Degradation probably occurs when CpxP is associated with some misfolded proteins; overexpression of PapE leads to DegP-mediated degradation of CpxP and PapE, which requires the N-terminus of PapE. Overexpression of NlpE does not induce this degradation however (PubMed:16303867). Hypersensitive to alkaline pH (greater than pH 8.8) (PubMed:9473036). Increased accumulation and toxicity of overexpressed, misfolded periplasmic proteins (PubMed:16303867). Belongs to the CpxP/Spy family. Translation N-terminally shortened. 3D-structure Complete proteome Periplasm Reference proteome Signal Stress response Q P R Q M T R Q D E V A D G I D I G N A D A G A V Q H MRIVTAAVMASTLAVSSLSHAAEVGSGDNWHPGEELTQRSTQSHMFDGISLTEHQRQQMR DLMQQARHEQPPVNVSELETMHRLVTAENFDENAVRAQAEKMANEQIARQVEMAKVRNQM YRLLTPEQQAVLNEKHQQRMEQLRDVTQWQKSSSLKLLSSSNSRSQ P0AA89 P77793 DOSC_ECOLI Diguanylate cyclase DosC DGC 2.7.7.65 Direct oxygen-sensing cyclase dosC dgcO yddV b1490 JW5241 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION AS A DIGUANYLATE CYCLASE OPERON STRUCTURE K12 / MG1655 / ATCC 47076 K12 / W3110 / ATCC 27325 / DSM 5911 TOB1 RPOS-DEPENDENCE K12 / MC4100 CATALYTIC ACTIVITY HEME COFACTOR O(2)-BINDING INTERACTION WITH DOSP OPERON STRUCTURE INDUCTION RPOS-DEPENDENCE K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION CATALYTIC ACTIVITY ACTIVITY REGULATION DOMAIN O(2)-BINDING CO-BINDING CYANIDE-BINDING IMIDAZOLE-BINDING KINETIC PARAMETERS REDOX POTENTIAL MUTAGENESIS OF TYR-43; GLN-60; HIS-98; HIS-223; ARG-365; ASP-368; ASP-376 AND GLU-377 ABSORPTION SPECTROSCOPY RESONANCE RAMAN SPECTROSCOPY K12 ROLE IN MOTILITY DISRUPTION PHENOTYPE K12 / MG1655 / ATCC 47076 FUNCTION IN REGULATION OF CSGBAC EXPRESSION DISRUPTION PHENOTYPE INDUCTION K12 / MG1655 / ATCC 47076 FUNCTION IN REGULATION OF PGAABCD EXPRESSION DISRUPTION PHENOTYPE MUTAGENESIS OF 376-ASP-GLU-377 K12 / MG1655 / ATCC 47076 MUTAGENESIS OF LEU-65 ABSORPTION SPECTROSCOPY K12 NOMENCLATURE Globin-coupled heme-based oxygen sensor protein displaying diguanylate cyclase (DGC) activity in response to oxygen availability. Thus, catalyzes the synthesis of cyclic diguanylate (c-di-GMP) via the condensation of 2 GTP molecules. Is involved in the modulation of intracellular c-di-GMP levels, in association with DosP which catalyzes the degradation of c-di-GMP (PDE activity). Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria. DosC regulates biofilm formation through the oxygen-dependent activation of the csgBAC operon, which encodes curli structural subunits, while not affecting the expression of the regulatory operon csgDEFG. DosC, but not the other DGCs in E.coli, also promotes the production of the exopolysaccharide poly-N-acetylglucosamine (PNAG) through up-regulation of the expression of the PNAG biosynthetic pgaABCD operon, independently of CsrA. Overexpression leads to an increased level of c-di-GMP, which leads to changes in the cell surface, to abnormal cell division, increased biofilm formation and decreased swimming (the latter 2 in strain W3110). In a strain able to produce cellulose (strain TOB1, a fecal isolate) overexpression leads to an increase in cellulose production. 2 GTP = cyclic di-3',5'-guanylate + 2 diphosphate heme Binds 1 heme group per subunit. The Fe(2+) state binds O(2) and CO while the Fe(3+) state can bind CN(-) and imidazole. Mg(2+) Binds 1 Mg(2+) ion per subunit. Activity depends on O(2)-binding and heme redox state: the Fe(III), Fe(II)-O(2), and Fe(II)-CO complexes of DosC are active forms, whereas Fe(II) and Fe(II)-NO complexes are inactive forms. The Fe(III), Fe(II)-O(2), and Fe(II)-CO complexes of DosC display DGC activity with turnover numbers of 0.066, 0.022, and 0.022 min(-1), respectively. The DGC reaction catalyzed by DosC is the rate-determining step for c-di-GMP homeostasis. Binds O(2), CO, cyanide and imidazole with a dissociation constant of 14 uM, 0.095 uM, 4.7 uM and 0.055 uM, respectively. E(0) is -17 mV. Purine metabolism; 3',5'-cyclic di-GMP biosynthesis. Forms a complex with DosP. By RpoS in the late exponential growth phase and upon entry into stationary phase. Expression is higher at 28 than 37 degrees Celsius. In rich medium DosC and DgcM are the major RpoS-dependent GGDEF-domain containing proteins in the cell, whereas in minimal medium it is the major RpoS-dependent GGDEF-domain containing protein. Highly expressed on solid medium. A member of the dosCP operon. Is composed of an N-terminal sensory globin-fold domain that binds heme and oxygen, and a C-terminal GGDEF diguanylate cyclase domain. Disruption results in a 2.5-fold reduction in surface adhesion, a 3.5-fold reduction in biofilm formation, a large reduction in curli production, a drastic decrease in csgB expression (400-fold reduction in aerobic growth) and in an approximately 3.5-fold reduction in pgaA transcript levels in comparison with wild-type. Disruption partially suppresses the reduced motility of a pdeH disruption; concomitant disruption of dosC, dgcE, dgcQ and dgcN completely restores motility, suggesting these 4 genes, together with the c-di-GMP phosphodiesterase PdeH, form a network that regulates cell motility by altering levels of c-di-GMP. Translation N-terminally extended. 3D-structure Complete proteome GTP-binding Heme Iron Magnesium Metal-binding Nucleotide-binding Reference proteome Transcription Transcription regulation Transferase Y A L Y F W Q A E Q L L G T L M Q H A H A R A D A DE AA D A E A MEMYFKRMKDEWTGLVEQADPPIRAKAAEIAVAHAHYLSIEFYRIVRIDPHAEEFLSNEQ VERQLKSAMERWIINVLSAQVDDVERLIQIQHTVAEVHARIGIPVEIVEMGFRVLKKILY PVIFSSDYSAAEKLQVYHFSINSIDIAMEVMTRAFTFSDSSASKEDENYRIFSLLENAEE EKERQIASILSWEIDIIYKILLDSDLGSSLPLSQADFGLWFNHKGRHYFSGIAEVGHISR LIQDFDGIFNQTMRNTRNLNNRSLRVKFLLQIRNTVSQIITLLRELFEEVSRHEVGMDVL TKLLNRRFLPTIFKREIAHANRTGTPLSVLIIDVDKFKEINDTWGHNTGDEILRKVSQAF YDNVRSSDYVFRYGGDEFIIVLTEASENETLRTAERIRSRVEKTKLKAANGEDIALSLSI GAAMFNGHPDYERLIQIADEALYIAKRRGRNRVELWKASL P75883 Q9Z3A3 GFCC_ECOLI Uncharacterized protein GfcC Group 4 capsule protein C homolog gfcC ymcB b0985 JW0968 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 To E.coli YjbG. In E.coli K12 / MG1655 and K12 / W3110 this operon is silenced by an IS1D insertion in the promoter region. Complete proteome Reference proteome Signal MNKLQSYFIASVLYVMTPHAFAQGTVTIYLPGEQQTLSVGPVENVVQLVTQPQLRDRLWW PGALLTDSAAKAKALKDYQHVMAQLASWEAEADDDVAATIKSVRQQLLNLNITGRLPVKL DPDFVRVDENSNPPLVGDYTLYTVQRPVTITLLGAVSGAGQLPWQAGRSVTDYLQDHPRL AGADKNNVMVITPEGETVVAPVALWNKRHVEPPPGSQLWLGFSAHVLPEKYADLNDQIVS VLTQRVPD P0A932 P75881 GFCE_ECOLI Putative polysaccharide export protein GfcE Group 4 capsule protein E homolog gfcE yccZ b0983 JW0966 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 May be involved in polysaccharide transport. Cell outer membrane Multi-pass membrane protein Belongs to the BexD/CtrA/VexA family. In E.coli K12 / MG1655 and K12 / W3110 this operon is silenced by an IS1D insertion in the promoter region. Cell outer membrane Complete proteome Ion transport Lipoprotein Membrane Palmitate Polysaccharide transport Porin Reference proteome Signal Sugar transport Transmembrane Transmembrane beta strand Transport MKKNIFKFSVLTLAVLSLTACTLVPGQNLSTSNKDVIELPDNQYDLDKMVNIYPVTPGLI DQLRAKPIMSQANPELEQQIANYEYRIGIGDVLMVTVWDHPELTTPAGQYRSASDTGNWV NADGAIFYPYIGRLKVAGKTLTQVRNEITARLDSVIESPQVDVSVAAFRSQKAYVTGEVS KSGQQPITNIPLTIMDAINAAGGLTADADWRNVVLTQNGVKTKVNLYALMQRGDLRQNKL LHPGDILFIPRNDDLKVFVMGEVGKQSTLKMDRSGMTLAEALGNAEGMNQDVADATGIFV IRATQNKQNGKIANIYQLNAKDASAMILGTEFQLEPYDIVYVTTAPLARWNRVISLLVPT ISGVHDLTETSRWIQTWPN P25736 Q2M9P8 END1_ECOLI Endonuclease-1 3.1.21.1 Endonuclease I Endo I endA b2945 JW2912 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 SUBCELLULAR LOCATION CHARACTERIZATION CHARACTERIZATION GENE MAPPING Has double-strand break activity. Endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products. Inhibited by RNA. Periplasm Belongs to the EndA/NucM nuclease family. Complete proteome Endonuclease Hydrolase Nuclease Periplasm Reference proteome Signal MYRYLSIAAVVLSAAFSGPALAEGINSFSQAKAAAVKVHADAPGTFYCGCKINWQGKKGV VDLQSCGYQVRKNENRASRVEWEHVVPAWQFGHQRQCWQDGGRKNCAKDPVYRKMESDMH NLQPSVGEVNGDRGNFMYSQWNGGEGQYGQCAMKVDFKEKAAEPPARARGAIARTYFYMR DQYNLTLSRQQTQLFNAWNKMYPVTDWECERDERIAKVQGNHNPYVQRACQARKS P04128 Q2M5Z9 FIMA1_ECOLI Type-1 fimbrial protein, A chain Type-1A pilin fimA pilA b4314 JW4277 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Fimbriae (also called pili), polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, enable bacteria to colonize the epithelium of specific host organs. false 2 Fimbrium Belongs to the fimbrial protein family. 3D-structure Complete proteome Disulfide bond Fimbrium Reference proteome Signal A T MKIKTLAIVVLSALSLSSTAALAAATTVNGGTVHFKGEVVNAACAVDAGSVDQTVQLGQV RTASLAQEGATSSAVGFNIQLNDCDTNVASKAAVAFLGTAIDAGHTNVLALQSSAAGSAT NVGVQILDRTGAALTLDGATFSSETTLNNGTNTIPFQARYFATGAATPGAANADATFKVQ YQ Q46829 Q2M9U0 BGLA_ECOLI 6-phospho-beta-glucosidase BglA 3.2.1.86 Phospho-beta-glucosidase A bglA bglD yqfC b2901 JW2869 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION AS A GLUCOSIDASE SUBSTRATE SPECIFICITY INDUCTION X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) SUBUNIT Catalyzes the hydrolysis of phosphorylated beta-glucosides into glucose-6-phosphate (G-6-P) and aglycone. It has a high affinity for phosphorylated aromatic beta-glucosides (p-nitrophenyl-beta-glucoside, phenyl beta-glucoside, arbutin), with the exception of phosphorylated salicin, and a low affinity for phosphorylated beta-methyl-glucoside. Apparently, it has only a very limited role in the utilization of external beta-glucosides. 6-phospho-beta-D-glucosyl-(1->4)-D-glucose + H2O = D-glucose + D-glucose 6-phosphate Homotetramer. Constitutively expressed. Belongs to the glycosyl hydrolase 1 family. 3D-structure Complete proteome Glycosidase Hydrolase Reference proteome MIVKKLTLPKDFLWGGAVAAHQVEGGWNKGGKGPSICDVLTGGAHGVPREITKEVLPGKY YPNHEAVDFYGHYKEDIKLFAEMGFKCFRTSIAWTRIFPKGDEAQPNEEGLKFYDDMFDE LLKYNIEPVITLSHFEMPLHLVQQYGSWTNRKVVDFFVRFAEVVFERYKHKVKYWMTFNE INNQRNWRAPLFGYCCSGVVYTEHENPEETMYQVLHHQFVASALAVKAARRINPEMKVGC MLAMVPLYPYSCNPDDVMFAQESMRERYVFTDVQLRGYYPSYVLNEWERRGFNIKMEDGD LDVLREGTCDYLGFSYYMTNAVKAEGGTGDAISGFEGSVPNPYVKASDWGWQIDPVGLRY ALCELYERYQRPLFIVENGFGAYDKVEEDGSINDDYRIDYLRAHIEEMKKAVTYDGVDLM GYTPWGCIDCVSFTTGQYSKRYGFIYVNKHDDGTGDMSRSRKKSFNWYKEVIASNGEKL P0AE91 P08367 Q2M5S0 CREA_ECOLI Protein CreA Catabolite regulation protein A creA yjjD b4397 JW4360 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28 K12 / W3110 / ATCC 27325 / DSM 5911 DISRUPTION PHENOTYPE K12 / DH5-alpha No crucial effects on activation of cre regulon gene expression during aerobic growth on glucose or pyruvate minimal medium or during anaerobic growth on glucose minimal medium. Complete proteome Reference proteome Signal MKYKHLILSLSLIMLGPLAHAEEIGSVDTVFKMIGPDHKIVVEAFDDPDVKNVTCYVSRA KTGGIKGGLGLAEDTSDAAISCQQVGPIELSDRIKNGKAQGEVVFKKRTSLVFKSLQVVR FYDAKRNALAYLAYSDKVVEGSPKNAISAVPVMPWRQ P0A6F9 P05380 Q2M6G2 CH10_ECOLI 10 kDa chaperonin GroES protein Protein Cpn10 groS groES mopB b4142 JW4102 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 61-74 PROTEIN SEQUENCE OF 1-18 PROTEIN SEQUENCE OF 1-11 K12 / W3110 / ATCC 27325 / DSM 5911 PROTEIN SEQUENCE OF 1-12 K12 / EMG2 PROTEIN SEQUENCE OF 1-4 K12 / W3110 / ATCC 27325 / DSM 5911 IDENTIFICATION BY 2D-GEL SUCCINYLATION AT LYS-34 K12 SUBCELLULAR LOCATION K12 / MG1655 / ATCC 47076 X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) STRUCTURE BY NMR OF 19-27 Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. Heptamer of 7 subunits arranged in a ring. false 2 P0A6F5 groL false 31 Cytoplasm Exclusively localized in foci, usually near 1 cell pole in mid-to-late exponential phase; polar localization depends on the minCDE operon. Foci form near midcell. Belongs to the GroES chaperonin family. 3D-structure Cell cycle Cell division Chaperone Complete proteome Cytoplasm Direct protein sequencing Reference proteome S N MNIRPLHDRVIVKRKEVETKSAGGIVLTGSAAAKSTRGEVLAVGNGRILENGEVKPLDVK VGDIVIFNDGYGVKSEKIDNEEVLIMSESDILAIVEA P0A6A8 P02901 Q53352 ACP_ECOLI Acyl carrier protein ACP Cytosolic-activating factor CAF Fatty acid synthase acyl carrier protein acpP b1094 JW1080 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 PROTEIN SEQUENCE OF 2-78 PHOSPHOPANTETHEINYLATION AT SER-37 K12 / E15 PROTEIN SEQUENCE OF 2-78 K12 PROTEIN SEQUENCE OF 2-21 PROTEIN SEQUENCE OF 10-19 AND 63-78 INTERACTION WITH MUKB NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-78 K12 / W3110 / ATCC 27325 / DSM 5911 PARTIAL PROTEIN SEQUENCE K12 / E15 MUTAGENESIS OF SER-37 STRUCTURE BY NMR STRUCTURE BY NMR STRUCTURE BY NMR Carrier of the growing fatty acid chain in fatty acid biosynthesis. Lipid metabolism; fatty acid biosynthesis. Interacts with MukB. P13001 bioH false 3 O32591 espP true 2 P0A7A7 plsB false 4 P0AG24 spoT false 7 P0A8Z3 ybgC false 7 Cytoplasm 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group. Belongs to the acyl carrier protein (ACP) family. 3D-structure Complete proteome Cytoplasm Direct protein sequencing Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism Phosphopantetheine Phosphoprotein Reference proteome S A T N D V I D V H N MSTIEERVKKIIGEQLGVKQEEVTNNASFVEDLGADSLDTVELVMALEEEFDTEIPDEEA EKITTVQAAIDYINGHQA P27254 Q2M9S4 ARGK_ECOLI GTPase ArgK 3.6.5.- G-protein chaperone argK ygfD b2918 JW2885 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] PRELIMINARY CHARACTERIZATION K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION GTPASE ACTIVITY SUBUNIT INTERACTION WITH SCPA X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) Binds and hydrolyzes GTP (PubMed:18950999). Likely functions as a G-protein chaperone that assists AdoCbl cofactor delivery to the methylmalonyl-CoA mutase (MCM) ScpA and reactivation of the enzyme during catalysis. GTP + H2O = GDP + H(+) + phosphate Monomer. Interacts with the methylmalonyl-CoA mutase ScpA. Part of an operon that encodes enzymes converting succinate to propionate. Belongs to the SIMIBI class G3E GTPase family. ArgK/MeaB subfamily. Was originally thought to be a membrane protein kinase involved in phosphorylation of the AO and LAO periplasmic-binding proteins (PubMed:9733684). However, its role needs to be reexamined. 3D-structure ATP-binding Complete proteome GTP-binding Hydrolase Nucleotide-binding Reference proteome S R T A MINEATLAESIRRLRQGERATLAQAMTLVESRHPRHQALSTQLLDAIMPYCGNTLRLGVT GTPGAGKSTFLEAFGMLLIREGLKVAVIAVDPSSPVTGGSILGDKTRMNDLARAEAAFIR PVPSSGHLGGASQRARELMLLCEAAGYDVVIVETVGVGQSETEVARMVDCFISLQIAGGG DDLQGIKKGLMEVADLIVINKDDGDNHTNVAIARHMYESALHILRRKYDEWQPRVLTCSA LEKRGIDEIWHAIIDFKTALTASGRLQQVRQQQSVEWLRKQTEEEVLNHLFANEDFDRYY RQTLLAVKNNTLSPRTGLRQLSEFIQTQYFD P76472 Q2MAN3 ARND_ECOLI Probable 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnD 3.5.1.n3 arnD pmrJ yfbH b2256 JW2250 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION CATALYTIC ACTIVITY K12 / W3110 / ATCC 27325 / DSM 5911 PATHWAY K12 / W3110 / ATCC 27325 / DSM 5911 Catalyzes the deformylation of 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol to 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides (Probable). 4-deoxy-4-formamido-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + H2O = 4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + formate Glycolipid biosynthesis; 4-amino-4-deoxy-alpha-L-arabinose undecaprenyl phosphate biosynthesis; 4-amino-4-deoxy-alpha-L-arabinose undecaprenyl phosphate from UDP-4-deoxy-4-formamido-beta-L-arabinose and undecaprenyl phosphate: step 2/2. Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. Induced by BasR. Belongs to the polysaccharide deacetylase family. ArnD deformylase subfamily. Antibiotic resistance Complete proteome Hydrolase Lipid A biosynthesis Lipid biosynthesis Lipid metabolism Lipopolysaccharide biosynthesis Reference proteome MTKVGLRIDVDTFRGTREGVPRLLEILSKHNIQASIFFSVGPDNMGRHLWRLVKPQFLWK MLRSNAASLYGWDILLAGTAWPGKEIGHANADIIREAAKHHEVGLHAWDHHAWQARSGNW DRQTMIDDIARGLRTLEEIIGQPVTCSAAAGWRADQKVIEAKEAFHLRYNSDCRGAMPFR PLLESGNPGTAQIPVTLPTWDEVIGRDVKAEDFNGWLLNRILRDKGTPVYTIHAEVEGCA YQHNFVDLLKRAAQEGVTFCPLSELLSETLPLGQVVRGNIAGREGWLGCQQIAGSR P31572 CAIB_ECOLI L-carnitine CoA-transferase 2.8.3.21 Crotonobetainyl-CoA:carnitine CoA-transferase caiB yaaN b0038 JW0037 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] PROTEIN SEQUENCE OF 1-19 O44:K74 NUCLEOTIDE SEQUENCE [GENOMIC DNA] O44:K74 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION CATALYTIC ACTIVITY PATHWAY O44:K74 ENZYME ACTIVITY UNDER AEROBIOSIS ATCC 25922 / DSM 1103 / NCIB 12210 O44:K74 X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH COENZYME A ACTIVE SITE Catalyzes the reversible transfer of the CoA moiety from gamma-butyrobetainyl-CoA to L-carnitine to generate L-carnitinyl-CoA and gamma-butyrobetaine. Is also able to catalyze the reversible transfer of the CoA moiety from gamma-butyrobetainyl-CoA or L-carnitinyl-CoA to crotonobetaine to generate crotonobetainyl-CoA. (R)-carnitine + crotonobetainyl-CoA = (R)-carnitinyl-CoA + crotonobetaine (R)-carnitine + gamma-butyrobetainyl-CoA = (R)-carnitinyl-CoA + 4-(trimethylamino)butanoate Amine and polyamine metabolism; carnitine metabolism. Homodimer. Cytoplasm By L-carnitine or crotonobetaine. Some strains of E.coli, such as ATCC 25922, can metabolize carnitine under aerobiosis. Belongs to the CoA-transferase III family. CaiB subfamily. Was originally thought to be an L-carnitine dehydratase. 3D-structure Complete proteome Cytoplasm Direct protein sequencing Reference proteome Transferase V A T A MDHLPMPKFGPLAGLRVVFSGIEIAGPFAGQMFAEWGAEVIWIENVAWADTIRVQPNYPQ LSRRNLHALSLNIFKDEGREAFLKLMETTDIFIEASKGPAFARRGITDEVLWQHNPKLVI AHLSGFGQYGTEEYTNLPAYNTIAQAFSGYLIQNGDVDQPMPAFPYTADYFSGLTATTAA LAALHKVRETGKGESIDIAMYEVMLRMGQYFMMDYFNGGEMCPRMSKGKDPYYAGCGLYK CADGYIVMELVGITQIEECFKDIGLAHLLGTPEIPEGTQLIHRIECPYGPLVEEKLDAWL ATHTIAEVKERFAELNIACAKVLTVPELESNPQYVARESITQWQTMDGRTCKGPNIMPKF KNNPGQIWRGMPSHGMDTAAILKNIGYSENDIQELVSKGLAKVED P76236 CDGI_ECOLI Probable diguanylate cyclase CdgI DGC 2.7.7.65 cdgI yeaI b1785 JW1774 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 INDUCTION RPOS-DEPENDENCE K12 / MC4100 TOPOLOGY [LARGE SCALE ANALYSIS] SUBCELLULAR LOCATION K12 / MG1655 / ATCC 47076 DISRUPTION PHENOTYPE MUTAGENESIS OF GLU-407 NOMENCLATURE Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules. 2 GTP = cyclic di-3',5'-guanylate + 2 diphosphate Mg(2+) Binds 1 Mg(2+) ion per monomer. Purine metabolism; 3',5'-cyclic di-GMP biosynthesis. Homodimer. P0A6Z3 htpG false 3 Cell inner membrane Multi-pass membrane protein Induced by 0.3M NaCl in an RpoS-dependent fashion. Deletion of the gene increases swimming motility and early biofilm formation. Has a EGEVF motif instead of the conserved GG[D/E]EF motif characteristic of active diguanylate cyclases, suggesting that CdgI may be inactive. However, site-directed mutagenesis shows that it is probably a functional diguanylate cyclase. Cell inner membrane Cell membrane Complete proteome GTP-binding Magnesium Membrane Metal-binding Nucleotide-binding Reference proteome Transferase Transmembrane Transmembrane helix E A MIQSTRISMGLFFKYFLSLTKIDPGQNYISLPSIKSSTHIALLFMVSMGTQKLKAQSFFI FSLLLTLILFCITTLYNENTNVKLIPQMNYLMVVVALFFLNAVIFLFMLMKYFTNKQILP TLILSLAFLSGLIYLVETIVIIHKPINGSTLIQTKSNDVSIFYIFRQLSFICLTSLALFC YGKDNILDNNKKKTGILLLALIPFLVFPLLAHNLSSYNADYSLYVVDYCPDNHTATWGIN YTKILVCLWAFLLFFIIMRTRLASELWPLIALLCLASLCCNLLLLTLDEYNYTIWYISRG IEVSSKLFVVSFLIYNIFQELQLSSKLAVHDVLTNIYNRRYFFNSVESLLSRPVVKDFCV MLVDINQFKRINAQWGHRVGDKVLVSIVDIIQQSIRPDDILARLEGEVFGLLFTELNSAQ AKIIAERMRKNVELLTGFSNRYDVPEQMTISIGTVFSTGDTRNISLVMTEADKALREAKS EGGNKVIIHHI P0AE74 P77405 CITT_ECOLI Citrate/succinate antiporter Citrate carrier Citrate transporter citT ybdS b0612 JW0604 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION Responsible for the uptake of citrate in exchange with the efflux of succinate, fumarate or tartrate. Has a relatively broad specificity for C(4)-dicarboxylates and tricarboxylates (PubMed:9696764). Cell inner membrane Multi-pass membrane protein Belongs to the SLC13A/DASS transporter (TC 2.A.47) family. DIT1 subfamily. Antiport Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix Transport MSLAKDNIWKLLAPLVVMGVMFLIPVPDGMPPQAWHYFAVFVAMIVGMILEPIPATAISF IAVTICVIGSNYLLFDAKELADPAFNAQKQALKWGLAGFSSTTVWLVFGAFIFALGYEVS GLGRRIALFLVKFMGKRTLTLGYAIVIIDILLAPFTPSNTARTGGTVFPVIKNLPPLFKS FPNDPSARRIGGYLMWMMVISTSLSSSMFVTGAAPNVLGLEFVSKIAGIQISWLQWFLCF LPVGVILLIIAPWLSYVLYKPEITHSEEVATWAGDELKTMGALTRREWTLIGLVLLSLGL WVFGSEVINATAVGLLAVSLMLALHVVPWKDITRYNSAWNTLVNLATLVVMANGLTRSGF IDWFAGTMSTHLEGFSPNATVIVLVLVFYFAHYLFASLSAHTATMLPVILAVGKGIPGVP MEQLCILLVLSIGIMGCLTPYATGPGVIIYGCGYVKSKDYWRLGAIFGVIYISMLLLVGW PILAMWN Q46925 Q2MA24 CSDA_ECOLI Cysteine desulfurase CsdA 2.8.1.7 Cysteine sulfinate desulfinase CSD 4.4.1.- Selenocysteine lyase 4.4.1.16 csdA ygdJ b2810 JW2781 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] PROTEIN SEQUENCE OF 1-20 FUNCTION CATALYTIC ACTIVITY COFACTOR BIOPHYSICOCHEMICAL PROPERTIES SUBSTRATE SPECIFICITY MUTAGENESIS OF CYS-100; CYS-176 AND CYS-323 K12 / JM109 / ATCC 53323 NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION MUTAGENESIS OF CYS-358 ACTIVE SITE CYS-358 FUNCTION CATALYTIC ACTIVITY COFACTOR ACTIVITY REGULATION INTERACTION WITH CSDE SUBUNIT K12 / MG1655 / ATCC 47076 INDUCTION IN PERSISTER CELLS K12 FUNCTION INTERACTION WITH CSDE DISRUPTION PHENOTYPE K12 / MG1655 / ATCC 47076 FUNCTION ROLE IN CT(6)A37 FORMATION DISRUPTION PHENOTYPE Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine, and transiently retains the released sulfur atom on a cysteine residue, in the form of a persulfide. Can also desulfinate L-cysteine sulfinate, which is the best substrate of the enzyme. Functions as a selenium delivery protein in the pathway for the biosynthesis of selenophosphate. Seems to participate in Fe/S biogenesis by recruiting the SufBCD-SufE proteins. Transfers sulfur to CsdE that increases the cysteine desulfurase activity of CsdA. Can also transfer sulfur directly to TcdA/CsdL in vitro. Appears to support the function of TcdA in the generation of cyclic threonylcarbamoyladenosine at position 37 (ct(6)A37) in tRNAs that read codons beginning with adenine. [sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine AH2 + L-selenocysteine = A + H(+) + hydrogenselenide + L-alanine pyridoxal 5'-phosphate Cysteine desulfurase activity is increased 2-fold in the presence of CsdE. 0.24 mM for L-cysteine sulfinate 1.0 mM for L-selenocysteine 35 mM for L-cysteine 3.3 mM for L-cystine 20 umol/min/mg enzyme with L-cysteine sulfinate as substrate 7.4 umol/min/mg enzyme with L-selenocysteine as substrate 3.4 umol/min/mg enzyme with L-cysteine as substrate 0.017 umol/min/mg enzyme with L-cystine as substrate Optimum pH is around 7.0 and 7.5 for the removal of selenium and sulfur atoms from L-selenocysteine and L-cysteine, respectively. Homodimer. Forms a heterodimer with CsdE. P0AGF2 csdE false 8 P15877 gcd false 2 Q46927 tcdA false 2 Induced in persister cells. Cells lacking this gene display a high decrease in the level of ct(6)A modification in tRNAs, and show the t(6)A modification instead. They also exhibit a fitness defect, are unable to swim, and are more resistant to the norfloxacin antibiotic than the wild-type. Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. Csd subfamily. 3D-structure Complete proteome Direct protein sequencing Lyase Pyridoxal phosphate Reference proteome Transferase C A C A C A C A MNVFNPAQFRAQFPALQDAGVYLDSAATALKPEAVVEATQQFYSLSAGNVHRSQFAEAQR LTARYEAAREKVAQLLNAPDDKTIVWTRGTTESINMVAQCYARPRLQPGDEIIVSVAEHH ANLVPWLMVAQQTGAKVVKLPLNAQRLPDVDLLPELITPRSRILALGQMSNVTGGCPDLA RAITFAHSAGMVVMVDGAQGAVHFPADVQQLDIDFYAFSGHKLYGPTGIGVLYGKSELLE AMSPWLGGGKMVHEVSFDGFTTQSAPWKLEAGTPNVAGVIGLSAALEWLADYDINQAESW SRSLATLAEDALAKRPGFRSFRCQDSSLLAFDFAGVHHSDMVTLLAEYGIALRAGQHCAQ PLLAELGVTGTLRASFAPYNTKSDVDALVNAVDRALELLVD P0A6P9 P08324 Q2MA53 ENO_ECOLI Enolase 4.2.1.11 2-phospho-D-glycerate hydro-lyase 2-phosphoglycerate dehydratase eno b2779 JW2750 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 / JM109 / ATCC 53323 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-123 PROTEIN SEQUENCE OF 2-16 SUBUNIT PROTEIN SEQUENCE OF 2-13 K12 / EMG2 PROTEIN SEQUENCE OF 2-5 K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION CATALYTIC ACTIVITY COFACTOR ACTIVITY REGULATION BIOPHYSICOCHEMICAL PROPERTIES SUBUNIT B PRELIMINARY CHARACTERIZATION PHOSPHORYLATION K12 / JA200 IDENTIFICATION BY 2D-GEL INTERACTION WITH RNASE E SUBSTRATE BINDING AT LYS-342 ACTIVITY REGULATION SECRETION OF SUBSTRATE-BOUND ENOLASE SUBCELLULAR LOCATION MUTAGENESIS OF GLU-168; GLU-209 AND LYS-342 FUNCTION IN MRNA TURNOVER FUNCTION IN THE DECAY OF GLUCOSE TRANSPORTER MRNA K12 / W3110 / ATCC 27325 / DSM 5911 SUBCELLULAR LOCATION PB103 INTERACTION WITH RNASE E SUBCELLULAR LOCATION ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-257 IDENTIFICATION BY MASS SPECTROMETRY K12 / JW1106 K12 / MG1655 / ATCC 47076 X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS COFACTOR SUBUNIT X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH THE MINIMAL BINDING SEGMENT OF RNASE E AND MAGNESIUM IONS SUBUNIT X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH THE MINIMAL BINDING SEGMENT OF RNASE E SUBUNIT IDENTIFICATION BY MASS SPECTROMETRY Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. It is also a component of the RNA degradosome, a multi-enzyme complex involved in RNA processing and messenger RNA degradation. Its interaction with RNase E is important for the turnover of mRNA, in particular on transcripts encoding enzymes of energy-generating metabolic routes. Its presence in the degradosome is required for the response to excess phosphosugar. May play a regulatory role in the degradation of specific RNAs, such as ptsG mRNA, therefore linking cellular metabolic status with post-translational gene regulation. (2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate Mg(2+) Mg(2+) is required for catalysis and for stabilizing the dimer. The covalent binding to the substrate at Lys-342 causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein. Inhibited by fluoride ion. Optimum pH is 8.1. Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. Component of the RNA degradosome, which is a multiprotein complex involved in RNA processing and mRNA degradation. Interacts with the C-terminal region of the endoribonuclease RNase E. Homodimer. false 2 P21513 rne false 17 P0AG07 rpe false 3 Cytoplasm Cytoskeleton Secreted Cell surface Fractions of enolase are present in both the cytoplasm and on the cell surface. As part of the bacterial cytoskeleton in the cytoplasm, is organized as extended coiled structures that wind around the cell, from one cell pole to the other. When covalently bound to the substrate at Lys-342, the inactive enolase is secreted, and remains attached to the cell surface. Phosphorylated on serine residue(s). Belongs to the enolase family. 3D-structure Acetylation Complete proteome Cytoplasm Cytoskeleton Direct protein sequencing Glycolysis Lyase Magnesium Metal-binding Reference proteome Secreted E Q E Q K A Q R K E N K A D I Y PYNGRKEIKGQA RTTVVKRSKARHKTDFI MSKIVKIIGREIIDSRGNPTVEAEVHLEGGFVGMAAAPSGASTGSREALELRDGDKSRFL GKGVTKAVAAVNGPIAQALIGKDAKDQAGIDKIMIDLDGTENKSKFGANAILAVSLANAK AAAAAKGMPLYEHIAELNGTPGKYSMPVPMMNIINGGEHADNNVDIQEFMIQPVGAKTVK EAIRMGSEVFHHLAKVLKAKGMNTAVGDEGGYAPNLGSNAEALAVIAEAVKAAGYELGKD ITLAMDCAASEFYKDGKYVLAGEGNKAFTSEEFTHFLEELTKQYPIVSIEDGLDESDWDG FAYQTKVLGDKIQLVGDDLFVTNTKILKEGIEKGIANSILIKFNQIGSLTETLAAIKMAK DAGYTAVISHRSGETEDATIADLAVGTAAGQIKTGSMSRSDRVAKYNQLIRIEEALGEKA PYNGRKEIKGQA P0ABX5 P75939 FLGG_ECOLI Flagellar basal-body rod protein FlgG Distal rod protein flgG fla FVII flaL b1078 JW1065 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 The basal body constitutes a major portion of the flagellar organelle and consists of four rings (L,P,S, and M) mounted on a central rod. The rod consists of about 26 subunits of FlgG in the distal portion, and FlgB, FlgC and FlgF are thought to build up the proximal portion of the rod with about 6 subunits each. Bacterial flagellum basal body Belongs to the flagella basal body rod proteins family. Bacterial flagellum Complete proteome Reference proteome MISSLWIAKTGLDAQQTNMDVIANNLANVSTNGFKRQRAVFEDLLYQTIRQPGAQSSEQT TLPSGLQIGTGVRPVATERLHSQGNLSQTNNSKDVAIKGQGFFQVMLPDGSSAYTRDGSF QVDQNGQLVTAGGFQVQPAITIPANALSITIGRDGVVSVTQQGQAAPVQVGQLNLTTFMN DTGLESIGENLYTETQSSGAPNESTPGLNGAGLLYQGYVETSNVNVAEELVNMIQVQRAY EINSKAVSTTDQMLQKLTQL P21189 Q8KMX7 Q8KMX8 DPO2_ECOLI DNA polymerase II Pol II 2.7.7.7 polB dinA b0060 JW0059 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] PROTEIN SEQUENCE OF 2-9 K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] SEQUENCE REVISION K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-458 PROTEIN SEQUENCE OF 2-28 K12 STIMULATION BY BETA SLIDING-CLAMP (DNAN) STIMULATION BY BETA SLIDING-CLAMP (DNAN) VARIANT MUTANT ALLELE POLB100 Thought to be involved in DNA repair and/or mutagenesis. Its processivity is enhanced by the beta sliding clamp (dnaN) and clamp loader (PubMed:1999435, PubMed:1534562). a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1) DNA polymerase II activity is regulated by the lexA gene during the SOS response. Belongs to the DNA polymerase type-B family. 3D-structure Complete proteome Direct protein sequencing DNA damage DNA repair DNA-binding DNA-directed DNA polymerase Nucleotidyltransferase Reference proteome SOS response Transferase G D G A EH DD R G N T LDYQRSPLDYEHYLTRQLQPVAEGILPFIEDNFATLMTGQLGLF PGLPTFTTGLRTLSDPPATTRGGGNTPFY MAQAGFILTRHWRDTPQGTEVSFWLATDNGPLQVTLAPQESVAFIPADQVPRAQHILQGE QGFRLTPLALKDFHRQPVYGLYCRAHRQLMNYEKRLREGGVTVYEADVRPPERYLMERFI TSPVWVEGDMHNGTIVNARLKPHPDYRPPLKWVSIDIETTRHGELYCIGLEGCGQRIVYM LGPENGDASSLDFELEYVASRPQLLEKLNAWFANYDPDVIIGWNVVQFDLRMLQKHAERY RLPLRLGRDNSELEWREHGFKNGVFFAQAKGRLIIDGIEALKSAFWNFSSFSLETVAQEL LGEGKSIDNPWDRMDEIDRRFAEDKPALATYNLKDCELVTQIFHKTEIMPFLLERATVNG LPVDRHGGSVAAFGHLYFPRMHRAGYVAPNLGEVPPHASPGGYVMDSRPGLYDSVLVLDY KSLYPSIIRTFLIDPVGLVEGMAQPDPEHSTEGFLDAWFSREKHCLPEIVTNIWHGRDEA KRQGNKPLSQALKIIMNAFYGVLGTTACRFFDPRLASSITMRGHQIMRQTKALIEAQGYD VIYGDTDSTFVWLKGAHSEEEAAKIGRALVQHVNAWWAETLQKQRLTSALELEYETHFCR FLMPTIRGADTGSKKRYAGLIQEGDKQRMVFKGLETVRTDWTPLAQQFQQELYLRIFRNE PYQEYVRETIDKLMAGELDARLVYRKRLRRPLSEYQRNVPPHVRAARLADEENQKRGRPL QYQNRGTIKYVWTTNGPEPLDYQRSPLDYEHYLTRQLQPVAEGILPFIEDNFATLMTGQL GLF P0AEC5 P26607 P77032 BARA_ECOLI Signal transduction histidine-protein kinase BarA 2.7.13.3 barA b2786 JW2757 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 106-918 K12 / W3110 / ATCC 27325 / DSM 5911 CHARACTERIZATION K12 / MC4100 / ATCC 35695 / DSM 6574 CHARACTERIZATION K12 / MC4100 / ATCC 35695 / DSM 6574 CHARACTERIZATION SUBCELLULAR LOCATION K12 / MG1655 / ATCC 47076 Member of the two-component regulatory system UvrY/BarA involved in the regulation of carbon metabolism via the CsrA/CsrB regulatory system. Phosphorylates UvrY, probably via a four-step phosphorelay. ATP + protein L-histidine = ADP + protein N-phospho-L-histidine. P0ABH9 clpA false 3 Cell inner membrane Multi-pass membrane protein Activation requires a sequential transfer of a phosphate group from a His in the primary transmitter domain, to an Asp in the receiver domain and to a His in the secondary transmitter domain. ATP-binding Cell inner membrane Cell membrane Complete proteome Kinase Membrane Nucleotide-binding Phosphoprotein Reference proteome Transcription Transcription regulation Transferase Transmembrane Transmembrane helix Two-component regulatory system MTNYSLRARMMILILAPTVLIGLLLSIFFVVHRYNDLQRQLEDAGASIIEPLAVSTEYGM SLQNRESIGQLISVLHRRHSDIVRAISVYDENNRLFVTSNFHLDPSSMQLGSNVPFPRQL TVTRDGDIMILRTPIISESYSPDESPSSDAKNSQNMLGYIALELDLKSVRLQQYKEIFIS SVMMLFCIGIALIFGWRLMRDVTGPIRNMVNTVDRIRRGQLDSRVEGFMLGELDMLKNGI NSMAMSLAAYHEEMQHNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANM SHELRTPLNGVIGFTRLTLKTELTPTQRDHLNTIERSANNLLAIINDVLDFSKLEAGKLI LESIPFPLRSTLDEVVTLLAHSSHDKGLELTLNIKSDVPDNVIGDPLRLQQIITNLVGNA IKFTENGNIDILVEKRALSNTKVQIEVQIRDTGIGIPERDQSRLFQAFRQADASISRRHG GTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHINLDLNPNIIIEGPSTQCLAGKRLA YVEPNSAAAQCTLDILSETPLEVVYSPTFSALPPAHYDMMLLGIAVTFREPLTMQHERLA KAVSMTDFLMLALPCHAQVNAEKLKQDGIGACLLKPLTPTRLLPALTEFCHHKQNTLLPV TDESKLAMTVMAVDDNPANLKLIGALLEDMVQHVELCDSGHQAVERAKQMPFDLILMDIQ MPDMDGIRACELIHQLPHQQQTPVIAVTAHAMAGQKEKLLGAGMSDYLAKPIEEERLHNL LLRYKPGSGISSRVVTPEVNEIVVNPNATLDWQLALRQAAGKTDLARDMLQMLLDFLPEV RNKVEEQLVGENPEGLVDLIHKLHGSCGYSGVPRMKNLCQLIEQQLRSGTKEEDLEPELL ELLDEMDNVAREASKILG P32720 Q2M6L7 ALSC_ECOLI D-allose transport system permease protein AlsC alsC yjcV b4086 JW4047 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-133 K12 / MG1655 / ATCC 47076 FUNCTION TOPOLOGY [LARGE SCALE ANALYSIS] K12 / MG1655 / ATCC 47076 Part of the binding-protein-dependent transport system AlsBAC for D-allose; probably responsible for the translocation of the substrate across the membrane. Cell inner membrane Multi-pass membrane protein Belongs to the binding-protein-dependent transport system permease family. AraH/RbsC subfamily. Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Sugar transport Transmembrane Transmembrane helix Transport MGFTTRVKSEASEKKPFNFALFWDKYGTFFILAIIVAIFGSLSPEYFLTTNNITQIFVQS SVTVLIGMGEFFAILVAGIDLSVGAILALSGMVTAKLMLAGVDPFLAAMIGGVLVGGALG AINGCLVNWTGLHPFIITLGTNAIFRGITLVISDANSVYGFSFDFVNFFAASVIGIPVPV IFSLIVALILWFLTTRMRLGRNIYALGGNKNSAFYSGIDVKFHILVVFIISGVCAGLAGV VSTARLGAAEPLAGMGFETYAIASAIIGGTSFFGGKGRIFSVVIGGLIIGTINNGLNILQ VQTYYQLVVMGGLIIAAVALDRLISK P60844 P48838 P75827 Q47159 AQPZ_ECOLI Aquaporin Z Bacterial nodulin-like intrinsic protein aqpZ bniP b0875 JW0859 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 / DH5-alpha NUCLEOTIDE SEQUENCE [GENOMIC DNA] LE392 NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION K12 / DH5-alpha FUNCTION SUBUNIT SUBCELLULAR LOCATION MUTAGENESIS OF CYS-9; CYS-20; THR-183 AND ARG-189 K12 / DH5-alpha FUNCTION CHARACTERIZATION OF MEMBRANE SELECTIVITY K12 / DH5-alpha CRYSTALLIZATION SUBUNIT SUBUNIT SUBCELLULAR LOCATION TOPOLOGY TOPOLOGY [LARGE SCALE ANALYSIS] K12 / MG1655 / ATCC 47076 X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) REVIEW Channel that permits osmotically driven movement of water in both directions. It is involved in the osmoregulation and in the maintenance of cell turgor during volume expansion in rapidly growing cells. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity. Homotetramer. false 4 Cell inner membrane Multi-pass membrane protein By extracellular hypoosmotic conditions, especially during the mid-logarithmic phase of growth. Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA). It is a remarkably rigid tetramer that does not dissociate even when solubilized in SDS. Belongs to the MIP/aquaporin (TC 1.A.8) family. 3D-structure Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Repeat Transmembrane Transmembrane helix Transport C S C S T C R V S W C A P L V MFRKLAAECFGTFWLVFGGCGSAVLAAGFPELGIGFAGVALAFGLTVLTMAFAVGHISGG HFNPAVTIGLWAGGRFPAKEVVGYVIAQVVGGIVAAALLYLIASGKTGFDAAASGFASNG YGEHSPGGYSMLSALVVELVLSAGFLLVIHGATDKFAPAGFAPIAIGLALTLIHLISIPV TNTSVNPARSTAVAIFQGGWALEQLWFFWVVPIVGGIIGGLIYRTLLEKRD C1P605 AZUC_ECOLI Uncharacterized protein AzuC azuC b4663 JW1891.1 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 IDENTIFICATION SUBCELLULAR LOCATION INDUCTION K12 / MG1655 / ATCC 47076 INDUCTION K12 / MG1655 / ATCC 47076 SUBCELLULAR LOCATION K12 / MG1655 / ATCC 47076 Cell inner membrane Peripheral membrane protein Constitutively expressed (PubMed:19121005). Repressed in minimal glycerol medium, at low oxygen, induced by H(2)O(2), the thiol reductant diamide, at 45 degrees Celsius and at pH 5.5 (PubMed:19734316) (at protein level). Transcription is repressed by CRP. Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Stress response MKLRKILKSMFNNYCKTFKDVPPGNMFR P75989 Q9R7N5 BLUR_ECOLI HTH-type transcriptional repressor BluR bluR ycgE b1162 JW1149 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 ROLE IN REGULATION OF OMPF IN ASSOCIATION WITH LON DISRUPTION PHENOTYPE K12 / AG100 FUNCTION INTERACTION WITH BLUF DNA-BINDING INDUCTION DISRUPTION PHENOTYPE K12 / MC4100 FUNCTION DNA-BINDING INTERACTION WITH BLUF K12 / W3110 / ATCC 27325 / DSM 5911 Controls the expression of several small proteins that may play a role in biofilm maturation. Binds to and represses the operator of the ycgZ-ymgA-ariR-ymgC operon and also regulates ynaK. Binding is antagonized by BluF upon blue light (470 nm) irradiation. Blue light may increase the affinity of BluF for BluR, allowing it to be released from its operator. Interacts with BluF. P23874 hipA false 2 P0A9P0 lpdA false 2 Expression is strongly activated (7-fold at 16 degrees Celsius compared to 37 degrees) at low temperature. 3- to 20-fold derepression of several genes coding for small proteins including the ycgZ-ymgA-ariR-ymgC operon. While the BluR/F system is induced at low temperatures under blue light irradiation, it is not essential for growth under these conditions. When both lon and bluR are disrupted, levels of OmpF decrease, leading to lower drug susceptibility, with a greater effect at 26 degrees than at 37 degrees Celsius. The mechanism is not yet understood. Complete proteome DNA-binding Reference proteome Repressor Transcription Transcription regulation MAYYSIGDVAERCGINPVTLRAWQRRYGLLKPQRSEGGHRLFDEEDIQRIEEIKRWISNG VPVGKVKALLETTSQDTEDDWSRLQEEMMSILRMANPAKLRARIISLGREYPVDQLINHV YLPVRQRLVLDHNTSRIMSSMFDGALIEYAATSLFEMRRKPGKEAILMAWNVEERARLWL EAWRLSLSGWHISVLADPIESPRPELFPTQTLIVWTGMAPTRRQNELLQHWGEQGYKVIF HAP P0ABR7 P76253 CNTA_ECOLI Carnitine monooxygenase oxygenase subunit 1.14.13.239 Carnitine monooxygenase alpha subunit yeaW b1802 JW5294 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION CATALYTIC ACTIVITY PATHWAY K12 / DH10B Converts carnitine to trimethylamine and malic semialdehyde. Can also use gamma-butyrobetaine, choline and betaine as substrates. (R)-carnitine + H(+) + NADH + O2 = (3R)-3-hydroxy-4-oxobutanoate + H2O + NAD(+) + trimethylamine (R)-carnitine + H(+) + NADPH + O2 = (3R)-3-hydroxy-4-oxobutanoate + H2O + NADP(+) + trimethylamine [2Fe-2S] cluster Binds 1 [2Fe-2S] cluster per subunit. Fe cation Binds 1 Fe cation per subunit. Amine and polyamine metabolism; carnitine metabolism. Composed of an oxygenase subunit (yeaW) and a reductase subunit (yeaX). Belongs to the bacterial ring-hydroxylating dioxygenase alpha subunit family. CntA subfamily. 2Fe-2S Complete proteome Iron Iron-sulfur Metal-binding NAD NADP Oxidoreductase Reference proteome MSNLSPDFVLPENFCANPQEAWTIPARFYTDQNAFEHEKENVFAKSWICVAHSSELANAN DYVTREIIGESIVLVRGRDKVLRAFYNVCPHRGHQLLSGEGKAKNVITCPYHAWAFKLDG NLAHARNCENVANFDSDKAQLVPVRLEEYAGFVFINMDPNATSVEDQLPGLGAKVLEACP EVHDLKLAARFTTRTPANWKNIVDNYLECYHCGPAHPGFSDSVQVDRYWHTMHGNWTLQY GFAKPSEQSFKFEEGTDAAFHGFWLWPCTMLNVTPIKGMMTVIYEFPVDSETTLQNYDIY FTNEELTDEQKSLIEWYRDVFRPEDLRLVESVQKGLKSRGYRGQGRIMADSSGSGISEHG IAHFHNLLAQVFKD P0ACZ4 P30854 EVGA_ECOLI DNA-binding transcriptional activator EvgA evgA b2369 JW2366 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 CHARACTERIZATION CHARACTERIZATION MASS SPECTROMETRY CHARACTERIZATION K12 CHARACTERIZATION K12 / W3104 / ATCC 19020 Member of the two-component regulatory system EvgS/EvgA. Regulates the expression of emrKY operon and yfdX. Seems also to control expression of at least one other multidrug efflux operon. Homodimer. P0AFB8 glnG false 3 P45577 proQ false 3 Cytoplasm Phosphorylated by EvgS. 3D-structure Activator Complete proteome Cytoplasm DNA-binding Phosphoprotein Reference proteome Transcription Transcription regulation Two-component regulatory system MNAIIIDDHPLAIAAIRNLLIKNDIEILAELTEGGSAVQRVETLKPDIVIIDVDIPGVNG IQVLETLRKRQYSGIIIIVSAKNDHFYGKHCADAGANGFVSKKEGMNNIIAAIEAAKNGY CYFPFSLNRFVGSLTSDQQKLDSLSKQEISVMRYILDGKDNNDIAEKMFISNKTVSTYKS RLMEKLECKSLMDLYTFAQRNKIG P76014 DHAL_ECOLI PEP-dependent dihydroxyacetone kinase, ADP-binding subunit DhaL 2.7.1.121 dhaL ycgS b1199 JW5186 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 IDENTIFICATION BY MASS SPECTROMETRY B / BL21 FUNCTION CATALYTIC ACTIVITY OF THE COMPLEX BIOPHYSICOCHEMICAL PROPERTIES ROLE OF ADP BIOPHYSICOCHEMICAL PROPERTIES FUNCTION INDUCTION X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH ADP AND MAGNESIUM ION COFACTOR SUBUNIT X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-210 IN COMPLEX WITH ADP AND MAGNESIUM ION COFACTOR SUBUNIT REACTION MECHANISM X-RAY CRYSTALLOGRAPHY (2.32 ANGSTROMS) OF 2-210 IN COMPLEX WITH DHAR; ADP AND MAGNESIUM COFACTOR INDUCTION SUBUNIT ADP-binding subunit of the dihydroxyacetone kinase, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone (PubMed:11350937). DhaL-ADP is converted to DhaL-ATP via a phosphoryl group transfer from DhaM and transmits it to dihydroxyacetone bound to DhaK (PubMed:11350937). DhaL acts also as coactivator of the transcription activator DhaR by binding to the sensor domain of DhaR (PubMed:15616579). In the presence of dihydroxyacetone, DhaL-ADP displaces DhaK and stimulates DhaR activity (PubMed:15616579). In the absence of dihydroxyacetone, DhaL-ADP is converted by the PTS to DhaL-ATP, which does not bind to DhaR (PubMed:15616579). dihydroxyacetone + phosphoenolpyruvate = dihydroxyacetone phosphate + pyruvate Mg(2+) 45 uM for dihydroxyacetone kcat is 2.8 sec(-1). Values measured with the DhaKLM complex. Complexation with ADP increases the thermal unfolding temperature from 40 to 65 degrees Celsius. Polyol metabolism; glycerol degradation. Homodimer (PubMed:16647083, PubMed:21209328, PubMed:24440518). The dihydroxyacetone kinase complex is composed of a homodimer of DhaM, a homodimer of DhaK and the subunit DhaL (PubMed:16647083, PubMed:21209328). DhaL also forms a complex with DhaR (PubMed:24440518). P76015 dhaK false 2 P76016 dhaR false 3 Cytoplasm Activated by DhaR. Unlike the carbohydrate-specific transporters of the PTS, the complex DhaKML has no transport activity. The tightly bound ADP participates in a double displacement phosphoryl transfer reaction and thus plays the same role as histidines, cysteines and aspartic acids in other phosphoprotein intermediates. 3D-structure ATP-binding Complete proteome Cytoplasm Glycerol metabolism Kinase Magnesium Metal-binding Nucleotide-binding Reference proteome Transferase MSLSRTQIVNWLTRCGDIFSTESEYLTGLDREIGDADHGLNMNRGFSKVVEKLPAIADKD IGFILKNTGMTLLSSVGGASGPLFGTFFIRAAQATQARQSLTLEELYQMFRDGADGVISR GKAEPGDKTMCDVWVPVVESLRQSSEQNLSVPVALEAASSIAESAAQSTITMQARKGRAS YLGERSIGHQDPGATSVMFMMQMLALAAKE P00811 Q2M6F2 AMPC_ECOLI Beta-lactamase 3.5.2.6 Cephalosporinase ampC ampA b4150 JW4111 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] PROTEIN SEQUENCE OF 20-31 K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29 IDENTIFICATION BY 2D-GEL X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGUE X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS) MUTAGENESIS OF SER-80; LYS-83; TYR-166; ASN-168 AND LYS-331 X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) This protein is a serine beta-lactamase with a substrate specificity for cephalosporins. a beta-lactam + H2O = a substituted beta-amino acid Monomer. Periplasm Belongs to the class-C beta-lactamase family. 3D-structure Antibiotic resistance Complete proteome Direct protein sequencing Hydrolase Periplasm Reference proteome Signal S D E G K Q T Y E N D H K A MFKTTLCALLITASCSTFAAPQQINDIVHRTITPLIEQQKIPGMAVAVIYQGKPYYFTWG YADIAKKQPVTQQTLFELGSVSKTFTGVLGGDAIARGEIKLSDPTTKYWPELTAKQWNGI TLLHLATYTAGGLPLQVPDEVKSSSDLLRFYQNWQPAWAPGTQRLYANSSIGLFGALAVK PSGLSFEQAMQTRVFQPLKLNHTWINVPPAEEKNYAWGYREGKAVHVSPGALDAEAYGVK STIEDMARWVQSNLKPLDINEKTLQQGIQLAQSRYWQTGDMYQGLGWEMLDWPVNPDSII NGSDNKIALAARPVKAITPPTPAVRASWVHKTGATGGFGSYVAFIPEKELGIVMLANKNY PNPARVDAAWQILNALQ P0AF08 P21590 Q2MAW5 APBC_ECOLI Iron-sulfur cluster carrier protein mrp b2113 JW2100 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / BHB2600 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Binds and transfers iron-sulfur (Fe-S) clusters to target apoproteins. Can hydrolyze ATP. Homodimer. Belongs to the Mrp/NBP35 ATP-binding proteins family. Translation N-terminally shortened. ATP-binding Complete proteome Hydrolase Iron Iron-sulfur Metal-binding Nucleotide-binding Reference proteome MNEQSQAKSPEALRAMVAGTLANFQHPTLKHNLTTLKALHHVAWMDDTLHVELVMPFVWH SAFEELKEQCSAELLRITGAKAIDWKLSHNIATLKRVKNQPGINGVKNIIAVSSGKGGVG KSSTAVNLALALAAEGAKVGILDADIYGPSIPTMLGAENQRPTSPDGTHMAPIMSHGLAT NSIGYLVTDDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIPV TGAVVVTTPQDIALIDAKKGIVMFEKVEVPVLGIVENMSVHICSNCGHHEPIFGTGGAEK LAEKYHTQLLGQMPLHISLREDLDKGTPTVISRPESEFTAIYRQLADRVAAQLYWQGEVI PGEISFRAV P37028 P77436 BTUF_ECOLI Vitamin B12-binding protein btuF yadT b0158 JW0154 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] SEQUENCE REVISION TO 208 K12 / W3110 / ATCC 27325 / DSM 5911 PROTEIN SEQUENCE OF 1-6 (PRECURSOR PROTEIN) PROTEIN SEQUENCE OF 23-27 FUNCTION SUBCELLULAR LOCATION K12 / MC4100 / ATCC 35695 / DSM 6574 X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 23-266 IN COMPLEX WITH VITAMIN B12 SUBUNIT X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 23-266 IN COMPLEX WITH VITAMIN B12 Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Binds vitamin B12 and delivers it to the periplasmic surface of BtuC. The complex is composed of two ATP-binding proteins (BtuD), two transmembrane proteins (BtuC) and a solute-binding protein (BtuF). P06609 btuC false 9 Periplasm Vitamin B12 is bound in a deep cleft formed at the interface between the two lobes of BtuF. Belongs to the BtuF family. 3D-structure Complete proteome Direct protein sequencing Disulfide bond Periplasm Reference proteome Signal Transport S L MAKSLFRALVALSFLAPLWLNAAPRVITLSPANTELAFAAGITPVGVSSYSDYPPQAQKI EQVSTWQGMNLERIVALKPDLVIAWRGGNAERQVDQLASLGIKVMWVDATSIEQIANALR QLAPWSPQPDKAEQAAQSLLDQYAQLKAQYADKPKKRVFLQFGINPPFTSGKESIQNQVL EVCGGENIFKDSRVPWPQVSREQVLARSPQAIVITGGPDQIPKIKQYWGEQLKIPVIPLT SDWFERASPRIILAAQQLCNALSQVD P0ABA6 P00837 P00838 Q2M851 ATPG_ECOLI ATP synthase gamma chain ATP synthase F1 sector gamma subunit F-ATPase gamma subunit atpG papC uncG b3733 JW3711 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 PROTEIN SEQUENCE OF 2-9; 72-81; 203-208 AND 214-220 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 261-287 SUBUNIT SUBCELLULAR LOCATION BL21-DE3 X-RAY CRYSTALLOGRAPHY (4.4 ANGSTROMS) Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. F-type ATPases have 2 components, CF(1) - the catalytic core - and CF(0) - the membrane proton channel. CF(1) has five subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main subunits: a, b and c. P0A6E6 atpC false 5 Cell inner membrane Peripheral membrane protein Belongs to the ATPase gamma chain family. Sequencing errors. 3D-structure ATP synthesis Cell inner membrane Cell membrane CF(1) Complete proteome Direct protein sequencing Hydrogen ion transport Ion transport Membrane Reference proteome Transport MAGAKEIRSKIASVQNTQKITKAMEMVAASKMRKSQDRMAASRPYAETMRKVIGHLAHGN LEYKHPYLEDRDVKRVGYLVVSTDRGLCGGLNINLFKKLLAEMKTWTDKGVQCDLAMIGS KGVSFFNSVGGNVVAQVTGMGDNPSLSELIGPVKVMLQAYDEGRLDKLYIVSNKFINTMS QVPTISQLLPLPASDDDDLKHKSWDYLYEPDPKALLDTLLRRYVESQVYQGVVENLASEQ AARMVAMKAATDNGGSLIKELQLVYNKARQASITQELTEIVSGAAAV P52107 CSGC_ECOLI Curli assembly protein CsgC csgC b1043 JW1026 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 / MC4100 / ATCC 35695 / DSM 6574 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 INDUCTION K12 / MC4100 Plays a role in the extracellular assembly of CsgA into thin aggregative fimbriae (Tafi) fibers. Assembly may also require CsgE. Tafi are thought to be assembled via an extracellular nucleation-precipitation (ENP) pathway, and possibly also via an intracellular non-CsgC-dependent pathway (By similarity). Periplasm Under control of the CsgD transcription factor, part of the csgBAC/ymdA operon. Belongs to the CsgC/AgfC family. Chaperone Complete proteome Periplasm Reference proteome Signal MNTLLLLAALSSQITFNTTQQGDVYTIIPEVTLTQSCLCRVQILSLREGSSGQSQTKQEK TLSLPANQPIALTKLSLNISPDDRVKIVVTVSDGQSLHLSQQWPPSSEKS P76254 O07970 O07972 CNTB_ECOLI Carnitine monooxygenase reductase subunit 1.14.13.239 Carnitine monooxygenase beta subunit yeaX b1803 JW1792 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION CATALYTIC ACTIVITY PATHWAY K12 / DH10B Converts carnitine to trimethylamine and malic semialdehyde. Can also use gamma-butyrobetaine, choline and betaine as substrates. (R)-carnitine + H(+) + NADH + O2 = (3R)-3-hydroxy-4-oxobutanoate + H2O + NAD(+) + trimethylamine (R)-carnitine + H(+) + NADPH + O2 = (3R)-3-hydroxy-4-oxobutanoate + H2O + NADP(+) + trimethylamine FMN [2Fe-2S] cluster Binds 1 2Fe-2S cluster. Amine and polyamine metabolism; carnitine metabolism. Composed of an oxygenase subunit (yeaW) and a reductase subunit (yeaX). Belongs to the PDR/VanB family. CntB subfamily. 2Fe-2S Complete proteome Flavoprotein FMN Iron Iron-sulfur Metal-binding NAD NADP Oxidoreductase Reference proteome MSDYQMFEVQVSQVEPLTEQVKRFTLVATDGKPLPAFTGGSHVIVQMSDGDNQYSNAYSL LSSPHDTSCYQIAVRLEENSRGGSRFLHQQVKVGDRLTISTPNNLFALIPSARKHLFIAG GIGITPFLSHMAELQHSDVDWQLHYCSRNPESCAFRDELVQHPQAEKVHLHHSSTGTRLE LARLLADIEPGTHVYTCGPEALIEAVRSEAARLDIAADTLHFEQFAIEDKTGDAFTLVLA RSGKEFVVPEEMTILQVIENNKAAKVECLCREGVCGTCETAILEGEADHRDQYFSDEERA SQQSMLICCSRAKGKRLVLDL P37313 Q2M7K2 DPPF_ECOLI Dipeptide transport ATP-binding protein DppF dppF dppE b3540 JW3509 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 / MM500 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Part of the binding-protein-dependent transport system for dipeptides. Probably responsible for energy coupling to the transport system. Cell inner membrane Peripheral membrane protein Belongs to the ABC transporter superfamily. ATP-binding Cell inner membrane Cell membrane Complete proteome Membrane Nucleotide-binding Peptide transport Protein transport Reference proteome Transport LVACFAVDQDENPQR RNDDKSADRQSQHA MSTQEATLQQPLLQAIDLKKHYPVKKGMFAPERLVKALDGVSFNLERGKTLAVVGESGCG KSTLGRLLTMIEMPTGGELYYQGQDLLKHDPQAQKLRRQKIQIVFQNPYGSLNPRKKVGQ ILEEPLLINTSLSKEQRREKALSMMAKVGLKTEHYDRYPHMFSGGQRQRIAIARGLMLDP DVVIADEPVSALDVSVRAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRC VEKGTKDQIFNNPRHPYTQALLSATPRLNPDDRRERIKLSGELPSPLNPPPGCAFNARCR RRFGPCTQLQPQLKDYGGQLVACFAVDQDENPQR P0ABY4 P41050 Q2M9U6 FLAW_ECOLI Flavodoxin 2 fldB b2895 JW2863 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Low-potential electron donor to a number of redox enzymes. FMN Belongs to the flavodoxin family. 3D-structure Complete proteome Electron transport Flavoprotein FMN Reference proteome Transport F C MNMGLFYGSSTCYTEMAAEKIRDIIGPELVTLHNLKDDSPKLMEQYDVLILGIPTWDFGE IQEDWEAVWDQLDDLNLEGKIVALYGLGDQLGYGEWFLDALGMLHDKLSTKGVKFVGYWP TEGYEFTSPKPVIADGQLFVGLALDETNQYDLSDERIQSWCEQILNEMAEHYA P29018 P77275 Q47656 CYDD_ECOLI ATP-binding/permease protein CydD cydD htrD b0887 JW0870 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 48-588 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-152 K12 CHARACTERIZATION SUBCELLULAR LOCATION K12 / MG1655 / ATCC 47076 Somehow involved in the cytochrome D branch of aerobic respiration. Seems to be a component of a transport system. Cell inner membrane Multi-pass membrane protein Required for growth at high temperatures. Belongs to the ABC transporter superfamily. Cysteine exporter (TC 3.A.1.129.1) family. ATP-binding Cell inner membrane Cell membrane Complete proteome Membrane Nucleotide-binding Reference proteome Transmembrane Transmembrane helix Transport A R W S MNKSRQKELTRWLKQQSVISQRWLNISRLLGFVSGILIIAQAWFMARILQHMIMENIPRE ALLLPFTLLVLTFVLRAWVVWLRERVGYHAGQHIRFAIRRQVLDRLQQAGPAWIQGKPAG SWATLVLEQIDDMHDYYARYLPQMALAVSVPLLIVVAIFPSNWAAALILLGTAPLIPLFM ALVGMGAADANRRNFLALARLSGHFLDRLRGMETLRIFGRGEAEIESIRSASEDFRQRTM EVLRLAFLSSGILEFFTSLSIALVAVYFGFSYLGELDFGHYDTGVTLAAGFLALILAPEF FQPLRDLGTFYHAKAQAVGAADSLKTFMETPLAHPQRGEAELASTDPVTIEAEELFITSP EGKTLAGPLNFTLPAGQRAVLVGRSGSGKSSLLNALSGFLSYQGSLRINGIELRDLSPES WRKHLSWVGQNPQLPAATLRDNVLLARPDASEQELQAALDNAWVSEFLPLLPQGVDTPVG DQAARLSVGQAQRVAVARALLNPCSLLLLDEPAASLDAHSEQRVMEALNAASLRQTTLMV THQLEDLADWDVIWVMQDGRIIEQGRYAELSVAGGPFATLLAHRQEEI P15770 Q2M6U6 AROE_ECOLI Shikimate dehydrogenase (NADP(+)) SD SDH 1.1.1.25 aroE b3281 JW3242 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] PROTEIN SEQUENCE OF 1-30 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION SUBUNIT X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH NADP FUNCTION CATALYTIC ACTIVITY BIOPHYSICOCHEMICAL PROPERTIES SUBSTRATE SPECIFICITY SUBUNIT Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). It displays no activity in the presence of NAD. NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH 56 uM for NADP 65 uM for shikimate Kcat is 14.2 min(-1) for dehydrogenase activity with NADP or shikimate. Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. Monomer or homodimer. P31064 yedE false 2 Belongs to the shikimate dehydrogenase family. 3D-structure Amino-acid biosynthesis Aromatic amino acid biosynthesis Complete proteome Direct protein sequencing NADP Oxidoreductase Reference proteome METYAVFGNPIAHSKSPFIHQQFAQQLNIEHPYGRVLAPINDFINTLNAFFSAGGKGANV TVPFKEEAFARADELTERAALAGAVNTLMRLEDGRLLGDNTDGVGLLSDLERLSFIRPGL RILLIGAGGASRGVLLPLLSLDCAVTITNRTVSRAEELAKLFAHTGSIQALSMDELEGHE FDLIINATSSGISGDIPAIPSSLIHPGIYCYDMFYQKGKTPFLAWCEQRGSKRNADGLGM LVAQAAHAFLLWHGVLPDVEPVIKQLQEELSA P0AB71 P11604 Q2M9R7 ALF_ECOLI Fructose-bisphosphate aldolase class 2 FBP aldolase FBPA 4.1.2.13 Fructose-1,6-bisphosphate aldolase Fructose-bisphosphate aldolase class II fbaA fba fda b2925 JW2892 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 / CS520 NUCLEOTIDE SEQUENCE [GENOMIC DNA] PROTEIN SEQUENCE OF 2-27 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 PROTEIN SEQUENCE OF 2-13 K12 / EMG2 PROTEIN SEQUENCE OF 2-5 K12 / W3110 / ATCC 27325 / DSM 5911 MUTAGENESIS OF HIS-108; HIS-111 AND CYS-112 FUNCTION CATALYTIC ACTIVITY SUBSTRATE SPECIFICITY KINETIC PARAMETERS REACTION MECHANISM MUTAGENESIS OF ASN-36; GLN-60; SER-62 AND LYS-326 K12 / MG1655 / ATCC 47076 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-9 IDENTIFICATION BY MASS SPECTROMETRY K12 / JW1106 K12 / MG1655 / ATCC 47076 MALONYLATION AT LYS-9 K12 SUCCINYLATION AT LYS-9; LYS-72; LYS-115; LYS-231; LYS-251; LYS-319; LYS-326 AND LYS-348 K12 X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) IN COMPLEX WITH ZINC X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH ZINC X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ZINC AND TRANSITION STATE ANALOG ACTIVE SITE X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH CADMIUM METAL BINDING SITES Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis. beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate Zn(2+) Binds 2 Zn(2+) ions per subunit. One is catalytic and the other provides a structural contribution. 0.17 mM for fructose-1,6-bisphosphate 0.35 mM for tagatose-1,6-bisphosphate The catalytic efficiency measured with fructose-1,6-bisphosphate as substrate is 1440-fold higher than that with tagatose-1,6-bisphosphate. Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. Homodimer. false 4 P0A6Y8 dnaK false 3 Belongs to the class II fructose-bisphosphate aldolase family. 3D-structure Acetylation Complete proteome Direct protein sequencing Glycolysis Lyase Metal-binding Reference proteome Zinc N A Q A S A S T H A H A C A K A MSKIFDFVKPGVITGDDVQKVFQVAKENNFALPAVNCVGTDSINAVLETAAKVKAPVIVQ FSNGGASFIAGKGVKSDVPQGAAILGAISGAHHVHQMAEHYGVPVILHTDHCAKKLLPWI DGLLDAGEKHFAATGKPLFSSHMIDLSEESLQENIEICSKYLERMSKIGMTLEIELGCTG GEEDGVDNSHMDASALYTQPEDVDYAYTELSKISPRFTIAASFGNVHGVYKPGNVVLTPT ILRDSQEYVSKKHNLPHNSLNFVFHGGSGSTAQEIKDSVSYGVVKMNIDTDTQWATWEGV LNYYKANEAYLQGQLGNPKGEDQPNKKYYDPRVWLRAGQTSMIARLEKAFQELNAIDVL P75734 CHIQ_ECOLI Uncharacterized lipoprotein ChiQ chiQ ybfN b0682 JW0668 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 SUBCELLULAR LOCATION INDUCTION K12 INDUCTION K12 Cell membrane Lipid-anchor In the absence of chitobiose, expression of chiPQ is silenced by the MicM small regulatory RNA (sRNA), which sequesters the ribosome binding site of the chiPQ mRNA by an antisense mechanism. In the presence of chitosugars, the chbBCARFG chitobiose operon is induced and acts as an RNA trap to degrade the constitutively expressed MicM, leading to the translation of chiPQ. Cell membrane Complete proteome Lipoprotein Membrane Palmitate Reference proteome Signal MKKLILIAIMASGLVACAQSTAPQEDSRLKEAYSACINTAQGSPEKIEACQSVLNVLKKE KQHQQFADQESVRVLDYQQCLRATQTGNDQAVKADCDKVWQEIRSNNK P06282 Q2M8L4 CDH_ECOLI CDP-diacylglycerol pyrophosphatase 3.6.1.26 CDP-diacylglycerol phosphatidylhydrolase CDP-diglyceride hydrolase cdh b3918 JW3889 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 a CDP-1,2-diacyl-sn-glycerol + H2O = a 1,2-diacyl-sn-glycero-3-phosphate + CMP + 2 H(+) Phospholipid metabolism; CDP-diacylglycerol degradation; phosphatidate from CDP-diacylglycerol: step 1/1. Cell inner membrane Single-pass membrane protein Belongs to the Cdh family. Cell inner membrane Cell membrane Complete proteome Hydrolase Lipid biosynthesis Lipid metabolism Membrane Phospholipid biosynthesis Phospholipid metabolism Reference proteome Transmembrane Transmembrane helix MKKAGLLFLVMIVIAVVAAGIGYWKLTGEESDTLRKIVLEECLPNQQQNQNPSPCAEVKP NAGYVVLKDLNGPLQYLLMPTYRINGTESPLLTDPSTPNFFWLAWQARDFMSKKYGQPVP DRAVSLAINSRTGRTQNHFHIHISCIRPDVRKQLDNNLANISSRWLPLPGGLRGHEYLAR RVTESELVQRSPFMMLAEEVPEAREHMGRYGLAMVRQSDNSFVLLATQRNLLTLNRASAE EIQDHQCEILR P04395 3MG2_ECOLI DNA-3-methyladenine glycosylase 2 3.2.2.21 3-methyladenine-DNA glycosylase II, inducible TAG II DNA-3-methyladenine glycosidase II DNA-3-methyladenine glycosylase II alkA aidA b2068 JW2053 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] PROTEIN SEQUENCE OF 1-12 AND 14-20 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 CHARACTERIZATION NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-2 X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) MUTAGENESIS X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine, 3-methylguanine, 7-methylguanine, O2-methylthymine, and O2-methylcytosine from the damaged DNA polymer formed by alkylation lesions. Hydrolysis of alkylated DNA, releasing 3-methyladenine, 3-methylguanine, 7-methylguanine and 7-methyladenine. Monomer. P06959 aceF false 2 Up-regulated by methylated Ada in response to the exposure to alkylating agents. Belongs to the alkylbase DNA glycosidase AlkA family. 3D-structure Complete proteome Direct protein sequencing DNA damage DNA repair Hydrolase Reference proteome Q A W A D N D N MYTLNWQPPYDWSWMLGFLAARAVSSVETVADSYYARSLAVGEYRGVVTAIPDIARHTLH INLSAGLEPVAAECLAKMSRLFDLQCNPQIVNGALGRLGAARPGLRLPGCVDAFEQGVRA ILGQLVSVAMAAKLTARVAQLYGERLDDFPEYICFPTPQRLAAADPQALKALGMPLKRAE ALIHLANAALEGTLPMTIPGDVEQAMKTLQTFPGIGRWTANYFALRGWQAKDVFLPDDYL IKQRFPGMTPAQIRRYAERWKPWRSYALLHIWYTEGWQPDEA P31801 CHAA_ECOLI Sodium-potassium/proton antiporter ChaA Na(+)/H(+) exchanger chaA b1216 JW1207 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] FUNCTION IN SODIUM AND CALCIUM EXPORT ACTIVITY REGULATION NM8191 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION IN SODIUM AND CALCIUM EXPORT K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION IN SODIUM EXPORT K12 / W3110 / ATCC 27325 / DSM 5911 TOPOLOGY [LARGE SCALE ANALYSIS] SUBCELLULAR LOCATION K12 / MG1655 / ATCC 47076 FUNCTION IN POTASSIUM EXPORT K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION IN CALCIUM EXPORT K12 Sodium exporter that functions mainly at alkaline pH. Can also function as a potassium/proton and calcium/proton antiporter at alkaline pH. Does not play a major role in calcium export. Pronounced pH dependence. Inhibited by magnesium. Cell inner membrane Multi-pass membrane protein Belongs to the Ca(2+):cation antiporter (CaCA) (TC 2.A.19) family. Antiport Calcium Cell inner membrane Cell membrane Complete proteome Ion transport Membrane Potassium Reference proteome Sodium Transmembrane Transmembrane helix Transport MSNAQEAVKTRHKETSLIFPVLALVVLFLWGSSQTLPVVIAINLLALIGILSSAFSVVRH ADVLAHRLGEPYGSLILSLSVVILEVSLISALMATGDAAPTLMRDTLYSIIMIVTGGLVG FSLLLGGRKFATQYMNLFGIKQYLIALFPLAIIVLVFPMALPAANFSTGQALLVALISAA MYGVFLLIQTKTHQSLFVYEHEDDSDDDDPHHGKPSAHSSLWHAIWLIIHLIAVIAVTKM NASSLETLLDSMNAPVAFTGFLVALLILSPEGLGALKAVLNNQVQRAMNLFFGSVLATIS LTVPVVTLIAFMTGNELQFALGAPEMVVMVASLVLCHISFSTGRTNVLNGAAHLALFAAY LMTIFA P0A6I9 P36679 P75646 Q2MCG6 COAE_ECOLI Dephospho-CoA kinase 2.7.1.24 Dephosphocoenzyme A kinase coaE yacE b0103 JW0100 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 PROTEIN SEQUENCE OF 2-12 CHARACTERIZATION K12 / W3110 / ATCC 27325 / DSM 5911 IDENTIFICATION BY MASS SPECTROMETRY B / BL21 Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A. 3'-dephospho-CoA + ATP = ADP + CoA + H(+) Optimum pH is 8.5. Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5. Monomer. Cytoplasm Belongs to the CoaE family. 3D-structure ATP-binding Coenzyme A biosynthesis Complete proteome Cytoplasm Direct protein sequencing Kinase Nucleotide-binding Reference proteome Transferase ERI DGL A V MRYIVALTGGIGSGKSTVANAFADLGINVIDADIIARQVVEPGAPALHAIADHFGANMIA ADGTLQRRALRERIFANPEEKNWLNALLHPLIQQETQHQIQQATSPYVLWVVPLLVENSL YKKANRVLVVDVSPETQLKRTMQRDDVTREHVEQILAAQATREARLAVADDVIDNNGAPD AIASDVARLHAHYLQLASQFVSQEKP P37686 Q2M7Q2 ADH2_ECOLI Probable alcohol dehydrogenase 1.1.1.1 yiaY b3589 JW5648 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 SEQUENCE REVISION TO 380-383 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 336-383 K12 / MG1655 / ATCC 47076 a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH a secondary alcohol + NAD(+) = a ketone + H(+) + NADH Fe cation Belongs to the iron-containing alcohol dehydrogenase family. Complete proteome Iron NAD Oxidoreductase Reference proteome RAAM AAR MAASTFFIPSVNVIGADSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNI FSVIYDGTQPNPTTENVAAGLKLLKENNCDSVISLGGGSPHDCAKGIALVAANGGDIRDY EGVDRSAKPQLPMIAINTTAGTASEMTRFCIITDEARHIKMAIVDKHVTPLLSVNDSSLM IGMPKSLTAATGMDALTHAIEAYVSIAATPITDACALKAVTMIAENLPLAVEDGSNAKAR EAMAYAQFLAGMAFNNASLGYVHAMAHQLGGFYNLPHGVCNAVLLPHVQVFNSKVAAARL RDCAAAMGVNVTGKNDAEGAEACINAIRELAKKVDIPAGLRDLNVKEEDFAVLATNALKD ACGFTNPIQATHEEIVAIYRAAM P36683 P36648 P75652 Q59382 ACNB_ECOLI Aconitate hydratase B ACN Aconitase 4.2.1.3 (2R,3S)-2-methylisocitrate dehydratase (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase 2-methyl-cis-aconitate hydratase 4.2.1.99 Iron-responsive protein-like IRP-like RNA-binding protein acnB yacI yacJ b0118 JW0114 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] SEQUENCE REVISION K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-131 PROTEIN SEQUENCE OF 1-11 FUNCTION SUBUNIT K12 / W3110 / ATCC 27325 / DSM 5911 PROTEIN SEQUENCE OF 1-12 K12 / EMG2 PROTEIN SEQUENCE OF 1-15 FUNCTION AS A 2-METHYL-ACONITATE HYDRATASE CATALYTIC ACTIVITY SUBSTRATE SPECIFICITY BIOPHYSICOCHEMICAL PROPERTIES PROTEIN SEQUENCE OF 568-663 FUNCTION CATALYTIC ACTIVITY BIOPHYSICOCHEMICAL PROPERTIES MAGNETIC CIRCULAR DICHROISM EPR SPECTROSCOPY FUNCTION DISRUPTION PHENOTYPE FUNCTION AS A RNA-BINDING PROTEIN FUNCTION DISRUPTION PHENOTYPE FUNCTION DISRUPTION PHENOTYPE MUTAGENESIS OF CYS-769 SUBUNIT X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR AND THE SUBSTRATE ANALOGS COFACTOR SUBUNIT Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. Also catalyzes the hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate. The apo form of AcnB functions as a RNA-binding regulatory protein. During oxidative stress inactive AcnB apo-enzyme without iron sulfur clusters binds the acnB mRNA 3' UTRs (untranslated regions), stabilizes acnB mRNA and increases AcnB synthesis, thus mediating a post-transcriptional positive autoregulatory switch. AcnB also decreases the stability of the sodA transcript. citrate = isocitrate (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = 2-methyl-cis-aconitate + H2O [4Fe-4S] cluster Binds 1 [4Fe-4S] cluster per subunit. 11 mM for citrate 0.016 mM for cis-aconitate 0.051 mM for isocitrate (using 0.01-0.8 mM substrate) 19.7 mM for isocitrate (using 0.8-40 mM substrate) 0.21 mM for (2R,3S)-2-methylisocitrate 23.8 umol/min/mg enzyme with citrate as substrate 39.1 umol/min/mg enzyme with cis-aconitate as substrate 5.92 umol/min/mg enzyme using 0.01-0.8 mM isocitrate as substrate 57.8 umol/min/mg enzyme using 0.8-40 mM isocitrate as substrate Optimum pH is 7.4. Organic acid metabolism; propanoate degradation. Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 2/2. Monomer. AcnB can also form a homodimer. The monomer-homodimer transition is dependent on iron availability and the carboxymethylation of C-273 inhibits the dimer formation. Cells lacking this gene are more sensitive to peroxide stress. The acnAB double mutant does not grow on unsupplemented glucose minimal medium and does not respond under aerobic conditions to glutamate. The acnAB double mutant retains a low but significant aconitase activity. AcnB is sensitive to oxidation in vivo. Belongs to the aconitase/IPM isomerase family. 3D-structure 4Fe-4S Complete proteome Direct protein sequencing Iron Iron-sulfur Lyase Metal-binding Reference proteome RNA-binding Tricarboxylic acid cycle C S MLEEYRKHVAERAAEGIAPKPLDANQMAALVELLKNPPAGEEEFLLDLLTNRVPPGVDEA AYVKAGFLAAIAKGEAKSPLLTPEKAIELLGTMQGGYNIHPLIDALDDAKLAPIAAKALS HTLLMFDNFYDVEEKAKAGNEYAKQVMQSWADAEWFLNRPALAEKLTVTVFKVTGETNTD DLSPAPDAWSRPDIPLHALAMLKNAREGIEPDQPGVVGPIKQIEALQQKGFPLAYVGDVV GTGSSRKSATNSVLWFMGDDIPHVPNKRGGGLCLGGKIAPIFFNTMEDAGALPIEVDVSN LNMGDVIDVYPYKGEVRNHETGELLATFELKTDVLIDEVRAGGRIPLIIGRGLTTKAREA LGLPHSDVFRQAKDVAESDRGFSLAQKMVGRACGVKGIRPGAYCEPKMTSVGSQDTTGPM TRDELKDLACLGFSADLVMQSFCHTAAYPKPVDVNTHHTLPDFIMNRGGVSLRPGDGVIH SWLNRMLLPDTVGTGGDSHTRFPIGISFPAGSGLVAFAAATGVMPLDMPESVLVRFKGKM QPGITLRDLVHAIPLYAIKQGLLTVEKKGKKNIFSGRILEIEGLPDLKVEQAFELTDASA ERSAAGCTIKLNKEPIIEYLNSNIVLLKWMIAEGYGDRRTLERRIQGMEKWLANPELLEA DADAEYAAVIDIDLADIKEPILCAPNDPDDARPLSAVQGEKIDEVFIGSCMTNIGHFRAA GKLLDAHKGQLPTRLWVAPPTRMDAAQLTEEGYYSVFGKSGARIEIPGCSLCMGNQARVA DGATVVSTSTRNFPNRLGTGANVFLASAELAAVAALIGKLPTPEEYQTYVAQVDKTAVDT YRYLNFNQLSQYTEKADGVIFQTAV P0AE58 P75622 Q2MCH0 Q47081 CAIF_ECOLI Transcriptional activatory protein CaiF caiF b0034 JW0033 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] O44:K74 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Potential transcriptional activator of carnitine metabolism. Activator Complete proteome Reference proteome Transcription Transcription regulation MCEGYVEKPLYLLIAEWMMAENRWVIAREISIHFDIEHSKAVNTLTYILSEVTEISCEVK MIPNKLEGRGCQCQRLVKVVDIDEQIYARLRNNSREKLVGVRKTPRIPAVPLTELNREQK WQMMLSKSMRR P08204 P78041 ARAB_ECOLI Ribulokinase 2.7.1.16 araB b0063 JW0062 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] SEQUENCE REVISION K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [MRNA] OF 1-14 PROTEIN SEQUENCE OF 2-14 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6 K12 INDUCTION INDUCTION IDENTIFICATION BY 2D-GEL ATP + D-ribulose = ADP + D-ribulose 5-phosphate + H(+) ATP + L-ribulose = ADP + H(+) + L-ribulose 5-phosphate Carbohydrate degradation; L-arabinose degradation via L-ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial route): step 2/3. Induced by arabinose. Transcription is dependent on the transcription factor AraC, the cAMP receptor protein (CRP) and cAMP. Belongs to the ribulokinase family. Arabinose catabolism ATP-binding Carbohydrate metabolism Complete proteome Direct protein sequencing Kinase Nucleotide-binding Reference proteome Transferase T S EA RS G S T A T S C R MAIAIGLDFGSDSVRALAVDCATGEEIATSVEWYPRWQKGQFCDAPNNQFRHHPRDYIES MEAALKTVLAELSVEQRAAVVGIGVDSTGSTPAPIDADGNVLALRPEFAENPNAMFVLWK DHTAVEEAEEITRLCHAPGNVDYSRYIGGIYSSEWFWAKILHVTRQDSAVAQSAASWIEL CDWVPALLSGTTRPQDIRRGRCSAGHKSLWHESWGGLPPASFFDELDPILNRHLPSPLFT DTWTADIPVGTLCPEWAQRLGLPESVVISGGAFDCHMGAVGAGAQPNALVKVIGTSTCDI LIADKQSVGERAVKGICGQVDGSVVPGFIGLEAGQSAFGDIYAWFGRVLGWPLEQLAAQH PELKTQINASQKQLLPALTEAWAKNPSLDHLPVVLDWFNGRRTPNANQRLKGVITDLNLA TDAPLLFGGLIAATAFGARAIMECFTDQGIAVNNVMALGGIARKNQVIMQACCDVLNRPL QIVASDQCCALGAAIFAAVAAKVHADIPSAQQKMASAVEKTLQPCSEQAQRFEQLYRRYQ QWAMSAEQHYLPTSAPAQAAQAVATL P35340 P77251 P77462 AHPF_ECOLI Alkyl hydroperoxide reductase subunit F 1.8.1.- Alkyl hydroperoxide reductase F52A protein ahpF b0606 JW0599 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-162 K12 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53 AND LYS-354 IDENTIFICATION BY MASS SPECTROMETRY K12 / JW1106 K12 / MG1655 / ATCC 47076 Serves to protect the cell against DNA damage by alkyl hydroperoxides. It can use either NADH or NADPH as electron donor for direct reduction of redox dyes or of alkyl hydroperoxides when combined with the AhpC protein. FAD Binds 1 FAD per subunit. Homodimer. The active site is a redox-active disulfide bond. Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family. Translation N-terminally shortened. 3D-structure Acetylation Complete proteome Disulfide bond FAD Flavoprotein NAD NADP Oxidoreductase Redox-active center Reference proteome MLDTNMKTQLKAYLEKLTKPVELIATLDDSAKSAEIKELLAEIAELSDKVTFKEDNSLPV RKPSFLITNPGSNQGPRFAGSPLGHEFTSLVLALLWTGGHPSKEAQSLLEQIRHIDGDFE FETYYSLSCHNCPDVVQALNLMSVLNPRIKHTAIDGGTFQNEITDRNVMGVPAVFVNGKE FGQGRMTLTEIVAKIDTGAEKRAAEELNKRDAYDVLIVGSGPAGAAAAIYSARKGIRTGL MGERFGGQILDTVDIENYISVPKTEGQKLAGALKVHVDEYDVDVIDSQSASKLIPAAVEG GLHQIETASGAVLKARSIIVATGAKWRNMNVPGEDQYRTKGVTYCPHCDGPLFKGKRVAV IGGGNSGVEAAIDLAGIVEHVTLLEFAPEMKADQVLQDKLRSLKNVDIILNAQTTEVKGD GSKVVGLEYRDRVSGDIHNIELAGIFVQIGLLPNTNWLEGAVERNRMGEIIIDAKCETNV KGVFAAGDCTTVPYKQIIIATGEGAKASLSAFDYLIRTKTA P76491 Q2MAM2 5DNU_ECOLI 5'-deoxynucleotidase YfbR 3.1.3.89 5'-deoxyribonucleotidase Nucleoside 5'-monophosphate phosphohydrolase yfbR b2291 JW2288 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION CATALYTIC ACTIVITY SUBSTRATE SPECIFICITY COFACTOR SUBUNIT ACTIVITY REGULATION BIOPHYSICOCHEMICAL PROPERTIES FUNCTION IN THE SYNTHESIS OF THYMIDYLATE X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT ALA-72 IN COMPLEX WITH COBALT ION AND SUBSTRATES FUNCTION CATALYTIC ACTIVITY MUTAGENESIS OF ARG-18; VAL-30; HIS-33; HIS-68; ASP-69; GLU-72; ASP-77; GLU-122 AND ASP-137 BIOPHYSICOCHEMICAL PROPERTIES SUBUNIT Essential component of the deoxycytidine triphosphate (dCTP) pathway for de novo synthesis of thymidylate. Catalyzes the strictly specific dephosphorylation of 2'-deoxyribonucleoside 5'-monophosphates (dAMP, dGMP, dTMP, dUMP, dIMP and dCMP) and does not dephosphorylate 5'-ribonucleotides or ribonucleoside 3'-monophosphates. a 2'-deoxyribonucleoside 5'-phosphate + H2O = a 2'-deoxyribonucleoside + phosphate Co(2+) Mn(2+) Cu(2+) A divalent metal cation. Highest activity with Co(2+), followed by Mn(2+) and Cu(2+). Inhibited by both ribo- and deoxyribonucleoside di- and triphosphates. 0.012 mM for 5'-dAMP 0.047 mM for 5'-dGMP 0.008 mM for 5'-dTMP 0.020 mM for 5'-dUMP 0.017 mM for 5'-dIMP 0.036 mM for 5'-dCMP 2.09 mM for pNPP 0.71 umol/min/mg enzyme with 5'-dAMP as substrate 0.46 umol/min/mg enzyme with 5'-dGMP as substrate 0.37 umol/min/mg enzyme with 5'-dTMP as substrate 0.54 umol/min/mg enzyme with 5'-dUMP as substrate 0.56 umol/min/mg enzyme with 5'-dIMP as substrate 0.53 umol/min/mg enzyme with 5'-dCMP as substrate 1.32 umol/min/mg enzyme with pNPP as substrate Optimum pH is 8.0. Homodimer. Cytoplasm Belongs to the 5DNU family. 3D-structure Cobalt Complete proteome Copper Cytoplasm Hydrolase Manganese Metal-binding Nucleotide-binding Reference proteome R A V A H A H A D A E A E V D A E A D A MKQSHFFAHLSRLKLINRWPLMRNVRTENVSEHSLQVAMVAHALAAIKNRKFGGNVNAER IALLAMYHDASEVLTGDLPTPVKYFNSQIAQEYKAIEKIAQQKLVDMVPEELRDIFAPLI DEHAYSDEEKSLVKQADALCAYLKCLEELAAGNNEFLLAKTRLEATLEARRSQEMDYFME IFVPSFHLSLDEISQDSPL P05100 Q2M7L0 3MG1_ECOLI DNA-3-methyladenine glycosylase 1 3.2.2.20 3-methyladenine-DNA glycosylase I, constitutive TAG I DNA-3-methyladenine glycosidase I DNA-3-methyladenine glycosylase I tag b3549 JW3518 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] PROTEIN SEQUENCE OF 1-29 FUNCTION CATALYTIC ACTIVITY ACTIVITY REGULATION NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 IDENTIFICATION BY 2D-GEL STRUCTURE BY NMR STRUCTURE BY NMR IN COMPLEX WITH ZINC ZINC-BINDING SITES STRUCTURE BY NMR IN COMPLEX WITH 3-METHYLADENINE AND ZINC ZINC-BINDING SITES Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine from the damaged DNA polymer formed by alkylation lesions. Hydrolysis of alkylated DNA, releasing 3-methyladenine. Activity is controlled by product inhibition. P0AFG8 aceE false 2 3D-structure Complete proteome Direct protein sequencing DNA damage DNA repair Hydrolase Metal-binding Reference proteome Zinc MERCGWVSQDPLYIAYHDNEWGVPETDSKKLFEMICLEGQQAGLSWITVLKKRENYRACF HQFDPVKVAAMQEEDVERLVQDAGIIRHRGKIQAIIGNARAYLQMEQNGEPFVDFVWSFV NHQPQVTQATTLSEIPTSTSASDALSKALKKRGFKFVGTTICYSFMQACGLVNDHVVGCC CYPGNKP P52697 P75760 6PGL_ECOLI 6-phosphogluconolactonase 6-P-gluconolactonase Pgl 3.1.1.31 pgl ybhE b0767 JW0750 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 IDENTIFICATION FUNCTION K12 / MG1655 / ATCC 47076 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-287 IDENTIFICATION BY MASS SPECTROMETRY K12 / JW1106 K12 / MG1655 / ATCC 47076 X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) Catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate. 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+) Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3. Belongs to the cycloisomerase 2 family. 3D-structure Acetylation Carbohydrate metabolism Complete proteome Glucose metabolism Hydrolase Reference proteome QVQPMVVSPDKRYLYV RCSRWWSARTNVISML VGQGPMWVVVNAH SGRDQCGWWLTHTKR MKQTVYIASPESQQIHVWNLNHEGALTLTQVVDVPGQVQPMVVSPDKRYLYVGVRPEFRV LAYRIAPDDGALTFAAESALPGSPTHISTDHQGQFVFVGSYNAGNVSVTRLEDGLPVGVV DVVEGLDGCHSANISPDNRTLWVPALKQDRICLFTVSDDGHLVAQDPAEVTTVEGAGPRH MVFHPNEQYAYCVNELNSSVDVWELKDPHGNIECVQTLDMMPENFSDTRWAADIHITPDG RHLYACDRTASLITVFSVSEDGSVLSKEGFQPTETQPRGFNVDHSGKYLIAAGQKSHHIS VYEIVGEQGLLHEKGRYAVGQGPMWVVVNAH P0AEA2 P52103 CSGG_ECOLI Curli production assembly/transport component CsgG csgG b1037 JW1020 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 / MC4100 / ATCC 35695 / DSM 6574 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-49 O78 May be involved in the biogenesis of curli organelles. false 4 P0AE95 csgE false 3 Cell membrane Lipid-anchor Belongs to the CsgG family. 3D-structure Cell membrane Complete proteome Lipoprotein Membrane Palmitate Reference proteome Signal MQRLFLLVAVMLLSGCLTAPPKEAARPTLMPRAQSYKDLTHLPAPTGKIFVSVYNIQDET GQFKPYPASNFSTAVPQSATAMLVTALKDSRWFIPLERQGLQNLLNERKIIRAAQENGTV AINNRIPLQSLTAANIMVEGSIIGYESNVKSGGVGARYFGIGADTQYQLDQIAVNLRVVN VSTGEILSSVNTSKTILSYEVQAGVFRFIDYQRLLEGEVGYTSNEPVMLCLMSAIETGVI FLINDGIDRGLWDLQNKAERQNDILVKYRHMSVPPES P0A8G3 P42605 P42606 P42607 P76662 P76663 P76664 Q2M9B4 UXAC_ECOLI Uronate isomerase 5.3.1.12 Glucuronate isomerase Uronic isomerase uxaC ygjX ygjY ygjZ b3092 JW3063 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 OPERON STRUCTURE INDUCTION K12 / BW25113 D-glucuronate = D-fructuronate aldehydo-D-galacturonate = keto-D-tagaturonate Carbohydrate metabolism; pentose and glucuronate interconversion. Repressed by LeuO and H-NS. Part of the uxaCA operon. Belongs to the metallo-dependent hydrolases superfamily. Uronate isomerase family. Complete proteome Isomerase Reference proteome MTPFMTEDFLLDTEFARRLYHDYAKDQPIFDYHCHLPPQQIAEDYRFKNLYDIWLKGDHY KWRAMRTNGVAERLCTGDASDREKFDAWAATVPHTIGNPLYHWTHLELRRPFGITGKLLS PSTADEIWNECNELLAQDNFSARGIMQQMNVKMVGTTDDPIDSLEHHAEIAKDGSFTIKV LPSWRPDKAFNIEQATFNDYMAKLGEVSDTDIRRFADLQTALTKRLDHFAAHGCKVSDHA LDVVMFAEANEAELDSILARRLAGETLSEHEVAQFKTAVLVFLGAEYARRGWVQQYHIGA LRNNNLRQFKLLGPDVGFDSINDRPMAEELSKLLSKQNEENLLPKTILYCLNPRDNEVLG TMIGNFQGEGMPGKMQFGSGWWFNDQKDGMERQMTQLAQLGLLSRFVGMLTDSRSFLSYT RHEYFRRILCQMIGRWVEAGEAPADINLLGEMVKNICFNNARDYFAIELN P76230 P76911 YDJK_ECOLI Putative metabolite transport protein YdjK ydjK b1775 JW5290 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Cell inner membrane Multi-pass membrane protein Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family. Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix Transport MEQITKPHCGARLDRLPDCRWHSSMFAIVAFGLLVCWSNAVGGLILAQLKALGWTDNSTT ATFSAITTAGMFLGALVGGIIGDKTGRRNAFILYEAIHIASMVVGAFSPNMDFLIACRFV MGVGLGALLVTLFAGFTEYMPGRNRGTWSSRVSFIGNWSYPLCSLIAMGLTPLISAEWNW RVQLLIPAILSLIATALAWRYFPESPRWLESRGRYQEAEKVMRSIEEGVIRQTGKPLPPV VIADDGKAPQAVPYSALLTGVLLKRVILGSCVLIAMNVVQYTLINWLPTIFMTQGINLKD SIVLNTMSMFGAPFGIFIAMLVMDKIPRKTMGVGLLILIAVLGYIYSLQTSMLLITLIGF FLITFVYMYVCYASAVYVPEIWPTEAKLRGSGLANAVGRISGIAAPYAVAVLLSSYGVTG VFILLGAVSIIVAIAIATIGIETKGVSVESLSIDAVANK P0AGA6 P10940 Q2M7Y2 UHPA_ECOLI Transcriptional regulatory protein UhpA uhpA b3669 JW3644 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 PROTEIN SEQUENCE OF 1-20 FUNCTION ACTIVITY REGULATION PHOSPHORYLATION AT ASP-54 MUTAGENESIS OF ASP-54 FUNCTION IDENTIFICATION BY 2D-GEL PHOSPHORYLATION BY UHPB PHOSPHORYLATION AND DEPHOSPHORYLATION BY UHPB Part of the UhpABC signaling cascade that controls the expression of the hexose phosphate transporter UhpT. Activates the transcription of the uhpT gene. Acts by binding specifically to the uhpT promoter region. Phosphorylation by UhpB enhances DNA binding activity. Cytoplasm Phosphorylated and dephosphorylated by UhpB. Activator Complete proteome Cytoplasm Direct protein sequencing DNA-binding Phosphoprotein Reference proteome Transcription Transcription regulation Two-component regulatory system D N MITVALIDDHLIVRSGFAQLLGLEPDLQVVAEFGSGREALAGLPGRGVQVCICDISMPDI SGLELLSQLPKGMATIMLSVHDSPALVEQALNAGARGFLSKRCSPDELIAAVHTVATGGC YLTPDIAIKLASGRQDPLTKRERQVAEKLAQGMAVKEIAAELGLSPKTVHVHRANLMEKL GVSNDVELARRMFDGW P0A8M6 O07992 O07995 P76367 Q8X8U3 YEEX_ECOLI UPF0265 protein YeeX yeeX b2007 JW1989 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 PROTEIN SEQUENCE OF 1-10 K12 Belongs to the UPF0265 family. Complete proteome Direct protein sequencing Reference proteome M D S D METTKPSFQDVLEFVRLFRRKNKLQREIQDVEKKIRDNQKRVLLLDNLSDYIKPGMSVEA IQGIIASMKGDYEDRVDDYIIKNAELSKERRDISKKLKAMGEMKNGEAK P0AD03 O07977 O07979 P76271 YEBS_ECOLI Intermembrane transport protein YebS yebS b1833 JW1822 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 TOPOLOGY [LARGE SCALE ANALYSIS] SUBCELLULAR LOCATION K12 / MG1655 / ATCC 47076 FUNCTION SUBUNIT SUBCELLULAR LOCATION TOPOLOGY INDUCTION Component of a transport pathway that contributes to membrane integrity. May form a complex with YebT. Cell inner membrane Multi-pass membrane protein Induced by a defect in lipopolysaccharide molecules. Belongs to the PqiA family. Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix Transport MALNTPQITPTKKITVRAIGEELPRGDYQRCPQCDMLFSLPEINSHQSAYCPRCQAKIRD GRDWSLTRLAAMAFTMLLLMPFAWGEPLLHIWLLGIRIDANVMQGIWQMTKQGDAITGSM VFFCVIGAPLILVTSIAYLWFGNRLGMNLRPVLLMLERLKEWVMLDIYLVGIGVASIKVQ DYAHIQAGVGLFSFVALVILTTVTLSHLNVEELWERFYPQRPATRRDEKLRVCLGCHFTG YPDQRGRCPRCHIPLRLRRRHSLQKCWAALLASIVLLLPANLLPISIIYLNGGRQEDTIL SGIMSLASSNIAVAGIVFIASILVPFTKVIVMFTLLLSIHFKCQQGLRTRILLLRMVTWI GRWSMLDLFVISLTMSLINRDQILAFTMGPAAFYFGAAVILTILAVEWLDSRLLWDAHES GNARFDD P37766 P76199 P76898 YDIF_ECOLI Acetate CoA-transferase YdiF 2.8.3.8 Short-chain acyl-CoA:acetate CoA-transferase ydiF b1694 JW1684 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64 IDENTIFICATION CoA transferase having broad substrate specificity for short-chain acyl-CoA thioesters with the activity decreasing when the length of the carboxylic acid chain exceeds four carbons. May play a role in short-chain fatty acid metabolism in E.coli (By similarity). acetate + an acyl-CoA = a fatty acid + acetyl-CoA Homotetramer; dimer of dimers. Formation of the covalent enzyme-CoA thioester intermediate proceeds via an unstable anhydride species formed between the carboxylate group of the catalytic glutamate of the enzyme and the carbonyl carbon of the thioester linkage of the substrate. Belongs to the 3-oxoacid CoA-transferase family. Complete proteome Reference proteome Transferase MKPVKPPRINGRVPVLSAQEAVNYIPDEATLCVLGAGGGILEATTLITALADKYKQTQTP RNLSIISPTGLGDRADRGISPLAQEGLVKWALCGHWGQSPRISELAEQNKIIAYNYPQGV LTQTLRAAAAHQPGIISDIGIGTFVDPRQQGGKLNEVTKEDLIKLVEFDNKEYLYYKAIA PDIAFIRATTCDSEGYATFEDEVMYLDALVIAQAVHNNGGIVMMQVQKMVKKATLHPKSV RIPGYLVDIVVVDPDQTQLYGGAPVNRFISGDFTLDDSTKLSLPLNQRKLVARRALFEMR KGAVGNVGVGIADGIGLVAREEGCADDFILTVETGPIGGITSQGIAFGANVNTRAILDMT SQFDFYHGGGLDVCYLSFAEVDQHGNVGVHKFNGKIMGTGGFIDISATSKKIIFCGTLTA GSLKTEITDGKLNIVQEGRVKKFIRELPEITFSGKIALERGLDVRYITERAVFTLKEDGL HLIEIAPGVDLQKDILDKMDFTPVISPELKLMDERLFIDAAMGFVLPEAAH Q46908 Q2MA59 YGCR_ECOLI Putative electron transfer flavoprotein subunit YgcR ygcR b2770 JW5441 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 DISRUPTION PHENOTYPE K12 / MC4100 / ATCC 35695 / DSM 6574 May play a role in a redox process. YgcQ and YgcR form a heterodimer. Cells undergo an apoptotic-like death upon DNA damage characterized by membrane depolarization. Belongs to the ETF beta-subunit/FixA family. Complete proteome Electron transport FAD Flavoprotein Reference proteome Transport MNILLAFKAEPDAGMLAEKEWQAAAQGKSGPDISLLRSLLGADEQAAAALLLAQRKNGTP MSLTALSMGDERALHWLRYLMALGFEEAVLLETAADLRFAPEFVARHIAEWQHQNPLDLI ITGCQSSEGQNGQTPFLLAEMLGWPCFTQVERFTLDALFITLEQRTEHGLRCCRVRLPAV IAVRQCGEVALPVPGMRQRMAAGKAEIIRKTVAAEMPAMQCLQLARAEQRRGATLIDGQT VAEKAQKLWQDYLRQRMQP P76004 YCGM_ECOLI Uncharacterized protein YcgM ycgM b1180 JW1169 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 IDENTIFICATION BY MASS SPECTROMETRY Belongs to the FAH family. 3D-structure Complete proteome Metal-binding Reference proteome MYQHHNWQGALLDYPVSKVVCVGSNYAKHIKEMGSAVPEEPVLFIKPETALCDLRQPLAI PSDFGSVHHEVELAVLIGATLRQATEEHVRKAIAGYGVALDLTLRDVQGKMKKAGQPWEK AKAFDNSCPLSGFIPAAEFTGDPQNTTLSLSVNGEQRQQGTTADMIHKIVPLIAYMSKFF TLKAGDVVLTGTPDGVGPLQSGDELTVTFDGHSLTTRVL Q46906 Q2MA61 YGCP_ECOLI Uncharacterized protein YgcP ygcP b2768 JW2738 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 P0A6Y8 dnaK false 3 To B.subtilis GlpP. Complete proteome Reference proteome MPLLHLLRQNPVIAAVKDNASLQLAIDSECQFISVLYGNICTISNIVKKIKNAGKYAFIH VDLLEGASNKEVVIQFLKLVTEADGIISTKASMLKAARAEGFFCIHRLFIVDSISFHNID KQVAQSNPDCIEILPGCMPKVLGWVTEKIRQPLIAGGLVCDEEDARNAINAGVVALSTTN TGVWTLAKKLL P32687 Q2M6S7 YJBF_ECOLI Uncharacterized lipoprotein YjbF yjbF b4027 JW5711 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Cell membrane Lipid-anchor To E.coli YmcC. Translation N-terminally shortened. Cell membrane Complete proteome Lipoprotein Membrane Palmitate Reference proteome Signal MKRPALILICLLLQACSATTKELGNSLWDSLFGTPGVQLTDDDIQNMPYASQYMQLNGGP QLFVVLAFAEDGQQKWVTQDQATLVTQHGRLVKTLLGGDNLIEVNNLAADPLIKPAQIVD GASWTRTMGWTEYQQVRYATARSVFKWDGTDTVKVGSDETPVRVLDEEVSTDQARWHNRY WIDSEGQIRQSEQYLGADYFPVKTTLIKAAKQ P77460 Q2MBL9 YBCY_ECOLI Putative uncharacterized protein YbcY ybcY b0562 JW0551 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Encoded by the cryptic lambdoid prophage DLP12. Could be the product of a pseudogene. Complete proteome Reference proteome MGVSNRLAWGCPTKEHLLPHFLEHLGNNHLDIGVGTGFYLTHVPESSLISLMDLNEASLN AASTRAGESKIKHKISHDVFEPYPAALHGQFDSISMSYLLHCLPGNISTKSCVIRNAAQA LTDDGTLYGATILGDGVVHNSFGQKLMRIYNQKGIFSNTKDSEEGLTHILSEHFENVKTK VQGTVVMFSASGKK P0DPC4 A0A385XJN9 YTIC_ECOLI Protein YtiC ytiC ytiB b4720 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 IDENTIFICATION INDUCTION DISRUPTION PHENOTYPE K12 / CF7789 IDENTIFICATION INDUCTION Cell inner membrane Single-pass membrane protein Expressed at fairly high levels during late logarithmic and stationary growth (at protein level) (PubMed:28851853). Expressed at low levels in stationary phase (at protein level) (PubMed:29645342). No effect on iraD expression. It is uncertain whether Met-1 or Met-12 is the initiator. Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MPVNGIFDVFDMLSIYIIYKLIVSNNTWLIMRK P37626 Q2M7F0 YHII_ECOLI Uncharacterized protein YhiI yhiI b3487 JW3454 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Complete proteome Reference proteome Signal MDKSKRHLAWWVVGLLAVAAIVAWWLLRPAGVPEGFAVSNGRIEATEVDIASKIAGRIDT ILVKEGKFVREGEVLAKMDTRVLQEQRLEAIAQIKEAQSAVAAAQALLEQRQSETRAAQS LVNQRQAELDSVAKRHTRSRSLAQRGAISAQQLDDDRAAAESARAALESAKAQVSASKAA IEAARTNIIQAQTRVEAAQATERRIAADIDDSELKAPRDGRVQYRVAEPGEVLAAGGRVL NMVDLSDVYMTFFLPTEQAGTLKLGGEARLILDAAPDLRIPATISFVASVAQFTPKTVET SDERLKLMFRVKARIPPELLQQHLEYVKTGLPGVAWVRVNEELPWPDDLVVRLPQ P77216 YBDN_ECOLI Uncharacterized protein YbdN ybdN b0602 JW0595 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Complete proteome Reference proteome MSIYKIPLPLNILEAARERITWTLNTLPRVCVSFSGGKDSGLMLHLTAELARQMGKKICV LFIDWEAQFSCTINYVQSLRELYTDVIEEFYWVALPLTTQNSLSQYQPEWQCWEPDVEWV RQPPQDAITDPDFFCFYQPGMTFEQFVREFAEWFSQKRPAAMMIGIRADESYNRFVAIAS LNKQRFADDKPWTTAAPGGHSWYIYPIYDWKVADIWTWYANHQSLCNPLYNLMYQAGVPL RHMRICEPFGPEQRQGLWLYHVIEPDRWAAMCARVSGVKSGGIYAGHDNHFYGHRKILKP EHLDWQEYALLLLNSMPEKTAEHYRNKIAIYLHWYQKKGIEVPQTQQGDIGAKDIPSWRR ICKVLLNNDYWCRALSFSPTKSKNYQRYNERIKGKRQEWGILCNND P76575 Q2MAH8 YFGJ_ECOLI Uncharacterized protein YfgJ yfgJ b2510 JW5402 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 3D-structure Complete proteome Reference proteome MELHCPQCQHVLDQDNGHARCRSCGEFIEMKALCPDCHQPLQVLKACGAVDYFCQHGHGL ISKKRVEFVLA P0DSH4 YIBY_ECOLI Protein YibY yibY b4796 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 IDENTIFICATION INDUCTION K12 / MG1655 / ATCC 47076 Expressed at low levels in exponential phase in rich medium (at protein level). Encoded antisense to waaL; it is entirely within the waaL coding region. Complete proteome Reference proteome MIIGMLRAHMITSLSPIPTMPSVNINKPKARFLYAI P76537 Q2MAJ4 Q47564 YFEY_ECOLI Uncharacterized protein YfeY yfeY b2432 JW2425 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 74-100 K12 / W3110 / ATCC 27325 / DSM 5911 3D-structure Complete proteome Reference proteome Signal MKSLRLMLCAMPLMLTGCSTMSSVNWSAANPWNWFGSSTKVSEQGVGELTASTPLQEQAI ADALDGDYRLRSGMKTANGNVVRFFEVMKGDNVAMVINGDQGTISRIDVLDSDIPADTGV KIGTPFSDLYSKAFGNCQKADGDDNRAVECKAEGSQHISYQFSGEWRGPEGLMPSDDTLK NWKVSKIIWRR C1P610 YPDK_ECOLI Uncharacterized membrane protein YpdK ypdK b4680 JW2375.1 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 IDENTIFICATION SUBCELLULAR LOCATION INDUCTION K12 / MG1655 / ATCC 47076 INDUCTION K12 / MG1655 / ATCC 47076 SUBCELLULAR LOCATION K12 / MG1655 / ATCC 47076 Cell inner membrane Single-pass membrane protein In exponential phase, strongly repressed by thiol oxidant diamide (at protein level). Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Stress response Transmembrane Transmembrane helix MKYFFMGISFMVIVWAGTFALMI P77585 YPDE_ECOLI Aminopeptidase YpdE 3.4.11.- ypdE b2384 JW2381 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION AS AN AMINOPEPTIDASE CATALYTIC ACTIVITY SUBSTRATE SPECIFICITY COFACTOR Has a broad aminopeptidase activity on non-blocked peptides by progressively cleaving amino acids off the peptide substrate. Aminopeptidase activity stops at the residue before the first proline in the peptide. Cannot cleave when proline is the first N-terminal residue. Co(2+) Ni(2+) Mn(2+) Cu(2+) Binds 2 divalent metal cations per subunit. Can use cobalt, and to a lesser extent, nickel, manganese or copper. Belongs to the peptidase M42 family. Aminopeptidase Cobalt Complete proteome Hydrolase Metal-binding Metalloprotease Protease Reference proteome MDLSLLKALSEADAIASSEQEVRQILLEEADRLQKEVRFDGLGSVLIRLNESTGPKVMIC AHMDEVGFMVRSISREGAIDVLPVGNVRMAARQLQPVRITTREECKIPGLLDGDRQGNDV SAMRVDIGARSYDEVMQAGIRPGDRVTFDTTFQVLPHQRVMGKAFDDRLGCYLLVTLLRE LHDAELPAEVWLVASSSEEVGLRGGQTATRAVSPDVAIVLDTACWAKNFDYGAANHRQIG NGPMLVLSDKSLIAPPKLTAWVETVAAEIGVPLQADMFSNGGTDGGAVHLTGTGVPTVVM GPATRHGHCAASIADCRDILQMQQLLSALIQRLTRETVVQLTDFR P0A8I1 P52050 Q2M9P4 YQGF_ECOLI Putative pre-16S rRNA nuclease 3.1.-.- yqgF ruvX b2949 JW2916 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 DISCUSSION OF POSSIBLE FUNCTION FUNCTION DISRUPTION PHENOTYPE MUTAGENESIS OF ALA-103; SER-105 AND SER-125 FUNCTION MUTAGENESIS OF ASP-9; GLU-96; THR-100; 108-PHE--ALA-115 AND ASP-122 K12 / MG1655 / ATCC 47076 STRUCTURE BY NMR STRUCTURE BY NMR SUBUNIT Involved in the processing of the 5'-end of pre-16S rRNA during 70S ribosome maturation (processing does not occur on total cellular RNA off the ribosome); may be a nuclease (PubMed:25545592). A temperature-sensitive yqgF mutant no longer grows when Rho or NusA are overproduced, and has reduced transcription of genes encoded downstream of Rho terminators; transcription increases again in the presence of the Rho inhibitor bicylomycin (PubMed:22353788). Monomer. Cytoplasm Essential, it cannot be disrupted. Belongs to the YqgF nuclease family. Was originally suggested to be a nuclease that resolves Holliday junction intermediates during genetic recombination. Translation N-terminally shortened. 3D-structure Complete proteome Cytoplasm Hydrolase Nuclease Reference proteome Ribosome biogenesis D A E A T I A I S I D A S A MSGTLLAFDFGTKSIGVAVGQRITGTARPLPAIKAQDGTPDWNIIERLLKEWQPDEIIVG LPLNMDGTEQPLTARARKFANRIHGRFGVEVKLHDERLSTVEARSGLFEQGGYRALNKGK VDSASAVIILESYFEQGY Q47157 YAFO_ECOLI mRNA interferase toxin YafO 3.1.-.- Endoribonuclease YafO Toxin YafO yafO b0233 JW0223 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 INDUCTION OPERON STRUCTURE K12 / MG1655 / ATCC 47076 FUNCTION AS AN MRNA INTERFERASE LARGE RIBOSOMAL SUBUNIT-BINDING K12 / BW25113 FUNCTION AS AN MRNA INTERFERASE INDUCTION OPERON STRUCTURE K12 / MG1655 / ATCC 47076 FUNCTION IN PERSISTENCE DISRUPTION PHENOTYPE K12 / MG1655 / ATCC 47076 Toxic component of a type II toxin-antitoxin (TA) system. A translation-dependent mRNA interferase. Overexpression causes cessation of cell growth and inhibits cell proliferation via inhibition of translation; this blockage is overcome by subsequent expression of antitoxin YafN. Overexpression causes cleavage of a number of mRNAs in a ribosome-dependent fashion. YafO binding to the 50S ribosomal subunit in the translation complex induces mRNA cleavage 3' to the region protected by the ribosome; YafO alone is not able to digest mRNA. mRNA interferases play a role in bacterial persistence to antibiotics; overexpression of this protein induces persisters resistant to ciprofloxacin and ampicillin (PubMed:21788497). Probably forms a complex with the antitoxin YafN which inhibits the mRNA interferase activity. Induced by amino acid starvation, glucose starvation, the DNA cross-linker mitomycin C (SOS response) and when translation is blocked. Induction is decreased in the absence of the Lon protease suggesting, by homology to other toxin-antitoxin systems, that Lon may degrade the YafN antitoxin. Transcription is negatively regulated by the cognate locus, probably by YafN. A member of the dinB-yafNOP operon; it has 2 promoters, 1 upstream of dinB and 1 specific for yafN-yfaO. mRNA interferases play a role in bacterial persistence to antibiotics; as 10 mRNA interferases are successively deleted reduced levels of persisters are generated (PubMed:21788497). Complete proteome DNA damage DNA repair Endonuclease Hydrolase Nuclease Reference proteome RNA-binding SOS response Stress response Toxin-antitoxin system MRVFKTKLIRLQLTAEELDALTADFISYKRDGVLPDIFGRDALYDDSFTWPLIKFERVAH IHLANENNPFPPQLRQFSRTNDEAHLVYCQGAFDEQAWLLIAILKPEPHKLARDNNQMHK IGKMAEAFRMRF P75672 P71281 YAFS_ECOLI Uncharacterized protein YafS yafS b0213 JW0203 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Complete proteome Reference proteome MKPARVPQTVVAPDCWGDLPWGKLYRKALERQLNPWFTKMYGFHLLKIGNLSAEINCEAC AVSHQVNVSAQGMPVQVQADPLHLPFADKSVDVCLLAHTLPWCTDPHRLLREADRVLIDD GWLVISGFNPISFMGLRKLVPVLRKTSPYNSRMFTLMRQLDWLSLLNFEVLHASRFHVLP WNKHGGKLLNAHIPALGCLQLIVARKRTIPLTLNPMKQSKNKPRIRQAVGATRQCRKPQA P77199 P71312 P75700 Q2MC51 Q2MC54 YAIT_ECOLI Putative uncharacterized protein YaiT yaiT b4580 JW0362/JW5051 b0371 b0374 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Could be the product of a pseudogene. The gene coding for this protein is interrupted by a IS3B element between amino acids 486 and 487. Complete proteome Reference proteome Signal MHSWKKKLVVSQLALACTLAITSQANAANYDTWTYIDNPVTALDWDHMDKAGTVDGNYVN YSGFVYYNNTNGDFDQSFNGDTVNGTISTYYLNHDYADSTANQLDISNSVIHGSITSMLP GGYYDRFDADGNNLGGYDFYTDAVVDTHWRDGDVFTLNIANTTIDDDYEALYFTDSYKDG DVTKHTNETFDTSEGVAVNLDVESNINISNNSRVAGIALSQGNTYNETYTTESHTWDNNI SVKDSTVTSGSNYILDSNTYGKTGHFGNSDEPSDYAGPGDVAMSFTASGSDYAMKNNVFL SNSTLMGDVAFTSTWNSNFDPNGHDSNGDGVKDTNGGWTDDSLNVDELNLTLDNGSKWVG QAIYNVAETSAMYDVATNSLTPDATYENNDWKRVVDDKVFQSGVFNVALNNGSEWDTTGR SIVDTLTVNNGSQVNVSESKLTSDTIDLTNGSSLNIGEDGYVDTDHLTINSYSTVALTES TGWGADYNLYANTITVTNGGVLDVNVDQFDTEAFRTDKLELTSGNIADHNGNVVSGVFDI HSSDYVLNADLVNDRTWDTSKSNYGYGIVAMNSDGHLTINGNGDVDNGTELDNSSVDNVV AATGNYKVRIDNATGAGAIADYKDKEIIYVNDVNSNATFSAANKADLGAYTYQAEQRGNT VVLQQMELTDYANMALSIPSANTNIWNLEQDTVGTRLTNSRHGLADNGGAWVSYFGGNFN GDNGTINYDQDVNGIMVGVDTKIDGNNAKWIVGAAAGFAKGDMNDRSGQVDQDSQTAYIY SSAHFANNVFVDGSLSYSHFNNDLSATMSNGTYVDGSTNSDAWGFGLKAGYDFKLGDAGY VTPYGSVSGLFQSGDDYQLSNDMKVDGQSYDSMRYELGVDAGYTFTYSEDQALTPYFKLA YVYDDSNNDNDVNGDSIDNGTEGSAVRVGLGTQFSFTKNFSAYTDANYLGGGDVDQDWSA NVGVKYTW P37008 A0A385XJ59 P77583 Q2MCF4 YAGB_ECOLI Orphan antitoxin YagB yagB b0266 JW0259 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 IDENTIFICATION Putative antitoxin component of a type IV toxin-antitoxin (TA) system; its cognate toxin is unknown. Encoded by the CP4-6 prophage. An insertion element (ISX') seems to have deleted the end of yagB, fusing it to 13 insX' codons to make a 116 fusion pseudogene that may be expressed. The cognate toxin appears to have been deleted at the same time. Belongs to the CbeA/YafW/YfjZ antitoxin family. Translation N-terminally shortened. Complete proteome Reference proteome Toxin-antitoxin system MNKDSTQTWGLKRDITPCFGARLVQEGHRLHFLADRAGFTGSFSEVQTLQLDEAFPHFVA HLELMLLSCELNPRYAHCVTLYRNGLTGEADTLGSHGYVYIAILNRHGFNRHLRVI P37003 P37004 P75738 YBFG_ECOLI Putative uncharacterized protein YbfG ybfG b0691 JW5094/JW5095 b0690 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Could be the product of a pseudogene. Complete proteome Reference proteome MREMNQLVNTEDSAWPIIQNWLKDATNHTELLPVNKDLAETALYQLQVTTKSPMGALVYG SGGLLIDNGXLRIAGSGHPRLPRDPVSWTQRPEFAGVRALPIADDVAGVIFALNGGDLGE DTGCVYYFAPDTLNWESLEVGYSEFLQWALSGDLDTFYENVRWQQWREDVIKLSATEAFT FYPFLWVQSEEARTRKVISLTELWEMQYQMKETFTQ P0DPM9 A0A385XJA7 YKGV_ECOLI Protein YkgV ykgV b4729 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 IDENTIFICATION INDUCTION Expressed at low, approximately equal levels in exponential and stationary phases (at protein level). Complete proteome Reference proteome MSAFKLPDTSQSQLISTAELAKIISYKSQTIRKWLCQDKLPEGLPRPKQINGRHYWLRKD VLDFIDTFSVRESL P75683 P71292 Q2MCF2 YAGG_ECOLI Putative glycoside/cation symporter YagG yagG b0270 JW0263 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 SUBCELLULAR LOCATION TOPOLOGY [LARGE SCALE ANALYSIS] K12 / MG1655 / ATCC 47076 Cell inner membrane Multi-pass membrane protein Belongs to the sodium:galactoside symporter (TC 2.A.2) family. Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Symport Transmembrane Transmembrane helix Transport K N MTQLTMKDKIGYGLGDTACGFVWQATMFLLAYFYTDVFGLSAGIMGTLFLVSRVLDAVTD PLMGLLVDRTRTRHGQFRPFLLWGAIPFGIVCVLTFYTPDFSAQGKIIYACVTYILLTLV YTFVNVPYCAMPGVITADPKERHALQSWRFFLAAAGSLAISGIALPLVSIIGKGDEQVGY FGAMCVLGLSGVVLLYVCFFTTKERYTFEVQPGSSVAKDLKLLLGNSQWRIMCAFKMMAT CSNVVRGGATLYFVKYVMDHPELATQFLLYGSLATMFGSLCSSRLLGRFDRVTAFKWIIV AYSLISLLIFVTPAEHIALIFALNILFLFVFNTTTPLQWLMASDVVDYEESRSGRRLDGL VFSTYLFSLKIGLAIGGAVVGWILAYVNYSASSSVQPVEVLTTIKILFCVVPVVLYAGMF IMLSLYKLTDARVEAISRQLIKHRAAQGEAVPDAATAASH P0ADX7 P23850 Q2M7B1 YHHA_ECOLI Uncharacterized protein YhhA ORFQ yhhA b3448 JW3413 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 P0ABH0 ftsA false 3 Complete proteome Reference proteome Signal MKRLLILTALLPFVGFAQPINTLNNPNQPGYQIPSQQRMQTQMQTQQIQQKGMLNQQLKT QTQLQQQHLENQINNNSQRVLQSQPGERNPARQQMLPNTNGGMLNSNRNPDSSLNQQHML PERRNGDMLNQPSTPQPDIPLKTIGP P76639 Q2M9Y5 Q46788 YGEH_ECOLI Uncharacterized protein YgeH ygeH b2852 JW2820 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Complete proteome DNA-binding Reference proteome TPR repeat Transcription Transcription regulation MDLENKFSYHFLEGLTLTEDGILTQGNEQVYIPQKELGVLIVLLESAGHVVLKDMIIESV WKNIIVSDESLTRCIYSLRCIFEKIGYDRCIETIYRKGYRFSGQVFKTKINEDNTSDYSI AIFPFTTSLNTLDPLILNQELVQIISNKKIDGLYTYPMAATNFCNDHISQNSFLSRFKPD YFVTGRINQNNAVNTLYIELIDAKNLFLIASNHLPVDELHNTSQFIIDNILQTVHKPERS VRLAKQDQGYKNHYLSDEMLAGKKELYDFTPESIYRAMTIFDRLQNKSDIQTLKTECYCL LAECHMSLALHGKSELELAAQKALELLDYVSDITTVDGKILAIMGLITGLSGQAKVSHIL FEQAKIHSTDIASLYYYRALVHFHNEKIEEARICIDKSLQLEPRRRKAVVIKECVDMYVP NPLKNNIKLYYKETESESHRVIIDNILKLKQLTRICMR P39270 Q2M6I3 YJDF_ECOLI Inner membrane protein YjdF yjdF b4121 JW4082 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-57 K12 TOPOLOGY [LARGE SCALE ANALYSIS] K12 / MG1655 / ATCC 47076 Cell inner membrane Multi-pass membrane protein Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MTRTLKPLILNTSALTLTLILIYTGISAHDKLTWLMEVTPVIIVVQLLLATARRYPLTPL LYTLIFLHAIILMVGGQYTYAKVPVGFEVQEWLGLSRNPYDKLGHFFQGLVPALVAREIL VRGMYVRGRKMVAFLVCCVALAISAMYELIEWWAALAMGQGADDFLGTQGDQWDTQSDMF CALLGALTTVIFLARFHCRQLRRFGLITG P0DPC5 A0A385XJP8 YTID_ECOLI Protein YtiD ytiD b4721 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 IDENTIFICATION INDUCTION DISRUPTION PHENOTYPE K12 / CF7789 Expressed at low levels during late logarithmic and stationary growth (at protein level) (PubMed:28851853). No effect on iraD expression (PubMed:28851853). Complete proteome Reference proteome MADYAEINNFPPELSSSGDKYFHLRNYSEYSEYTSGFFLSLMIFIKS P32137 Q2M8H4 YIHP_ECOLI Putative 2,3-dihydroxypropane-1-sulfonate exporter yihP b3877 JW3848 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] SEQUENCE REVISION TO C-TERMINUS K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 TOPOLOGY [LARGE SCALE ANALYSIS] K12 / MG1655 / ATCC 47076 FUNCTION K12 Could be involved in the export of 2,3-dihydroxypropane-1-sulfonate (DHPS). Cell inner membrane Multi-pass membrane protein Belongs to the sodium:galactoside symporter (TC 2.A.2) family. Translation N-terminally shortened. Translation N-terminally shortened. Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Symport Transmembrane Transmembrane helix Transport RTA AHGVIIINDAAGRYKE MSHITTEDPATLRLPFKEKLSYGIGDLASNILLDIGTLYLLKFYTDVLGLPGTYGGIIFL ISKFFTAFTDMGTGIMLDSRRKIGPKGKFRPFILYASFPVTLLAIANFVGTPFDVTGKTV MATILFMLYGLFFSMMNCSYGAMVPAITKNPNERASLAAWRQGGATLGLLLCTVGFVPVM NLIEGNQQLGYIFAATLFSLFGLLFMWICYSGVKERYVETQPANPAQKPGLLQSFRAIAG NRPLFILCIANLCTLGAFNVKLAIQVYYTQYVLNDPILLSYMGFFSMGCIFIGVFLMPAS VRRFGKKKVYIGGLLIWVLGDLLNYFFGGGSVSFVAFSCLAFFGSAFVNSLNWALVSDTV EYGEWRTGVRSEGTVYTGFTFFRKVSQALAGFFPGWMLTQIGYVPNVAQADHTIEGLRQL IFIYPSALAVVTIVAMGCFYSLNEKMYVRIVEEIEARKRTA P0AFV2 P26606 Q2M7H0 YHID_ECOLI Putative magnesium transporter YhiD yhiD yhhE b3508 JW5670 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-148 K12 FUNCTION DISRUPTION PHENOTYPE Could be involved in magnesium uptake. Cell inner membrane Multi-pass membrane protein Deletion of yhiD in addition to mgtA and corA leads to Mg(2+) auxotrophy. Belongs to the MgtC/SapB family. Cell inner membrane Cell membrane Complete proteome Magnesium Membrane Reference proteome Transmembrane Transmembrane helix Transport MTAEFIIRLILAAIACGAIGMERQMRGKGAGLRTHVLIGMGSALFMIVSKYGFADVLSLD HVGLDPSRIAAQVVTGVGFIGAGNILVRNQNIVGLTTAADIWVTAAIGMVIGSGMYELGI YGSVMTLLVLEVFHQLTFRLMNKNYHLQLTLVNGNTVSMLDWFKQQKIKTDLVSLQENED HEVVAIDIQLHATTSIEDLLRLLKGMAGVKGVSIS P76055 Q2MBE9 Q47558 TTCA_ECOLI tRNA-cytidine(32) 2-sulfurtransferase 2.8.1.- Two-thiocytidine biosynthesis protein A tRNA 2-thiocytidine biosynthesis protein TtcA ttcA ydaO b1344 JW1338 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40 K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION DISRUPTION PHENOTYPE PATHWAY GRB105 CRYSTALLIZATION FUNCTION CATALYTIC ACTIVITY COFACTOR SUBUNIT MUTAGENESIS OF CYS-45; CYS-122; CYS-125; CYS-191; CYS-210 AND CYS-213 REACTION MECHANISM Catalyzes the ATP-dependent 2-thiolation of cytidine in position 32 of tRNA, to form 2-thiocytidine (s(2)C32). The sulfur atoms are provided by the cysteine/cysteine desulfurase (IscS) system. [4Fe-4S] cluster Binds 1 [4Fe-4S] cluster per subunit. The cluster is chelated by three Cys residues, the fourth Fe has a free coordination site that may bind a sulfur atom transferred from the persulfide of IscS. The [4Fe-4S] cluster is highly sensitive to oxygen and prone to decompose into the [2Fe-2S] form and further degraded forms. Mg(2+) tRNA modification. Homodimer. Cytoplasm Loss of cytidine thiolation in position 32 in tRNA. The thiolation reaction likely consists of two steps: a first activation step by ATP to form an adenylated intermediate of the target base of tRNA, and a second nucleophilic substitution step of the sulfur (S) atom supplied by the hydrosulfide attached to the Fe-S cluster. Belongs to the TtcA family. 4Fe-4S ATP-binding Complete proteome Cytoplasm Iron Iron-sulfur Magnesium Metal-binding Nucleotide-binding Reference proteome RNA-binding Transferase tRNA processing tRNA-binding C A C A C A C A C A C A E A MQENQQITKKEQYNLNKLQKRLRRNVGEAIADFNMIEEGDRIMVCLSGGKDSYTMLEILR NLQQSAPINFSLVAVNLDQKQPGFPEHVLPEYLEKLGVEYKIVEENTYGIVKEKIPEGKT TCSLCSRLRRGILYRTATELGATKIALGHHRDDILQTLFLNMFYGGKMKGMPPKLMSDDG KHIVIRPLAYCREKDIQRFADAKAFPIIPCNLCGSQPNLQRQVIADMLRDWDKRYPGRIE TMFSAMQNVVPSHLCDTNLFDFKGITHGSEVVNGGDLAFDREEIPLQPACWQPEEDENQL DELRLNVVEVK P64519 P76328 Q2MB02 YODD_ECOLI Uncharacterized protein YodD yodD b1953 JW5317 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Complete proteome Reference proteome MKTAKEYSDTAKREVSVDVDALLAAINEISESEVHRSQNDSEHVSVDGREYHTWRELADA FELDIHDFSVSEVNR P07604 TYRR_ECOLI Transcriptional regulatory protein TyrR tyrR b1323 JW1316 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 SEQUENCE REVISION NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 CHARACTERIZATION DOMAINS PARTIAL PROTEIN SEQUENCE CHARACTERIZATION SUBUNIT SUBUNIT REVIEW Involved in transcriptional regulation of aromatic amino acid biosynthesis and transport. Modulates the expression of at least 8 unlinked operons. Seven of these operons are regulated in response to changes in the concentration of the three aromatic amino acids (phenylalanine, tyrosine and tryptophan). These amino acids are suggested to act as co-effectors which bind to the TyrR protein to form an active regulatory protein. In most cases TyrR causes negative regulation, but positive effects on the tyrP gene have been observed at high phenylalanine concentrations. Homodimer. In presence of tyrosine (to the lesser extent, phenylalanine or tryptophan) and excess of ATP it undergoes a ligand-induced hexamerization. It is suggested that the hexameric form of TyrR is the active repressing species, interacting with two or three tyrR boxes in the targeted regulatory DNA. P06959 aceF false 2 The tyrR gene is autogenously regulated by a mechanism that gives similar rates of expression of tyrR irrespective of concentration of the aromatic amino acids. 3D-structure Activator Aromatic hydrocarbons catabolism ATP-binding Complete proteome Direct protein sequencing DNA-binding Nucleotide-binding Reference proteome Repressor Transcription Transcription regulation Two-component regulatory system MRLEVFCEDRLGLTRELLDLLVLRGIDLRGIEIDPIGRIYLNFAELEFESFSSLMAEIRR IAGVTDVRTVPWMPSEREHLALSALLEALPEPVLSVDMKSKVDMANPASCQLFGQKLDRL RNHTAAQLINGFNFLRWLESEPQDSHNEHVVINGQNFLMEITPVYLQDENDQHVLTGAVV MLRSTIRMGRQLQNVAAQDVSAFSQIVAVSPKMKHVVEQAQKLAMLSAPLLITGDTGTGK DLFAYACHQASPRAGKPYLALNCASIPEDAVESELFGHAPEGKKGFFEQANGGSVLLDEI GEMSPRMQAKLLRFLNDGTFRRVGEDHEVHVDVRVICATQKNLVELVQKGMFREDLYYRL NVLTLNLPPLRDCPQDIMPLTELFVARFADEQGVPRPKLAADLNTVLTRYAWPGNVRQLK NAIYRALTQLDGYELRPQDILLPDYDAATVAVGEDAMEGSLDEITSRFERSVLTQLYRNY PSTRKLAKRLGVSHTAIANKLREYGLSQKKNEE P64432 P76599 Q2MAE9 YPJD_ECOLI Inner membrane protein YpjD ypjD b2611 JW2592 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 TOPOLOGY [LARGE SCALE ANALYSIS] K12 / MG1655 / ATCC 47076 Cell inner membrane Multi-pass membrane protein Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MPVFALLALVAYSVSLALIVPGLLQKNGGWRRMAIISAVIALVCHAIALEARILPDGDSG QNLSLLNVGSLVSLMICTVMTIVASRNRGWLLLPIVYAFALINLALATFMPNEYITHLEA TPGMLVHIGLSLFSYATLIIAALYALQLAWIDYQLKNKKLAFNQEMPPLMSIERKMFHIT QIGVVLLTLTLCTGLFYMHNLFSMENIDKAVLSIVAWFVYIVLLWGHYHEGWRGRRVVWF NVAGAVILTLAYFGSRIVQQLIS Q46834 Q2M9M5 YGHF_ECOLI Putative type II secretion system C-type protein YghF Putative general secretion pathway C-type protein YghF yghF b2970 JW5484 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Involved in a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of folded proteins across the outer membrane. Cell inner membrane Single-pass membrane protein In many other E.coli strains this gene is part of a type II secretion system, but in MG1655 the locus is missing a number of genes. Belongs to the GSP C family. Translation N-terminally extended. Translation N-terminally extended. Cell inner membrane Cell membrane Complete proteome Membrane Protein transport Reference proteome Transmembrane Transmembrane helix Transport MARVVFRDARIYLIQWLTKIRHTLNQRQSLNTDKEHLRKIARGMFWLMLLIISAKMAHSL WRYISFSAEYTAVSQPVNKPSRVDAKTFDKNDVQLISQQNWFGKYQPVAAQVKQPEPVPV AETRLNVVLRGIAFGARPGAVIEEGGKQQVYLQGETLGSHNAVIEEINRDHVMLRYQGKI ERLSLAEEERSTVAVTNKKAVSDEAKQAVAEPAVSVPVEIPAAVRQALAKDPQKIFNYIQ LTPVRKEGIVGYAAKPGADRSLFDASGFKEGDIAIALNQQDFTDPRAMIALMRQLPSMDS IQLTVLRKGARHDISIALRYRLFCPPYWKKS A5A605 P71282 YKFM_ECOLI Uncharacterized protein YkfM ykfM b4586 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 Membrane Multi-pass membrane protein Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MRLHVKLKEFLSMFFMAILFFPAFNASLFFTGVKPLYSIIKCSTEIFYDWRMLILCFGFM SFSFLNIHVILLTIIKSFLIKKTKVVNFATDITIQLTLIFLLIAIVIAPLIAPFVTGYVN TNYHPCGNNTGIFPGAIYIKNGMKCNNGYISRKEDSAVK P75677 Q9R2D8 YKFF_ECOLI UPF0401 protein YkfF ykfF b0249 JW5023 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Belongs to the UPF0401 family. 3D-structure Complete proteome Reference proteome MTQSVLLPPGPFTRRQAQAVTTTYSNITLEDDQGSHFRLVVRDTEGRMVWRAWNFEPDAG EGLNRYIRTSGIRTDTATR P39308 Q2M6A1 YJFZ_ECOLI Uncharacterized protein YjfZ yjfZ b4204 JW4162 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Membrane Single-pass membrane protein To E.coli YjiC. Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MTLPTTIYSFPAYLSRFSSTDKPVKLKFHQYARATLLSNRGRDHNCDGRRTVEIHKLDLS DWQAFNKLATRCNAYDGITMNGDNSFGWNHEATLDNIHAQKYNKAYAGARLTAELKYLLQ DVESFEPNSKYTIHEVVLGPGYGTPDYTGQTIGYVVTLPAQMPNCWSSELPTIDLYIDQL RTVTGVSNALGFIIAALLNAYSDLPHDLKIGLRSLSSSAAIYSGLGFERVPQERDISCAR MYLTPANHPDLWTQENGEWIYLRN P0DPN8 A0A385XJG4 YMGK_ECOLI Protein YmgK ymgK b4738 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 IDENTIFICATION INDUCTION Expressed at low levels in exponential and at slightly higher levels in stationary phase (at protein level). Complete proteome Reference proteome MFSKLAQSSIKAMF P39408 P78143 Q2M5T9 YJJV_ECOLI Uncharacterized metal-dependent hydrolase YjjV 3.1.-.- yjjV b4378 JW4341 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH ZINC IONS a divalent metal cation Binds 2 divalent metal cations per subunit. P0CE47 tufA false 2 Belongs to the metallo-dependent hydrolases superfamily. TatD-type hydrolase family. Translation N-terminally extended. 3D-structure Complete proteome Hydrolase Metal-binding Reference proteome MICRFIDTHCHFDFPPFSGDEEASLQRAAQAGVGKIIVPATEAENFARVLALAENYQPLY AALGLHPGMLEKHSDVSLEQLQQALERRPAKVVAVGEIGLDLFGDDPQFERQQWLLDEQL KLAKRYDLPVILHSRRTHDKLAMHLKRHDLPRTGVVHGFSGSLQQAERFVQLGYKIGVGG TITYPRASKTRDVIAKLPLASLLLETDAPDMPLNGFQGQPNRPEQAARVFAVLCELRREP ADEIAQALLNNTYTLFNVP P0A8X0 P26650 Q2M672 YJGA_ECOLI UPF0307 protein YjgA x96 protein yjgA b4234 JW4193 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 IDENTIFICATION BY MASS SPECTROMETRY SUBCELLULAR LOCATION ASSOCIATION WITH THE 50S RIBOSOMAL SUBUNIT K12 / MG1655 / ATCC 47076 Cytoplasm Has been seen to comigrate with the 50S ribosomal subunit in sucrose gradients. Belongs to the UPF0307 family. Complete proteome Cytoplasm Reference proteome MTKQPEDWLDDVPGDDIEDEDDEIIWVSKSEIKRDAEELKRLGAEIVDLGKNALDKIPLD ADLRAAIELAQRIKMEGRRRQLQLIGKMLRQRDVEPIRQALDKLKNRHNQQVVLFHKLEN LRDRLIDQGDDAIAEVLNLWPDADRQQLRTLIRNAKKEKEGNKPPKSARQIFQYLRELAE NEG P0DPO9 A0A385XJU6 YNFR_ECOLI Protein YnfR ynfR b4749 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 IDENTIFICATION INDUCTION By cold shock (at protein level). Complete proteome Reference proteome MKAPSGAFLLGVYSMDTHILR P0DPN1 A0A385XJN0 YKIC_ECOLI Protein YkiC ykiC b4731 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 IDENTIFICATION INDUCTION Cell inner membrane Single-pass membrane protein Expressed in both exponential and stationary phase; expression is higher in exponential phase (at protein level). Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MNYKAFTQIAIDLLSAKLCNCTQAIMTHIIASFLAFMFF P0AFN6 P36880 P75657 Q8KMY9 YADH_ECOLI Inner membrane transport permease YadH yadH b0128 JW0124 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] SEQUENCE REVISION K12 / W3110 / ATCC 27325 / DSM 5911 TOPOLOGY [LARGE SCALE ANALYSIS] K12 / MG1655 / ATCC 47076 Cell inner membrane Multi-pass membrane protein Belongs to the ABC-2 integral membrane protein family. Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix Transport F L MMHLYWVALKSIWAKEIHRFMRIWVQTLVPPVITMTLYFIIFGNLIGSRIGDMHGFSYMQ FIVPGLIMMSVITNAYANVASSFFGAKFQRNIEELLVAPVPTHVIIAGYVGGGVARGLFV GILVTAISLFFVPFQVHSWVFVALTLVLTAVLFSLAGLLNGVFAKTFDDISLVPTFVLTP LTYLGGVFYSLTLLPPFWQGLSHLNPIVYMISGFRYGFLGINDVPLVTTFGVLVVFIVAF YLICWSLIQRGRGLRS P0AAA1 P77262 Q2MCD5 YAGU_ECOLI Inner membrane protein YagU yagU b0287 JW0281 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 SUBUNIT SUBCELLULAR LOCATION BL21-DE3 TOPOLOGY [LARGE SCALE ANALYSIS] K12 / MG1655 / ATCC 47076 Homodimer. Cell inner membrane Multi-pass membrane protein Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MNIFEQTPPNRRRYGLAAFIGLIAGVVSAFVKWGAEVPLPPRSPVDMFNAACGPESLIRA AGQIDCSRNFLNPPYIFLRDWLGLTDPNAAVYTFAGHVFNWVGVTHIIFSIVFAVGYCVV AEVFPKIKLWQGLLAGALAQLFVHMISFPLMGLTPPLFDLPWYENVSEIFGHLVWFWSIE IIRRDLRNRITHEPDPEIPLGSNR P33128 YADV_ECOLI Probable fimbrial chaperone YadV yadV ecpD b0140 JW0136 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] INDUCTION BY HEAT SHOCK K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION INDUCTION DISRUPTION PHENOTYPE K12 / MG1655 / ATCC 47076 Part of the yadCKLM-htrE-yadVN fimbrial operon. Could contribute to adhesion to various surfaces in specific environmental niches. Periplasm Repressed by H-NS. Induced by heat shock. Deletion of the operon under classical laboratory conditions does not result in any major effect on E.coli capacity to form biofilms compared with the wild-type strain. The operon is cryptic under classical laboratory conditions, but is functional when constitutively expressed. Belongs to the periplasmic pilus chaperone family. Was originally called ecpD, but ecp is now used for the ecpABCDE operon involved in E.coli common pilus (ECP) synthesis. 3D-structure Chaperone Complete proteome Fimbrium biogenesis Immunoglobulin domain Periplasm Reference proteome Signal Stress response A R SV RA MFFNTKHTTALCFVTCMAFSSSSIADIVISGTRVIYKSDQKSVNVRLENKGNNPLLVQSW LDTGDDNAEPGSITVPFTATPPVSRIDAKRGQTIKLMYTASTSLPKDRESVFWFNVLEVP PKPDAEKVANQSLLQLAFRTRIKLFYRPDGLKGNPSEAPLALKWFWSGSEGKASLRVTNP TPYYVSFSSGDLEASGKRYPIDVKMIAPFSDEVMKVNGLNGKANSAKVHFYAINDFGGAI EGNARL P39376 Q2M5Y6 YJIE_ECOLI HTH-type transcriptional regulator YjiE Hypochlorite-response regulator protein YjiE Quorum-sensing regulator protein D yjiE qseD b4327 JW4290 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-117 K12 / W3110 / ATCC 27325 / DSM 5911 POSSIBLE ROLE IN REGULATION OF MOTILITY DNA-BINDING INDUCTION DISRUPTION PHENOTYPE K12 / BW25113 ROLE IN HYPOCHLORITE RESPONSE SUBUNIT DNA-BINDING INDUCTION DISRUPTION PHENOTYPE K12 / C600 / ATCC 23724 / DSM 3925 / LMG 3041 / NCIB 10222 Protects cells from HOCl (hypochlorite) stress but not peroxide or diamide stress. Decreases the intracellular load of reactive oxygen species by up-regulating genes involved in methionine and cysteine biosynthesis and down-regulating Fur-regulated genes involved in iron acquisition. Has also been suggested to down-regulate expression of the flagellar regulon, decreasing motility, but this activity was not confirmed in a second study (PubMed:22223481). Forms dimers, tetramers and possibly dodecameric complexes; oligomerization may be governed by cellular concentrations. DNA-binding seems to decrease oligomerization. Transcription increases throughout growth and is maximal during stationary phase. Is not up-regulated upon exposure to HOCl. Controversial. Hypermotility, up-regulation of flagellar genes and up-regulation of flagellar protein FliC (PubMed:20494990). Decreased viability following HOCl stress; no effect on motility was seen in this study (PubMed:22223481). Belongs to the LysR transcriptional regulatory family. Complete proteome DNA-binding Reference proteome Transcription Transcription regulation MDDCGAILHNIETKWLYDFLTLEKCRNFSQAAVSRNVSQPAFSRRIRALEQAIGVELFNR QVTPLQLSEQGKIFHSQIRHLLQQLESNLAELRGGSDYAQRKIKIAAAHSLSLGLLPSII SQMPPLFTWAIEAIDVDEAVDKLREGQSDCIFSFHDEDLLEAPFDHIRLFESQLFPVCAS DEHGEALFNLAQPHFPLLNYSRNSYMGRLINRTLTRHSELSFSTFFVSSMSELLKQVALD GCGIAWLPEYAIQQEIRSGKLVVLNRDELVIPIQAYAYRMNTRMNPVAERFWRELRELEI VLS P24211 P76869 P77471 RHSE_ECOLI Putative protein RhsE rhsE b1456 JW1451 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-682 K12 SEQUENCE REVISION TO 442 REVIEW Rhs elements have a nonessential function. They may play an important role in the natural ecology of the cell. Belongs to the RHS family. Could be the product of a pseudogene. Complete proteome Reference proteome MSTRLTTLSHTSEGHRVSVHYGYDDKGRLTGERQTVENPETGELLWHHETGHAYNEQGLA NRVTPDSLPPVEWLTYGSGYLAGMKLGGTPLLEFTRDRLHRETVRSFGSMAGSNAAYKLT STYTPAGQLQSQHLNSLVYDRDYGWNDNGDLVRISGPRQTREYGYSATGRLESVRTLAPD LDIRIPYATDPAGNRLPDPELHPDSTLTVWPDNRIAEDAHYVYRHDEYGRLTEKTDRIPA GVIRTDDERTHHYHYDSQHRLVFYTRIQHGEPLVESRYLYDPLGRRMAKRVWRRERDLTG WMSLSRKPEVTWYGWDGDRLTTVQTDTTRIQTVYEPGSFTPLIRVETENGEREKAQRRSL AETLQQEGSENGHGVVFPAELVRLLDRLEEEIRADRVSSESRAWLAQCGLTVEQLARQVE PEYTPARKVHFYHCDHRGLPLALISEDGNTAWRGEYDEWGNQLNEENPHHLHQPYRLPGQ QHDEESGLYYNRHRHYDPLQGRYITPDPIGLRGGWNMYQYPLNPIQVIDPMGLDAIENMT SGGLIYAVSGVPGLIAANSITNSAYQFGYDMDAIVGGAHNGAADAMRHCYLMCRMTKTFG STIADVIGKNHEAAGDRQGQPAKERIMDLKNNTVGIACGDFSAKCSDACIEKYNTGQLFG LDGIKADNPIKAKQGSSDASNY P0A7R9 P02366 Q2M6W2 RS11_ECOLI 30S ribosomal protein S11 Small ribosomal subunit protein uS11 rpsK b3297 JW3259 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 PROTEIN SEQUENCE OF 2-129 METHYLATION AT ALA-2 SUBUNIT K CROSS-LINKING TO IF-3 B CROSS-LINKING TO IF-3 CROSS-LINKING TO IF-3 MRE-600 IDENTIFICATION BY 2D-GEL MASS SPECTROMETRY SUBUNIT K12 / ATCC 25404 / DSM 5698 / NCIMB 11290 NOMENCLATURE MODELING OF IF-3/30S SUBUNIT INTERACTION 3D-STRUCTURE MODELING SUBUNIT STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS) SUBUNIT MRE-600 X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES SUBUNIT MRE-600 STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) OF 70S RIBOSOME IN COMPLEX WITH ARFA AND RF2 SUBUNIT STRUCTURE BY ELECTRON MICROSCOPY (3.1 ANGSTROMS) OF 70S RIBOSOME IN COMPLEX WITH ARFA AND RF2 SUBUNIT STRUCTURE BY ELECTRON MICROSCOPY (2.97 ANGSTROMS) OF 70S RIBOSOME IN COMPLEX WITH ARFA AND RF2 SUBUNIT STRUCTURE BY ELECTRON MICROSCOPY (3.52 ANGSTROMS) OF 70S RIBOSOME IN COMPLEX WITH ARFA AND RF2 SUBUNIT Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome (By similarity). Part of the 30S ribosomal subunit (PubMed:7007074, PubMed:10094780, PubMed:12809609, PubMed:16272117, PubMed:27934701, PubMed:12244297, PubMed:27906160, PubMed:27906161, PubMed:28077875). Interacts with proteins S7 and S18 (By similarity). Cross-links to IF-3 (PubMed:7000779, PubMed:7020604, PubMed:6349681). Has been predicted to contact the N-terminal domain of IF-3 based on footprint studies; exactly how IF-3 interacts with the 30S subunit is controversial (PubMed:7000779, PubMed:7020604, PubMed:6349681). Belongs to the universal ribosomal protein uS11 family. 3D-structure Complete proteome Direct protein sequencing Methylation Reference proteome Ribonucleoprotein Ribosomal protein RNA-binding rRNA-binding MAKAPIRARKRVRKQVSDGVAHIHASFNNTIVTITDRQGNALGWATAGGSGFRGSRKSTP FAAQVAAERCADAVKEYGIKNLEVMVKGPGPGRESTIRALNAAGFRITNITDVTPIPHNG CRPPKKRRV P33011 P76368 YEEA_ECOLI Inner membrane protein YeeA yeeA b2008 JW1990 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-149 K12 / BHB2600 TOPOLOGY [LARGE SCALE ANALYSIS] K12 / MG1655 / ATCC 47076 Cell inner membrane Multi-pass membrane protein Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MRADKSLSPFEIRVYRHYRIVHGTRVALAFLLTFLIIRLFTIPESTWPLVTMVVIMGPIS FWGNVVPRAFERIGGTVLGSILGLIALQLELISLPLMLVWCAAAMFLCGWLALGKKPYQG LLIGVTLAIVVGSPTGEIDTALWRSGDVILGSLLAMLFTGIWPQRAFIHWRIQLAKSLTE YNRVYQSAFSPNLLERPRLESHLQKLLTDAVKMRGLIAPASKETRIPKSIYEGIQTINRN LVCMLELQINAYWATRPSHFVLLNAQKLRDTQHMMQQILLSLVHALYEGNPQPVFANTEK LNDAVEELRQLLNNHHDLKVVETPIYGYVWLNMETAHQLELLSNLICRALRK P65367 Q2MA44 Q46917 YQCA_ECOLI Uncharacterized protein YqcA yqcA b2790 JW2761 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Probable electron transporter. FMN Belongs to the flavodoxin family. MioC subfamily. Complete proteome Electron transport Flavoprotein FMN Reference proteome Transport MAEIGIFVGTMYGNSLLVAEEAEAILTAQGHKATVFEDPELSDWLPYQDKYVLVVTSTTG QGDLPDSIVPLFQGIKDSLGFQPNLRYGVIALGDSSYVNFCNGGKQFDALLQEQSAQRVG EMLLIDASENPEPETESNPWVEQWGTLLS P46474 P46475 P46476 P76676 Q2M8W8 Q6BF41 YHDP_ECOLI Uncharacterized protein YhdP yhdP yhdQ yhdR b4472 JW5542 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 SEQUENCE REVISION NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50 K12 Produces three separate ORFs (yhdP, yhdQ and yhdR). Produces three separate ORFs (yhdP, yhdQ and yhdR). Produces three separate ORFs (yhdP, yhdQ and yhdR). Complete proteome Reference proteome Signal G A P R MRRLPGILLLTGAALVVIAALLVSGLRIALPHLDAWRPEILNKIESATGMPVEASQLSAS WQNFGPTLEAHDIRAELKDGGEFSVKRVTLALDVWQSLLHMRWQFRDLTFWQLRFRTNTP ITSGGSDDSLEASHISDLFLRQFDHFDLRDSEVSFLTPSGQRAELAIPQLTWLNDPRRHR AEGLVSLSSLTGQHGVMQVRMDLRDDEGLLSNGRVWLQADDIDLKPWLGKWMQDNIALET AQFSLEGWMTIDKGDVTGGDVWLKQGGASWLGEKQTHTLSVDNLTAHITRENPGWQFSIP DTRITMDGKPWPSGALTLAWIPEQDVGGKDNKRSDELRIRASNLELAGLEGIRPLAAKLS PALGDVWRSTQPSGKINTLALDIPLQAADKTRFQASWSDLAWKQWKLLPGAEHFSGTLSG SVENGLLTASMKQAKMPYETVFRAPLEIADGQATISWLNNNKGFQLDGRNIDVKAKAVHA RGGFRYLQPANDEPWLGILAGISTDDGSQAWRYFPENLMGKDLVDYLSGAIQGGEADNAT LVYGGNPQLFPYKHNEGQFEVLVPLRNAKFAFQPDWPALTNLDIELDFINDGLWMKTDGV NLGGVRASNLTAVIPDYSKEKLLIDADIKGPGKAVGPYFDETPLKDSLGATLQELQLDGD VNARLHLDIPLNGELVTAKGEVTLRNNSLFIKPLDSTLKNLSGKFSFINSDLQSEPLTAS WFNQPLNVDFSTKEGAKAYQVAVNLNGNWQPAKTGVLPEAVNEALSGSVAWDGKVGIDLP YHAGATYNIELNGDLKNVSSHLPSPLAKPAGEPLAVNVKVDGNLNSFELTGQAGADNHFN SRWLLGQKLTLDRAIWAADSKTLPPLPEQSGVELNMPPMNGAEWLALFQKGAAESVGGAA SFPQHITLRTPMLSLGNQQWNNLSIVSQPTANGTLVEAQGREINATLAMRNNAPWLANIK YLYYNPSVAKTRGDSTPSSPFPTTERINFRGWPDAQIRCTECWFWGQKFGRIDSDITISG DTLTLTNGLIDTGFSRLTADGEWVNNPGNERTSLKGKLRGQKIDAAAEFFGVTTPIRQSS FNVDYDLHWRKAPWQPDEATLNGIIHTQLGKGEITEINTGHAGQLLRLLSVDALMRKLRF DFRDTFGEGFYFDSIRSTAWIKDGVMHTDDTLVDGLEADIAMKGSVNLVRRDLNMEAVVA PEISATVGVAAAFAVNPIVGAAVFAASKVLGPLWSKVSILRYHISGPLDDPQINEVLRQP RKEKAQ P0AAS7 P45571 P77661 Q2MBQ1 YBCJ_ECOLI Uncharacterized protein YbcJ ybcJ b0528 JW5070 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-25 IDENTIFICATION STRUCTURE BY NMR PROPOSED FUNCTION K12 / MC1061 / ATCC 53338 / DSM 7140 Its structure and the presence of conserved basic residues indicates that it probably binds RNA. Although the solution structure of this protein has been solved it has not been shown to be expressed in E.coli. Translation N-terminally shortened. 3D-structure Complete proteome Reference proteome RNA-binding MATFSLGKHPHVELCDLLKLEGWSESGAQAKIAIAEGQVKVDGAVETRKRCKIVAGQTVS FAGHSVQVVA P37635 Q2M7G6 YHIS_ECOLI Putative uncharacterized protein YhiS yhiS b3504 JW3471 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Could be the product of a pseudogene. Complete proteome Reference proteome MSIDFTPGIINTYHGDIYNCTTNTDNAKTPDTPKWPCDNWEEQQPINSTFSGEGYISDQY DLAQHQLQQINACHTNTTYTNADYSKVVAQLVSLITNIETISSTQLTQQTQSILNQINNI RYEKNKSAECRIIVIANPKPDKAIITKISVEEGIPITFSVQTMFSDTNFIAEQRADLPTN IKDIQSLYQKMTKLYIEHSENKNRMKVFAGTNFIDFNMTGQNLSGFVLTLSRFYFEDLLN INFTDANLGKVRISGEILLG P64545 P76571 Q2MAI1 YFGG_ECOLI Protein YfgG yfgG b2504 JW5399 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 PROTEIN SEQUENCE OF 49-59 INDENTIFICATION INDUCTION BY HEAT SHOCK K12 / MG1655 / ATCC 47076 Cell inner membrane Single-pass membrane protein By heat shock (shift from 30 to 45 degrees Celsius) (at protein level). Cell inner membrane Cell membrane Complete proteome Direct protein sequencing Membrane Reference proteome Stress response Transmembrane Transmembrane helix MSQATSMRKRHRFNSRMTRIVLLISFIFFFGRFIYSSVGAWQHHQSKKEAQQSTLSVESP VQR P76512 Q2MAK8 YFDP_ECOLI Uncharacterized protein YfdP yfdP b2359 JW2356 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 To phage T4 y06Q. Complete proteome Reference proteome MASERSTDVQAFIGELDGGVFETKIGAVLSEVASGVMNTKTKGKVSLNLEIEPFDENRLK IKHKLSYVRPTNRGKISEEDTTETPMYVNRGGRLTILQEDQGQLLTLAGEPDGKLRAAGH P0ADJ8 P11287 P76715 Q2M7M5 YIAA_ECOLI Inner membrane protein YiaA yiaA b3562 JW3534 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 / MM294 / ATCC 33625 / DSM 5208 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 TOPOLOGY [LARGE SCALE ANALYSIS] K12 / MG1655 / ATCC 47076 Cell inner membrane Multi-pass membrane protein Translation N-terminally shortened. Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MDNKISTYSPAFSIVSWIALVGGIVTYLLGLWNAEMQLNEKGYYFAVLVLGLFSAASYQK TVRDKYEGIPTTSIYYMTCLTVFIISVALLMVGLWNATLLLSEKGFYGLAFFLSLFGAVA VQKNIRDAGINPPKETQVTQEEYSE P0DPC8 A0A385XJE1 YMCF_ECOLI Protein YmcF ymcF b4723 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 IDENTIFICATION INDUCTION BY COLD SHOCK K12 / MG1655 / ATCC 47076 By cold shock, 10 degrees Celsius (at protein level). Uses the non-canonical initiation codon AUU, which may limit its expression (PubMed:28861998). Belongs to the YmcF/YnqF peptide family. Complete proteome Reference proteome MTQHLHFRCPCCHGSQYRTSAFDVTERNPLGAKCIFCKSTMITFDNVALQIRTDHAPLDF TK P33368 P33367 P76437 Q2MAU2 YOHF_ECOLI Uncharacterized oxidoreductase YohF 1.-.-.- yohF yohE b2137 JW2125 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / BHB2600 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Belongs to the short-chain dehydrogenases/reductases (SDR) family. Produces two separate ORFs. 3D-structure Complete proteome Oxidoreductase Reference proteome MAQVAIITASDSGIGKECALLLAQQGFDIGITWHSDEEGAKDTAREVVSHGVRAEIVQLD LGNLPEGALALEKLIQRLGRIDVLVNNAGAMTKAPFLDMAFDEWRKIFTVDVDGAFLCSQ IAARQMVKQGQGGRIINITSVHEHTPLPDASAYTAAKHALGGLTKAMALELVRHKILVNA VAPGAIATPMNGMDDSDVKPDAEPSIPLRRFGATHEIASLVVWLCSEGANYTTGQSLIVD GGFMLANPQFNPE P37674 Q2M7P0 YIAM_ECOLI 2,3-diketo-L-gulonate TRAP transporter small permease protein YiaM yiaM b3577 JW3549 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 PRELIMINARY FUNCTION K12 DELETION STUDIES K12 TOPOLOGY [LARGE SCALE ANALYSIS] K12 / MG1655 / ATCC 47076 FUNCTION K12 / W3110 / ATCC 27325 / DSM 5911 Part of the tripartite ATP-independent periplasmic (TRAP) transport system YiaMNO involved in the uptake of 2,3-diketo-L-gulonate. The complex comprises the extracytoplasmic solute receptor protein YiaO, and the two transmembrane proteins YiaM and YiaN. Cell inner membrane Multi-pass membrane protein Belongs to the TRAP transporter small permease family. Was originally proposed to be a subunit from an L-xylulose uptake system, but PubMed:16385129 shows that it does not bind L- or D-xylulose. Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix Transport MKKILEAILAINLAVLSCIVFINIILRYGFQTSILSVDELSRYLFVWLTFIGAIVAFMDN AHVQVTFLVEKLSPAWQRRVALVTHSLILFICGALAWGATLKTIQDWSDYSPILGLPIGL MYAACLPTSLVIAFFELRHLYQLITRSNSLTSPPQGA P52131 P76605 Q2MAD9 Q6BF68 YFJP_ECOLI Uncharacterized protein YfjP yfjP b2632 JW5419 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 SEQUENCE REVISION TO 218; 233 AND 248 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 To E.coli YkfA and YeeP. Complete proteome GTP-binding Nucleotide-binding Reference proteome A P T W GA DT MKNFEVLQPLQNSLSGLPLWVSERILQQINQLTHYEPVIGIMGKTGAGKSSLCNALFAGE VSPVSDVAACTRDPLRFRLQIGEHFMTIVDLPGVGESGVRDTEYAALYREQLPRLDLILW LIKADDRALATDEHFYRQVIGEAYRHKMLFVISQSDKAEPTSGGNILSTEQKQNISRKIC LLHELFQPVHPVCAVSVRLQWGLRVMAERMIKCLPREASSPVVALLQHPFRTTVAREQAR DDFGETVGAILDTVSTFPLIPAPVRTIIQAVRSSVVSVARAVWDFFF P32108 Q2M7R1 YIBI_ECOLI Uncharacterized protein YibI yibI b3598 JW3572 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 To E.coli YiaW. Complete proteome Reference proteome MFLNYFALGVLIFVFLVIFYGIIAIHDIPYLIAKKRNHPHADAIHTAGWVSLFTLHVIWP FLWIWATLYQPERGWGMQSHVASQEKATDPEIAALSDRISRLEHQLAAEKKTDYSTFPEI P39161 Q2M5Y9 UXUR_ECOLI Uxu operon transcriptional regulator uxuR b4324 JW4287 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Repressor for the uxuRBA operon. Complete proteome DNA-binding Reference proteome Repressor Transcription Transcription regulation MKSATSAQRPYQEVGAMIRDLIIKTPYNPGERLPPEREIAEMLDVTRTVVREALIMLEIK GLVEVRRGAGIYVLDNSGSQNTDSPDANVCNDAGPFELLQARQLLESNIAEFAALQATRE DIVKMRQALQLEERELASSAPGSSESGDMQFHLAIAEATHNSMLVELFRQSWQWRENNPM WIQLHSHLDDSLYRKEWLGDHKQILAALIKKDARAAKLAMWQHLENVKQRLLEFSNVDDI YFDGYLFDSWPLDKVDA P52133 Q2MAD7 YFJR_ECOLI Uncharacterized HTH-type transcriptional regulator YfjR yfjR b2634 JW2615 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Complete proteome DNA-binding Reference proteome Transcription Transcription regulation MTQAERRHDRLAVRLSLIISRLVAGETLSVRKLAAEFGVSVRTLRRDFRERLMYLDLEYQ SGYCRLRTAGSEMQMVPDVLIFAHRSGLAGLFPGLDRRLVNALLMCDESPCVIAPANPVP SPSGALSFWRLIQAITGRRRVTLIAEGRRCERLAPCRLLIHQQTWYLVAEHEGHIAVFTL DEIHLIQPLQETFRRNDSLCRLVEDPVFIQALPHFRFIQHSLLTFVPADSPPE P76657 Q2M9F4 YQIJ_ECOLI Inner membrane protein YqiJ yqiJ b3050 JW3022 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 TOPOLOGY [LARGE SCALE ANALYSIS] K12 / MG1655 / ATCC 47076 Cell inner membrane Multi-pass membrane protein Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MILFADYNTPYLFAISFVLLIGLLEIFALICGHMLSGALDAHLDHYDSITTGHISQALHY LNIGRLPALVVLCLLAGFFGLIGILLQHACIMVWQSPLSNLFVVPVSLLFTIIAVHYTGK IVAPWIPRDHSSAITEEEYIGSMALITGHQATSGNPCEGKLTDQFGQIHYLLLEPEEGKI FTKGDKVLIICRLSATRYLAENNPWPQIL V9HVX0 YPAA_ECOLI Uncharacterized protein YpaA ypaA b4543 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 Complete proteome Reference proteome MTIAERLRQEGHQIGWQEGKLEGLHEQAIKIALRMLEQGFDRDQVLAATQLSEADLAANN H P0AD47 O08101 P77751 YPHA_ECOLI Inner membrane protein YphA yphA b2543 JW2527 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 / MC1061 / ATCC 53338 / DSM 7140 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 TOPOLOGY [LARGE SCALE ANALYSIS] K12 / MG1655 / ATCC 47076 Cell inner membrane Multi-pass membrane protein Belongs to the DoxX family. Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MNTLRYFDFGAARPVLLLIARIAVVLIFIIFGFPKMMGFDGTVQYMASLGAPMPMLAAII AVVMEVPAAILIVLGFFTRPLAVLFIFYTLGTAVIGHHYWDMTGDAVGPNMINFWKNVSI AGAFLLLAITGPGAISLDRR A5A612 YMGJ_ECOLI Uncharacterized protein YmgJ ymgJ b4594 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 Complete proteome Reference proteome MSRRYSSATITLVILFCRRPHCRKISVRQYYQKRVIFYPTTLQRTACKKCLFLMRDIIIS S P0A8E5 P45567 P75653 Q8X955 YACL_ECOLI UPF0231 protein YacL yacL b0119 JW0115 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-120 K12 IDENTIFICATION P0ACJ8 crp false 4 Belongs to the UPF0231 family. Complete proteome Reference proteome MDYEFLRDITGVVKVRMSMGHEVVGHWFNEEVKENLALLDEVEQAAHALKGSERSWQRAG HEYTLWMDGEEVMVRANQLEFAGDEMEEGMNYYDEESLSLCGVEDFLQVVAAYRNFVQQK P0AAR5 P45808 P77478 Q2MBV9 YBAN_ECOLI Inner membrane protein YbaN ybaN b0468 JW0457 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-115 K12 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 95-125 K12 / EMG2 IDENTIFICATION TOPOLOGY [LARGE SCALE ANALYSIS] K12 / MG1655 / ATCC 47076 Cell inner membrane Multi-pass membrane protein Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix P R MQRIILIIIGWLAVVLGTLGVVLPVLPTTPFILLAAWCFARSSPRFHAWLLYRSWFGSYL RFWQKHHAMPRGVKPRAILLILLTFAISLWFVQMPWVRIMLLVILACLLFYMWRIPVIDE KQEKH P77433 Q2MCB4 YKGG_ECOLI Uncharacterized protein YkgG ykgG b0308 JW5042 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 LACK OF COMPLEMENTATION OF B.SUBTILIS LUTABC OPERON K12 The E.coli ykgEFG operon is a clear homolog of the B.subtilis lutABC operon, however it is not able of restoring L-lactate utilization to the B.subtilis mutant for lutABC operon. Thus, ykgEFG operon may contribute to lactate catabolism in E.coli, but under conditions other than those tested, or alternatively, the ykgEFG operon may be responsible for the catabolism of a metabolite other than (but perhaps related to) lactate in E.coli. Belongs to the LutC/YkgG family. Translation N-terminally shortened. Complete proteome Reference proteome MDNRGEFLNNVAQALGRPLRLEPQAEDAPLNNYANERLTQLNQQQRCDAFIQFASDVMLT RCELTSEAKAAEAAIRLCKELGDQSVVISGDTRLEELGISERLQQECNAVVWDPAKGAEN ISQAEQAKVGVVYAEYGLTESGGVVLFSAAERGRSLSLLPEYSLFILRKSTILPRVAQLA EKLHQKAQAGERMPSCINIISGPSSTADIELIKVVGVHGPVKAVYLIIEDC P77354 Q2MCG0 YAFU_ECOLI Putative inner membrane protein YafU yafU b0218 JW0207 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 SUBCELLULAR LOCATION TOPOLOGY [LARGE SCALE ANALYSIS] K12 / MG1655 / ATCC 47076 Cell inner membrane Multi-pass membrane protein When overexpressed using vectors that provide a promoter and ribosome binding site (PubMed:15919996). Could be the product of a pseudogene; is missing 186 N-terminal amino acids compared to its orthologs. Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MSSERDLVNFLGDFSMDVAKAVIAGGVATAIGSLASFACVSFGFPVILVGGAILLTGIVC TVVLNEIDAQCHLSEKLKYAIRDGLKRQQELDKWKRENMTPFMYVLNTPPVI P39409 Q2M5T8 YJJW_ECOLI Putative glycyl-radical enzyme activating enzyme YjjW GRE activating enzyme YjjW 1.97.1.- yjjW b4379 JW4342 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 [4Fe-4S] cluster May bind up to 3 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. P0AEF4 dpiA false 2 P09147 galE false 2 P18196 minC false 2 Belongs to the organic radical-activating enzymes family. 4Fe-4S Complete proteome Iron Iron-sulfur Metal-binding Oxidoreductase Reference proteome Repeat S-adenosyl-L-methionine MNSRCALVSKIIPFSCVDGPGSRLALFLQGCNLRCKNCHNPWTMGRCNDCGECVPQCPHQ ALQIVDGKVVWNAVVCEQCDTCLKRCPQHATPMAQSMSVDEVLSHVRKAVLFIEGITVSG GEATTQLPFVVALFTAIKNDPQLRHLTCLVDSNGMLSETGWEKLLPVCDGAMLDLKAWGS ECHQQLTGRDNQQIKRSIYLLAERGKLAELRLLVIPGQVDYLQHIEELAAFIKGLGDVPV RLNAFHAHGVYGEAQSWASATPEDVEPLADALKVRGVSRLIFPALYL P75828 YBJD_ECOLI Uncharacterized protein YbjD ybjD b0876 JW0860 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 ATP-binding Complete proteome Nucleotide-binding Reference proteome MILERVEIVGFRGINRLSLMLEQNNVLIGENAWGKSSLLDALTLLLSPESDLYHFERDDF WFPPGDINGREHHLHIILTFRESLPGRHRVRRYRPLEACWTPCTDGYHRIFYRLEGESAE DGSVMTLRSFLDKDGHPIDVEDINDQARHLVRLMPVLRLRDARFMRRIRNGTVPNVPNVE VTARQLDFLARELSSHPQNLSDGQIRQGLSAMVQLLEHYFSEQGAGQARYRLMRRRASNE QRSWRYLDIINRMIDRPGGRSYRVILLGLFATLLQAKGTLRLDKDARPLLLIEDPETRLH PIMLSVAWHLLNLLPLQRIATTNSGELLSLTPVEHVCRLVRESSRVAAWRLGPSGLSTED SRRISFHIRFNRPSSLFARCWLLVEGETETWVINELARQCGHHFDAEGIKVIEFAQSGLK PLVKFARRMGIEWHVLVDGDEAGKKYAATVRSLLNNDREAEREHLTALPALDMEHFMYRQ GFSDVFHRMAQIPENVPMNLRKIISKAIHRSSKPDLAIEVAMEAGRRGVDSVPTLLKKMF SRVLWLARGRAD P76092 Q2MBC5 YNBC_ECOLI Uncharacterized protein YnbC ynbC b1410 JW1407 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 P77398 arnA false 2 P28632 holD false 3 P76340 hprR false 2 P13458 sbcC false 3 P15082 srlR false 4 Complete proteome Reference proteome MENSRIPGEHFFTTSDNTALFYRHWPALQPGAKKVIVLFHRGHEHSGRLQHLVDELAMPD TAFYAWDARGHGKSSGPRGYSPSLARSVRDVDEFVRFAASDSQVGLEEVVVIAQSVGAVL VATWIHDYAPAIRGLVLASPAFKVKLYVPLARPALALWHRLRGLFFINSYVKGRYLTHDR QRGASFNNDPLITRAIAVNILLDLYKTSERIIRDAAAITLPTQLLISGDDYVVHRQPQID FYQRLRSPLKELHLLPGFYHDTLGEENRALAFEKMQSFISRLYANKSQKFDYQHEDCTGP SADRWRLLSGGPVPLSPVDLAYRFMRKAMKLFGTHSSGLHLGMSTGFDSGSSLDYVYQNQ PQGSNAFGRLVDKIYLNSVGWRGIRQRKTHLQILIKQAVADLHAKGLAVRVVDIAAGHGR YVLDALANEPAVSDILLRDYSELNVAQGQEMIAQRGMSGRVRFEQGDAFNPEELSALTPR PTLAIVSGLYELFPENEQVKNSLAGLANAIEPGGILIYTGQPWHPQLEMIAGVLTSHKDG KPWVMRVRSQGEMDSLVRDAGFDKCTQRIDEWGIFTVSMAVRRDN P45767 Q2M8U6 Q6BF40 YHDX_ECOLI Putative amino-acid ABC transporter permease protein YhdX yhdX b3269 JW5544 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 SEQUENCE REVISION NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Probably part of the binding-protein-dependent transport system YdhWXYZ for an amino acid; probably responsible for the translocation of the substrate across the membrane. Cell inner membrane Multi-pass membrane protein Belongs to the binding-protein-dependent transport system permease family. HisMQ subfamily. Amino-acid transport Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix Transport MSHRRSTVKGSLSFANPTVRAWLFQILAVVAVVGIVGWLFHNTVTNLNNRGITSGFAFLD RGAGFGIVQHLIDYQQGDTYGRVFIVGLLNTLLVSALCIVFASVLGFFIGLARLSDNWLL RKLSTIYIEIFRNIPPLLQIFFWYFAVLRNLPGPRQAVSAFDLAFLSNRGLYIPSPQLGD GFIAFILAVVMAIVLSVGLFRFNKTYQIKTGQLRRTWPIAAVLIIGLPLLAQWLFGAALH WDVPALRGFNFRGGMVLIPELAALTLALSVYTSAFIAEIIRAGIQAVPYGQHEAARSLGL PNPVTLRQVIIPQALRVIIPPLTSQYLNIVKNSSLAAAIGYPDMVSLFAGTVLNQTGQAI ETIAMTMSVYLIISLTISLLMNIYNRRIAIVER P65294 Q2MA04 Q46932 YGDR_ECOLI Uncharacterized lipoprotein YgdR ygdR b2833 JW2801 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 STRUCTURE BY NMR OF 21-72 Cell membrane Lipid-anchor To E.coli YgdI. 3D-structure Cell membrane Complete proteome Lipoprotein Membrane Palmitate Reference proteome Signal MKKWAVIISAVGLAFAVSGCSSDYVMATKDGRMILTDGKPEIDDDTGLVSYHDQQGNAMQ INRDDVSQIIER Q46801 Q2M9X2 XDHC_ECOLI Putative xanthine dehydrogenase iron-sulfur-binding subunit XdhC xdhC ygeU b2868 JW2836 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 DISCUSSION OF FUNCTION K12 / W3110 / ATCC 27325 / DSM 5911 Iron-sulfur subunit of the xanthine dehydrogenase complex. [2Fe-2S] cluster Binds 2 [2Fe-2S] clusters. Purine metabolism; hypoxanthine degradation; urate from hypoxanthine: step 1/2. Heterotrimer of XdhA, XdhB and XdhC. 2Fe-2S Complete proteome Iron Iron-sulfur Metal-binding Purine metabolism Purine salvage Reference proteome MNHSETITIECTINGMPFQLHAAPGTPLSELLREQGLLSVKQGCCVGECGACTVLVDGTA IDSCLYLAAWAEGKEIRTLEGEAKGGKLSHVQQAYAKSGAVQCGFCTPGLIMATTAMLAK PREKPLTITEIRRGLAGNLCRCTGYQMIVNTVLDCEKTK P0ACM9 P32133 Q2M8G9 YIHL_ECOLI Uncharacterized HTH-type transcriptional regulator YihL yihL b3872 JW3843 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Complete proteome DNA-binding Reference proteome Transcription Transcription regulation MAENQSTVENAKEKLDRWLKDGITTPGGKLPSERELGELLGIKRMTLRQALLNLEAESKI FRKDRKGWFVTQPRFNYSPELSASFQRAAIEQGREPSWGFTEKNRTSDIPETLAPLIAVT PSTELYRITGWGALEGHKVFYHETYINPEVAPGFIEQLENHSFSAVWEKCYQKETVVKKL IFKPVRMPGDISKYLGGSAGMPAILIEKHRADQQGNIVQIDIEYWRFEAVDLIINL P0A8W5 P52049 P76648 Q2M9P5 YQGE_ECOLI UPF0301 protein YqgE yqgE b2948 JW2915 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 IDENTIFICATION BY MASS SPECTROMETRY B / BL21 Belongs to the UPF0301 (AlgH) family. Translation N-terminally shortened. Complete proteome Reference proteome MNLQHHFLIAMPALQDPIFRRSVVYICEHNTNGAMGIIVNKPLENLKIEGILEKLKITPE PRDESIRLDKPVMLGGPLAEDRGFILHTPPSNFASSIRISDNTVMTTSRDVLETLGTDKQ PSDVLVALGYASWEKGQLEQEILDNAWLTAPADLNILFKTPIADRWREAAKLIGVDILTM PGVAGHA P0DSF8 YODE_ECOLI Protein YodE yodE b4780 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 IDENTIFICATION INDUCTION K12 / MG1655 / ATCC 47076 Expressed at high levels equally in exponential and stationary phase in rich medium (at protein level). Overlaps on the same strand with small regulatory RNA RyeG. Complete proteome Reference proteome MGNDAFKLSSADRGDITINNESGHLIVNTAILSGDIVTLRGGEIRLVL P39310 Q2M699 YTFB_ECOLI Cell division protein YtfB ytfB b4206 JW5745 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION SUBCELLULAR LOCATION DOMAIN DISRUPTION PHENOTYPE OVEREXPRESSION Cell division protein whose function is related to the generation of a transient cell wall structure. Function is linked to the late stages of cell division. Cell inner membrane Single-pass membrane protein Localizes to the septal ring prior to the onset of constriction and remains at the midcell throughout cytokinesis. Recruitment to the septal ring requires FtsZ, but not downstream division proteins. The OapA domain binds peptidoglycan. Deletion of the gene has no discernible impact on morphology or cell size. YtfB/dedD double mutant grows as filamentous cells. Overproduction causes cells to filament, most likely by disrupting FtsZ ring assembly. Belongs to the OapA family. Translation N-terminally shortened. Cell cycle Cell division Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MPGRFELKPTLEKVWHAPDNFRFMDPLPPMHRRGIIIAAIVLVVGFLLPSDDTPNAPVVT REAQLDIQSQSQPPTEEQLRAQLVTPQNDPDQVAPVAPEPIQEGQPEEQPQTTQTQPFQP DSGIDNQWRSYRVEPGKTMAQLFRDHGLPATDVYAMAQVEGAGKPLSNLQNGQMVKIRQN ASGVVTGLTIDTGNNQQVLFTRQPDGSFIRAR P76501 Q2MAL4 YFCR_ECOLI Uncharacterized fimbrial-like protein YfcR yfcR b2335 JW2332 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION INDUCTION DISRUPTION PHENOTYPE K12 / MG1655 / ATCC 47076 Part of the yfcOPQRSUV fimbrial operon. Could contribute to adhesion to various surfaces in specific environmental niches. Increases adhesion to eukaryotic T24 bladder epithelial cells in the absence of fim genes. Expression is negatively regulated by H-NS and subjected to cAMP receptor protein (CRP)-mediated catabolite repression. Deletion of the operon under classical laboratory conditions does not result in any major effect on E.coli capacity to form biofilms compared with the wild-type strain. The operon is cryptic under classical laboratory conditions, but is functional when constitutively expressed. Belongs to the fimbrial protein family. Complete proteome Reference proteome Signal MTGGVMSQKFVVGAGLLVCSVCSLSAMAGSKPVDLILRVLVDAPPPCSIKGSQVEFGNMI ADNVDGTNYRQDAKYTLNCTNSLANDLRMQLKGNTSTINGETVLSTNITGLGIRIENSAD NSLFAVGENSWTPFNINNQPQLKAVPVKASGAQLAAGEFNASLTMVVDYQ P0DPP5 A0A385XMM6 YQFI_ECOLI Protein YqfI yqfI b4754 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 IDENTIFICATION INDUCTION Expressed approximately equally in exponential and stationary phases (at protein level). Complete proteome Reference proteome MSKNTKSKNNGIRKYNAKTEVKLVYFK P0AA49 P76519 P76947 P76948 YFDV_ECOLI Uncharacterized transporter YfdV yfdV b2372 JW2369 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] SEQUENCE REVISION K12 / W3110 / ATCC 27325 / DSM 5911 Cell membrane Multi-pass membrane protein Belongs to the auxin efflux carrier (TC 2.A.69) family. Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix Transport MLTFFIGDLLPIIVIMLLGYFSGRRETFSEDQARAFNKLVLNYALPAALFVSITRANREM IFADTRLTLVSLVVIVGCFFFSWFGCYKFFKRTHAEAAVCALIAGSPTIGFLGFAVLDPI YGDSVSTGLVVAIISIIVNAITIPIGLYLLNPSSGADGKKNSNLSALISAAKEPVVWAPV LATILVLVGVKIPAAWDPTFNLIAKANSGVAVFAAGLTLAAHKFEFSAEIAYNTFLKLIL MPLALLLVGMACHLNSEHLQMMVLAGALPPAFSGIIIASRFNVYTRTGTASLAVSVLGFV VTAPLWIYVSRLVS P07021 YFIB_ECOLI Putative lipoprotein YfiB yfiB b2605 JW2586 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 SHOWS THAT THE PROTEIN IS EXPRESSED Cell membrane Lipid-anchor Belongs to the outer membrane OOP (TC 1.B.6) superfamily. Translation N-terminally extended. Cell membrane Complete proteome Lipoprotein Membrane Palmitate Reference proteome Signal MIKHLVAPLVFTSLILTGCQSPQGKFTPEQVAAMQSYGFTESAGDWSLGLSDAILFAKND YKLLPESQQQIQTMAAKLASTGLTHARMDGHTDNYGEDSYNEGLSLKRANVVADAWAMGG QIPRSNLTTQGLGKKYPIASNKTAQGRAENRRVAVVITTP P0ACA1 P32105 Q2M7Q5 YIBF_ECOLI Uncharacterized GST-like protein YibF yibF b3592 JW3565 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [GENOMIC DNA] ECOR 32 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 PUTATIVE FUNCTION IN SELENIUM BIOCHEMISTRY X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE Glutathione (GSH) transferase homolog, that might be involved in selenium metabolism. Belongs to the GST superfamily. HSP26 family. 3D-structure Complete proteome Reference proteome A T MKLVGSYTSPFVRKLSILLLEKGITFEFINELPYNADNGVAQFNPLGKVPVLVTEEGECW FDSPIIAEYIELMNVAPAMLPRDPLESLRVRKIEALADGIMDAGLVSVREQARPAAQQSE DELLRQREKINRSLDVLEGYLVDGTLKTDTVNLATIAIACAVGYLNFRRVAPGWCVDRPH LVKLVENLFSRESFARTEPPKA P0DSG5 YQIM_ECOLI Protein YqiM yqiM b4787 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 IDENTIFICATION INDUCTION K12 / MG1655 / ATCC 47076 Expressed at low levels in exponential phase in rich medium (at protein level). Complete proteome Reference proteome MLMYQTRRTYQNSNNIAVVHLLKPAWR P52143 P76610 P77017 P77019 YPJA_ECOLI Uncharacterized outer membrane protein YpjA ypjA b2647 JW5422 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Cell outer membrane Peripheral membrane protein Cell outer membrane Complete proteome Membrane Reference proteome Signal Transmembrane Transmembrane beta strand MNRTSPYYCRRSVLSLLISALIYAPPGMAAFTTNVIGVVNDETVDGNQKVDERGTTNNTH IINHGQQNVHGGVSNGSLIESGGYQDIGSHNNFVGQANNTTINGGRQSIHDGGISTGTTI ESGNQDVYKGGISNGTTIKGGASRVEGGSANGILIDGGSQIVKVQGHADGTTINKSGSQD VVQGSLATNTTINGGRQYVEQSTVETTTIKNGGEQRVYESRALDTTIEGGTQSLNSKSTA KNTHIYSGGTQIVDNTSTSDVIEVYSGGVLDVRGGTATNVTQHDGAILKTNTNGTTVSGT NSEGAFSIHNHVADNVLLENGGHLDINAYGSANKTIIKDKGTMSVLTNAKADATRIDNGG VMDVAGNATNTIINGGTQNINNYGIATGTNINSGTQNIKSGGKADTTIISSGSRQVVEKD GTAIGSNISAGGSLIVYTGGIAHGVNQETGSALVANTGAGTDIEGYNKLSHFTITGGEAN YVVLENTGELTVVAKTSAKNTTIDTGGKLIVQKEAKTDSTRLNNGGVLEVQDGGEAKHVE QQSGGALIASTTSGTLIEGTNSYGDAFYIRNSEAKNVVLENAGSLTVVTGSRAVDTIINA NGKMDVYGKDVGTVLNSAGTQTIYASATSDKANIKGGKQTVYGLATEANIESGEQIVDGG STEKTHINGGTQTVQNYGKAINTDIVSGLQQIMANGTAEGSIINGGSQVVNEGGLAENSV LNDGGTLDVREKGSATGIQQSSQGALVATTRATRVTGTRADGVAFSIEQGAANNILLANG GVLTVESDTSSDKTQVNMGGREIVKTKATATGTTLTGGEQIVEGVANETTINDGGIQTVS ANGEAIKTKINEGGTLTVNDNGKATDIVQNSGAALQTSTANGIEISGTHQYGTFSISGNL ATNMLLENGGNLLVLAGTEARDSTVGKGGAMQNLGQDSATKVNSGGQYTLGRSKDEFQAL ARAEDLQVAGGTAIVYAGTLADASVSGATGSLSLMTPRDNVTPVKLEGAVRITDSATLTL GNGVDTTLADLTAASRGSVWLNSNNSCAGTSNCEYRVNSLLLNDGDVYLSAQTAAPATTN GIYNTLTTNELSGSGNFYLHTNVAGSRGDQLVVNNNATGNFKIFVQDTGVSPQSDDAMTL VKTGGGDASFTLGNTGGFVDLGTYEYVLKSDGNSNWNLTNDVKPNPDPIPNPKPDPKPDP KPDPNPKPDPTPDPTPTPVPEKRITPSTAAVLNMAATLPLVFDAELNSIRERLNIMKASP HNNNVWGATYNTRNNVTTDAGAGFEQTLTGMTVGIDSRNDIPEGITTLGAFMGYSHSHIG FDRGGHGSVGSYSLGGYASWEHESGFYLDGVVKLNRFKSNVAGKMSSGGAANGSYHSNGL GGHIETGMRFTDGNWNLTPYASLTGFTADNPEYHLSNGMKSKSVDTRSIYRELGATLSYN MRLGNGMEVEPWLKAAVRKEFVDDNRVKVNSDGNFVNYLSGRRGIYQAGIKASFSSTLSG HLGVGYSHSAGVESPWNAVAGVNWSF P75976 YMFL_ECOLI Uncharacterized protein YmfL ymfL b1147 JW1133 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Complete proteome Reference proteome MGKHHWKIEKQPEWYVKAVRKTIAALPSGYAEAADWLDVTENALFNRLRADGDQIFPLGW AMVLQRAGGTHFIADAVAQSANGVFVSLPDVEDVDNADINQRLLEVIEQIGSYSKQIRSA IEDGVVEPHEKTAINDELYLSISKLQEHAALVYKIFCISESNDARECAAPGVVASIASGC GETNA P0AAN5 P08366 Q2MC36 YAIA_ECOLI Uncharacterized protein YaiA yaiA b0389 JW0380 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 3D-structure Complete proteome Reference proteome MPTKPPYPREAYIVTIEKGKPGQTVTWYQLRADHPKPDSLISEHPTAQEAMDAKKRYEDP DKE P0A858 P04790 Q2M8L5 TPIS_ECOLI Triosephosphate isomerase TIM TPI 5.3.1.1 Triose-phosphate isomerase tpiA tpi b3919 JW3890 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] CATALYTIC ACTIVITY NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 PROTEIN SEQUENCE OF 1-9 K12 / W3110 / ATCC 27325 / DSM 5911 PROTEIN SEQUENCE OF 1-14 K12 / EMG2 PROTEIN SEQUENCE OF 1-8 K12 PROTEIN SEQUENCE OF 1-4 K12 / W3110 / ATCC 27325 / DSM 5911 INDUCTION FUNCTION CATALYTIC ACTIVITY BIOPHYSICOCHEMICAL PROPERTIES INDUCTION K12 / W3110 DISRUPTION PHENOTYPE K12 / BW25113 X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) SUBUNIT X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) SUBUNIT X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) SUBUNIT Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate 1030 uM for D-glyceraldehyde 3-phosphate (at 25 degrees Celsius) Kcat is 54000 min(-1) for isomerase activity with D-glyceraldehyde 3-phosphate as substrate (at 25 degrees Celsius). Carbohydrate biosynthesis; gluconeogenesis. Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1. Homodimer. false 3 P29745 pepT false 7 P09373 pflB false 7 Cytoplasm Induced by CsrA and repressed by spermidine. Cells lacking this gene accumulates methylglyoxal and are unable to grow on glucose, lactate or other carbon sources. Belongs to the triosephosphate isomerase family. 3D-structure Complete proteome Cytoplasm Direct protein sequencing Gluconeogenesis Glycolysis Isomerase Reference proteome D N MRHPLVMGNWKLNGSRHMVHELVSNLRKELAGVAGCAVAIAPPEMYIDMAKREAEGSHIM LGAQNVDLNLSGAFTGETSAAMLKDIGAQYIIIGHSERRTYHKESDELIAKKFAVLKEQG LTPVLCIGETEAENEAGKTEEVCARQIDAVLKTQGAAAFEGAVIAYEPVWAIGTGKSATP AQAQAVHKFIRDHIAKVDANIAEQVIIQYGGSVNASNAAELFAQPDIDGALVGGASLKAD AFAVIVKAAEAAKQA P76043 P78306 YCJQ_ECOLI Uncharacterized zinc-type alcohol dehydrogenase-like protein YcjQ 1.-.-.- ycjQ b1313 JW1306 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] SEQUENCE REVISION TO 234-243 K12 / W3110 / ATCC 27325 / DSM 5911 Zn(2+) Belongs to the zinc-containing alcohol dehydrogenase family. Complete proteome Metal-binding Oxidoreductase Reference proteome Zinc MKKLVATAPRVAALVEYEDRAILANEVKIRVRFGAPKHGTEVVDFRAASPFIDEDFNGEW QMFTPRPADAPRGIEFGKFQLGNMVVGDIIECGSDVTDYAVGDSVCGYGPLSETVIINAV NNYKLRKMPQGSSWKNAVCYDPAQFAMSGVRDANVRVGDFVVVVGLGAIGQIAIQLAKRA GASVVIGVDPIAHRCDIARRHGADFCLNPIGTDVGKEIKTLTGKQGADVIIETSGYADAL QSALRGLAYGGTISYVAFAKPFAEGFNLGREAHFNNAKIVFSRACSEPNPDYPRWSRKRI EETCWELLMNGYLNCEDLIDPVVTFANSPESYMQYVDQHPEQSIKMGVTF P76134 P77755 YDEM_ECOLI Anaerobic sulfatase-maturating enzyme homolog YdeM AnSME homolog ydeM b1497 JW1492 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NON-INVOLVEMENT IN SULFATASE MATURATION K12 / BW25113 [4Fe-4S] cluster Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. iron-sulfur cluster May bind at least one other iron-sulfur cluster. Belongs to the radical SAM superfamily. Anaerobic sulfatase-maturating enzyme family. Despite its homology to the anaerobic sulfatase-maturating enzymes, it is not involved in Cys-type sulfatase maturation in vivo. 4Fe-4S Complete proteome Iron Iron-sulfur Metal-binding Reference proteome S-adenosyl-L-methionine MHVTAKPSSFQCNLKCDYCFYLEKESQFTHEKWMDDSTLKEFIKQYIAASGNQVYFTWQG GEPTLAGLDFFRKVIHYQQRYAGQKRIFNALQTNGILLNNEWCAFLKEHEFLVGISIDGP QELHDRYRRSNSGNGTFAKVIAAIERLKSYQVEFNTLTVINNVNVHYPLEVYHFLKSIGS KHMQFIELLETGTPNIDFSGHSENTFRIIDFSVPPTAYGKFMSTIFMQWVKNDVGEIFIR QFESFVSRFLGNGHTSCIFQESCKDNLVVESNGDIYECDHFVYPQYKIGNINKSELKTMN SVQLTAQKKRIPAKCQQCAYKPICNGGCPKHRITKVNNETVSYFCEGYKILFSTMVPYMN AMVELAKNRVPLYHIMDVAKQMENN P28911 P76702 Q2M7E6 YHHH_ECOLI Uncharacterized protein YhhH ORF-B2 yhhH b3483 JW3449 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [GENOMIC DNA] ECOR 32 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Translation N-terminally extended. Complete proteome Reference proteome MSAEFMVICKKILFRNCVIVSLFVFTYNTWAQCNNNIKIMRKYESEGKYTVRNLVKNKAI ALELAEIYVKNRYGQDAAEEEKPYEITELTTSWVVEGTIHSDQIAGGVFIIEIGKNDGRI LNFGHGK P0AD27 P33922 P33923 Q2MAQ3 YEJM_ECOLI Inner membrane protein YejM yejM yejN b2188 JW2176 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / BHB2600 SEQUENCE REVISION NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 TOPOLOGY [LARGE SCALE ANALYSIS] K12 / MG1655 / ATCC 47076 Cell inner membrane Multi-pass membrane protein To H.influenzae HI_0842. 3D-structure Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MVTHRQRYREKVSQMVSWGHWFALFNILLSLVIGSRYLFIADWPTTLAGRIYSYVSIIGH FSFLVFATYLLILFPLTFIVGSQRLMRFLSVILATAGMTLLLIDSEVFTRFHLHLNPIVW QLVINPDENEMARDWQLMFISVPVILLLELVFATWSWQKLRSLTRRRRFARPLAAFLFIA FIASHVVYIWADANFYRPITMQRANLPLSYPMTARRFLEKHGLLDAQEYQRRLIEQGNPD AVSVQYPLSELRYRDMGTGQNVLLITVDGLNYSRFEKQMPALAGFAEQNISFTRHMSSGN TTDNGIFGLFYGISPSYMDGILSTRTPAALITALNQQGYQLGLFSSDGFTSPLYRQALLS DFSMPSVRTQSDEQTATQWINWLGRYAQEDNRWFSWVSFNGTNIDDSNQQAFARKYSRAA GNVDDQINRVLNALRDSGKLDNTVVIITAGRGIPLSEEEETFDWSHGHLQVPLVIHWPGT PAQRINALTDHTDLMTTLMQRLLHVSTPASEYSQGQDLFNPQRRHYWVTAADNDTLAITT PKKTLVLNNNGKYRTYNLRGERVKDEKPQLSLLLQVLTDEKRFIAN P0DSF6 YECV_ECOLI Protein YecV yecV b4778 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 IDENTIFICATION INDUCTION K12 / MG1655 / ATCC 47076 Expressed in both exponential and stationary phase in rich medium; expression is higher in exponential phase (at protein level). Complete proteome Reference proteome MSIFRIHLDGNKKA P75839 YCAP_ECOLI UPF0702 transmembrane protein YcaP ycaP b0906 JW0889 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Cell membrane Multi-pass membrane protein Belongs to the UPF0702 family. Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MKAFDLHRMAFDKVPFDFLGEVALRSLYTFVLVFLFLKMTGRRGVRQMSLFEVLIILTLG SAAGDVAFYDDVPMVPVLIVFITLALLYRLVMWLMAHSEKLEDLLEGKPVVIIEDGELAW SKLNNSNMTEFEFFMELRLRGVEQLGQVRLAILETNGQISVYFFEDDKVKPGLLILPSDC TQRYKVVPESADYACIRCSEIIHMKAGEKQLCPRCANPEWTKASRAKRVT P76296 Q2MB07 YECT_ECOLI Uncharacterized protein YecT yecT b1877 JW5310 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 To R.meliloti R02472. Complete proteome Reference proteome MFKFLVLTLGIISCQAYAEDTVIVNDHDISAIKDCWQKNSDDDTDVNVIKSCLRQEYNLV DAQLNKAYGEAYRYIEQVPRTGVKKPDTEQLNLLKKSQRAWLDFRDKECELILSNEDVQD LSDPYSESEWLSCMIIQTNTRTRQLQLYRNSEDFYPSPLTRG P64562 P52038 Q2M9S7 YQFE_ECOLI Putative protein YqfE yqfE b2915 JW2882 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Could be the product of a pseudogene, it is missing up to 240 N-terminal residues compared to orthologs. Complete proteome Reference proteome MHFAQRVRALVVLNGVALLPQFACKQGLANGELVRLFAPWSGIPRPLYALFAGRKGMPAI ARYFMDELTTRLANGV P52102 Q2MAG8 YFHL_ECOLI Ferredoxin YfhL EcFd yfhL b2562 JW2546 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 2-86 IN COMPLEX WITH IRON-SULFUR (4FE-4S) COFACTOR BIOPHYSICOCHEMICAL PROPERTIES Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. [4Fe-4S] cluster Binds 2 [4Fe-4S] cluster. E(0) is -675 mV for the cluster 1, and -418 mV for the cluster 2. 3D-structure 4Fe-4S Complete proteome Electron transport Iron Iron-sulfur Metal-binding Reference proteome Repeat Transport MALLITKKCINCDMCEPECPNEAISMGDHIYEINSDKCTECVGHYETPTCQKVCPIPNTI VKDPAHVETEEQLWDKFVLMHHADKI P64596 P45467 Q2M960 YRAP_ECOLI Uncharacterized protein YraP yraP b3150 JW3119 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Periplasm Complete proteome Periplasm Reference proteome Repeat Signal MKALSPIAVLISALLLQGCVAAAVVGTAAVGTKAATDPRSVGTQVDDGTLEVRVNSALSK DEQIKKEARINVTAYQGKVLLVGQSPNAELSARAKQIAMGVDGANEVYNEIRQGQPIGLG EASNDTWITTKVRSQLLTSDLVKSSNVKVTTENGEVFLMGLVTEREAKAAADIASRVSGV KRVTTAFTFIK P37675 Q2M7P1 Q6BF20 YIAN_ECOLI 2,3-diketo-L-gulonate TRAP transporter large permease protein YiaN yiaN b3578 JW5651 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 SEQUENCE REVISION NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 PRELIMINARY FUNCTION K12 DELETION STUDIES K12 FUNCTION K12 / W3110 / ATCC 27325 / DSM 5911 Part of the tripartite ATP-independent periplasmic (TRAP) transport system YiaMNO involved in the uptake of 2,3-diketo-L-gulonate. The complex comprises the extracytoplasmic solute receptor protein YiaO, and the two transmembrane proteins YiaM and YiaN. Cell inner membrane Multi-pass membrane protein Belongs to the TRAP transporter large permease family. Was originally proposed to be a subunit from an L-xylulose uptake system, but PubMed:16385129 shows that it does not bind L- or D-xylulose. Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix Transport MAVLIFLGCLLGGIAIGLPIAWALLLCGAALMFWLDMFDVQIMAQTLVNGADSFSLLAIP FFVLAGEIMNAGGLSKRIVDLPMKLVGHKPGGLGYVGVLAAMIMASLSGSAVADTAAVAA LLVPMMRSANYPVNRAAGLIASGGIIAPIIPPSIPFIIFGVSSGLSISKLFMAGIAPGMM MGATLMLTWWWQASRLNLPRQQKATMQEIWHSFVSGIWALFLPVIIIGGFRSGLFTPTEA GAVAAFYALFVATVIYREMTFATLWHVLIGAAKTTSVVMFLVASAQVSAWLITIAELPMM VSDLLQPLVDSPRLLFIVIMVAILIVGMVMDLTPTVLILTPVLMPLVKEAGIDPIYFGVM FIINCSIGLITPPIGNVLNVISGVAKLKFDDAVRGVFPYVLVLYSLLVVFVFIPDLIILP LKWIN P52126 Q2MAE4 YFJK_ECOLI Uncharacterized protein YfjK yfjK b2627 JW2608 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Complete proteome Reference proteome MTEIYEQAKHSLQGEDFSSFNYLFAVNKLLSNPVSYDLGRDLIVRALDSRERFSEHTTIL KNMVRKSGLFPYLKKEFTSLTPDDLRVLELYRTPFSDGYVFHSMQFHIFDLLKSGQNVVL SAPTSMGKSAIVDSLLGMGTLKRLVLVVPTVALADETRRRLQERFGDRYQIIHHSSQVCH SDQAVYVLTQERVNERDDIVDIDLFVIDEFYKLAFRQLKSGDIDHQDERVIELNIALSKL LKVSRQFYLTGPFVNSIRGLEKLGYPHTFVSTDFNTVALDVKTFGIKANDDKAKLKALGE IAHACVDATIIYCKSPTVAGLVARELIRLGHGTPTENPHVDWVSEEFDADWDYTVALRNG IGLHFGALPRALQQYTADQFNAGKLRFLLCTSTIIEGVNTIAKNVVIYDNRDGTRSIDKF THGNIKGRAGRMGVHFVGKIFCLEEIPEDNLNQEVDIPLGIQGIDTPINLLASVQPDHLS EFSQDRFDEVFINDRVSIDLVKKHSYFRVEQFEMLQSMFEMMDDNEFSSLVFHWTPATNF LKTFAKIIARLVPHTFSRNGVPVKPTDVMIAKLAGYLSAESYSEYLKNQIDYARQWISEG EKRTLSIALNNDLKLITNTFGYTLPKVLSLMEDVVKHHAVKRGIRSKVDYTHVKLAFESF HLPPGVNALEEIGIPIQTLHRLVDLLEFSDEADVDELSQYLRDTQDIWSRSIGYVDQMFI RRALGIRRH P56614 Q9R302 Q9ZN60 YMDF_ECOLI Uncharacterized protein YmdF ymdF b4518 JW5136 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 IDENTIFICATION Belongs to the con-10 family. Complete proteome Reference proteome MANHRGGSGNFAEDRERASEAGKKGGQHSGGNFKNDPQRASEAGKKGGKSSHGKSDN P46890 P77158 Q2MBY1 YBAE_ECOLI Uncharacterized protein YbaE ybaE b0445 JW0435 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-358 K12 / MC4100 / ATCC 35695 / DSM 6574 Complete proteome Reference proteome MRLLNRLNQYQRLWQPSAGKPQTVTVSELAERCFCSERHVRTLLRQAQEAGWLEWQAQSG RGKRGQLRFLVTPESLRNAMMEQALETGKQQDVLELAQLAPGELRTLLQPFMGGQWQNDT PTLRIPYYRPLEPLQPGFLPGRAEQHLAGQIFSGLTRFDNNTQRPIGDLAHHWETSTDGL RWDFYLRSTLHWHNGDAVKASHLHQRLLMLLQLPALDQLFISVKRIEVTHPQCLTFFLHR PDYWLAHRLASYCSHLAHPQFPLIGTGPFRLTQFTAELVRLESHDYYHLRHPLLKAVEYW ITPPLFEKDLGTSCRHPVQITIGKPEELQRVSQVSSGISLGFCYLTLRKSPRLSLWQARK VISIIHQSGLLQTLEVGENLITASHALLPGWTIPHWQVPDEVKLPKTLTLVYHLPIELHT MAERLQATLAAEGCELTIIFHNAKNWDDTTLQAHADLMMGDRLIGEAPEYTLEQWLRCDP LWPHVFDAPAYAHLQSTLDAVQIMPDEENRFNALKAVFSQLMTDATLTPLFNYHYRISAP PGVNGVRLTPRGWFEFTEAWLPAPSQ P0DPN9 A0A385XJE8 YMGL_ECOLI Protein YmgL ymgL b4739 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 IDENTIFICATION INDUCTION Expressed approximately equally in exponential and stationary phases (at protein level). Complete proteome Reference proteome MEIKVQRLSLWMINTVFLLSPINNHQTNTINLIFEM P55914 Q2EEU5 Q2M5U8 YJJZ_ECOLI Uncharacterized protein YjjZ yjjZ b4567 JW5797 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 IDENTIFICATION Complete proteome Reference proteome MLQRTLGSGWGVLLPGLLIAGLMYADLSSDQWRIVILMGLVLTPMMLYHKQLRHYILLPS CLALIAGIMLMIMNLNQG P77657 Q2MCE5 YAGK_ECOLI Uncharacterized protein YagK yagK b0277 JW0271 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 To E.coli YfjJ. Complete proteome Reference proteome MKTYQGTHGVHILEYQSKINKLLCYLTNRYPRLIAVRVDLHYPKIVDNGDNICCFPNLEP GVISRMRESLRAKLEADRTRKVREDKRIYRCPLFIIWAKEYSESGKCHYHICLLFNKDAY YHLGDYDQDDNLRGMITGAWYSALRLERDDHPGLVHFPENCKYVLDTNSTDFQQNYQALL TRLDYLTKVESKVFGEGDRNFGCSQIEL P21367 YCAC_ECOLI Probable hydrolase YcaC 4.-.-.- ycaC b0897 JW0880 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 / C600 / ATCC 23724 / DSM 3925 / LMG 3041 / NCIB 10222 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) SUBUNIT Homooctamer composed of two tetrameric rings. 3D-structure Complete proteome Hydrolase Lyase Reference proteome MTKPYVRLDKNDAAVLLVDHQAGLLSLVRDIEPDKFKNNVLALGDLAKYFNLPTILTTSF ETGPNGPLVPELKAQFPDTPYIARPGNINAWDNEDFVKAVKATGKKQLIIAGVVTEVCVA FPALSAIEEGFDVFVVTDASGTFNEITRHSAWDRLSQAGAQLMTWFGVACELHRDWRNDI EGLATLFSNHIPDYRNLMTSYDTLTKQK P29013 P76006 YCGB_ECOLI Uncharacterized protein YcgB ycgB b1188 JW1177 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-443 K12 To B.subtilis SpoVR. Complete proteome Reference proteome MATIDSMNKDTTRLSDGPDWTFDLLDVYLAEIDRVAKLYRLDTYPHQIEVITSEQMMDAY SSVGMPINYPHWSFGKKFIETERLYKHGQQGLAYEIVINSNPCIAYLMEENTITMQALVM AHACYGHNSFFKNNYLFRSWTDASSIVDYLIFARKYITECEERYGVDEVERLLDSCHALM NYGVDRYKRPQKISLQEEKARQKSREEYLQSQVNMLWRTLPKREEEKTVAEARRYPSEPQ ENLLYFMEKNAPLLESWQREILRIVRKVSQYFYPQKQTQVMNEGWATFWHYTILNHLYDE GKVTERFMLEFLHSHTNVVFQPPYNSPWYSGINPYALGFAMFQDIKRICQSPTEEDKYWF PDIAGSDWLETLHFAMRDFKDESFISQFLSPKVMRDFRFFTVLDDDRHNYLEISAIHNEE GYREIRNRLSSQYNLSNLEPNIQIWNVDLRGDRSLTLRYIPHNRAPLDRGRKEVLKHVHR LWGFDVMLEQQNEDGSIELLERCPPRMGNL P10908 P22633 Q2M7B2 UGPQ_ECOLI Glycerophosphodiester phosphodiesterase, cytoplasmic Glycerophosphoryl diester phosphodiesterase, cytoplasmic 3.1.4.46 ugpQ b3449 JW3414 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50 K12 CATALYTIC ACTIVITY COFACTOR BIOPHYSICOCHEMICAL PROPERTIES SUBCELLULAR LOCATION INDUCTION K12 Glycerophosphoryl diester phosphodiesterase hydrolyzes deacylated phospholipids to G3P and the corresponding alcohols. a sn-glycero-3-phosphoester + H2O = an alcohol + H(+) + sn-glycerol 3-phosphate Mg(2+) Co(2+) Mn(2+) 0.22 mM for glycerophosphoethanolamine 0.66 mM for glycerophosphoserine 0.62 mM for glycerophosphoglycerol 0.39 mM for glycerophosphoinositol 2.0 mM for glycerophosphocholine Optimum pH is 7.5. Cytoplasm Up-regulated by low levels of phosphate in the medium. There are 2 isozymes of glycerophosphoryl diester phosphodiesterase in E.coli: a periplasmic isozyme (GlpQ) and a cytosolic isozyme (UgpQ). Belongs to the glycerophosphoryl diester phosphodiesterase family. Complete proteome Cytoplasm Glycerol metabolism Hydrolase Magnesium Metal-binding Reference proteome MSNWPYPRIVAHRGGGKLAPENTLASIDVGAKYGHKMIEFDAKLSKDGEIFLLHDDNLER TSNGWGVAGELNWQDLLRVDAGSWYSKMFKGEPLPLLSQVAERCREHGMMANIEIKPTTG TGPLTGKMVALAARELWAGMTPPLLSSFEIDALEAAQQAAPELPRGLLLDEWRDDWRELT ARLGCVSIHLNHKLLNKARVMQLKDAGLRILVYTVNKPQRAAELLRWGVDCICTDAIDVI GPNFTAQ P76628 P76629 Q2MAC3 YGAY_ECOLI Putative uncharacterized transporter YgaY ygaY b2681 JW2655 b2680 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 CONCEPTUAL TRANSLATION Cell inner membrane Multi-pass membrane protein Belongs to the major facilitator superfamily. Could be the product of a pseudogene. There seems to be a natural frameshift that produces two separate ORFs. Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix Transport MTKPNHELSPALIVLMSIATGLAVASNYYAQPLLDTIARNFSLSASSAGFIVTAAQLGYA AGLLFLVPLGDMFERRRLIVSMTLLAAGGMLITASSQSLAMMILGTALTGLFSVVAQILV PLAATLASPDKRGKVVGTIMSGLLLGILLARTVAGLLANLGGWRTVFWVASVLMALMALA LWRGLPQMKSETHLNYPQLLGSVFSMFISDKILRTRALLGCLTFANFSILWTSMAFLLAA PPFNYSDGVIGLFGLAGAAGALGARPAGGFADKGKSHHTTTFGLLLLLLSWLAIWFGHTS VLALIIGILVLDLTVQGVHITNQTVIYRIHPDARNRLTAGYMTSYFIGGAAGSLISASAW QHGGWAGVCLAGATIALVNLLVWWRGFHRQEAAN P64592 P42622 Q2M9A2 YHAI_ECOLI Inner membrane protein YhaI yhaI b3104 JW3075 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 TOPOLOGY [LARGE SCALE ANALYSIS] K12 / MG1655 / ATCC 47076 Cell inner membrane Multi-pass membrane protein To E.coli YhaH. Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MQWYLSVLKNYVGFSGRARRKEYWMFTLINAIVGAIINVIQLILGLELPYLSMLYLLATF LPVLALAIRRLHDTDRSGAWALLFFVPFIGWLVLLVFFCTEGTSGSNRYGNDPKFGSN Q46791 Q2M9Y2 Q2M9Y3 Q46792 YGEK_ECOLI Uncharacterized response regulatory protein YgeK ygeK ygeL b2856 JW5458/JW2824 b2855 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 PHOSPHORYLATION K12 / W3110 / ATCC 27325 / DSM 5911 Overexpressed protein is phosphorylated in vitro by non-cognate histidine kinases BarA and UhpB. Lacks the N-terminal receiver domain usually found in response regulators, which is usally phosphorylated by the cognate histidine kinase. Translation N-terminally shortened. Complete proteome DNA-binding Phosphoprotein Reference proteome Transcription Transcription regulation MGAELVKWVKSHKIDAHIITFVAKMPYIDSIKLLEAGAKGCVWKTSHPAKLNRAIDSISN GYTYFDSVHMDCEKISSRYSSDNQLTNRESEILQLIADGKTNKEIANFLQLSRKTVETHR LNIMKKLDVHSGIELIKTALRMGVCTI P32717 Q2M6M1 YJCS_ECOLI Putative alkyl/aryl-sulfatase YjcS 3.1.6.- yjcS b4083 JW5721 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] SEQUENCE REVISION TO 614 K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Belongs to the metallo-beta-lactamase superfamily. Translation N-terminally shortened. 3D-structure Complete proteome Hydrolase Reference proteome Signal H D MNNSRLFRLSRIVIALTAASGMMVNTANAKEEAKAATQYTQQVNQNYAKSLPFSDRQDFD DAQRGFIAPLLDEGILRDANGKVYYRADDYKFDINAAAPETVNPSLWRQSQINGISGLFK VTDKMYQVRGQDISNITFVEGEKGIIVIDPLVTPPAAKAALDLYFQHRPQKPIVAVIYTH SHTDHYGGVKGIISEADVKSGKVQVIAPAGFMDEAISENVLAGNIMSRRALYSYGLLLPH NAQGNVGNGLGVTLATGDPSIIAPTKTIVRTGEKMIIDGLEFDFLMTPGSEAPAEMHFYI PALKALCTAENATHTLHNFYTLRGAKTRDTSKWTEYLNETLDMWGNDAEVLFMPHTWPVW GNKHINDYIGKYRDTIKYIHDQTLHLANQGYTMNEIGDMIKLPPALANNWASRGYYGSVS HNARAVYNFYLGYYDGNPANLHPYGQVEMGKRYVQALGGSARVINLAQEANKQGDYRWSA ELLKQVIAANPGDQVAKNLQANNFEQLGYQAESATWRGFYLTGAKELREGVHKFSHGTTG SPDTIRGMSVEMLFDFMAVRLDSAKAAGKNISLNFNMSNGDNLNLTLNDSVLNYRKTLQP QADASFYISREDLHAVLTGQAKMADLVKAKKAKIIGNGAKLEEIIACLDNFDLWVNIVTP N P0DSH1 YSAE_ECOLI Protein YsaE ysaE b4793 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 IDENTIFICATION INDUCTION K12 / MG1655 / ATCC 47076 Expressed in both exponential and stationary phase in rich medium; expression is considerably higher during exponential phase (at protein level). Complete proteome Reference proteome MRNAVSKAGIISRRRLLLFQFAG P0AF73 P39289 Q2M6C9 YJET_ECOLI Uncharacterized protein YjeT yjeT b4176 JW4134 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Cell membrane Multi-pass membrane protein Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MNSTIWLALALVLVLEGLGPMLYPKAWKKMISAMTNLPDNILRRFGGGLVVAGVVVYYML RKTIG P75711 Q2MBR8 YBBV_ECOLI Uncharacterized protein YbbV ybbV b0510 JW0498 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Complete proteome Reference proteome MNRPAILKKKAAKDVASVLKIIFLFYLFLIARLKQRYSIREIKRDLWNIRENYSSNAAIA KIYCRKRKASGPGKHLTILPYGWVRFITFPIM P64612 P46442 Q2M8Y1 ZAPE_ECOLI Cell division protein ZapE Z ring-associated protein ZapE zapE yhcM b3232 JW3201 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION INTERACTION WITH FTSZ SUBCELLULAR LOCATION DISRUPTION PHENOTYPE GENE NAME MUTAGENESIS OF LYS-84 K12 / MG1655 / ATCC 47076 Reduces the stability of FtsZ polymers in the presence of ATP. Required for cell division under low-oxygen conditions. Hydrolyzes ATP but not GTP. Interacts with FtsZ. Cytoplasm Localizes to the constricting Z-ring during late stages of the cell division process. Mutants have no growth defect in aerobic conditions. However, inactivation leads to a stress-dependent elongated phenotype (in anaerobiosis or at temperatures over 37 degrees Celsius). ZapE abundance has to be tightly regulated to allow cell division. Loss or overexpression of ZapE alters Z-ring stability and leads to bacterial filamentation (PubMed:24595368). Belongs to the AFG1 ATPase family. ZapE subfamily. ATP-binding Cell cycle Cell division Complete proteome Cytoplasm Hydrolase Nucleotide-binding Reference proteome K A MQSVTPTSQYLKALNEGSHQPDDVQKEAVSRLEIIYQELINSTPPAPRTSGLMARVGKLW GKREDTKHTPVRGLYMWGGVGRGKTWLMDLFYQSLPGERKQRLHFHRFMLRVHEELTALQ GQTDPLEIIADRFKAETDVLCFDEFFVSDITDAMLLGGLMKALFARGITLVATSNIPPDE LYRNGLQRARFLPAIDAIKQHCDVMNVDAGVDYRLRTLTQAHLWLSPLHDETRAQMDKLW LALAGGKRENSPTLEINHRPLATMGVENQTLAVSFTTLCVDARSQHDYIALSRLFHTVML FDVPVMTRLMESEARRFIALVDEFYERHVKLVVSAEVPLYEIYQGDRLKFEFQRCLSRLQ EMQSEEYLKREHLAG P46850 P76690 Q2M785 RTCB_ECOLI RNA-splicing ligase RtcB 6.5.1.- rtcB yhgL b3421 JW3384 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 GENE NAME FUNCTION SUBUNIT INDUCTION K12 FUNCTION COFACTOR FUNCTION COFACTOR FUNCTION FUNCTION IDENTIFICATION BY MASS SPECTROMETRY ACTIVE SITE REACTION MECHANISM MUTAGENESIS OF HIS-337 FUNCTION REACTION MECHANISM RNA ligase that mediates the joining of broken tRNA-like stem-loop structures in case of tRNA damage. Probably participates to tRNA restriction-repair by ligating broken tRNA-like stem-loop structures with 2',3'-cyclic phosphate and 5'-OH ends to form a splice junction with a 2'-OH, 3',5'-phosphodiester, a step that requires GTP (PubMed:21224389, PubMed:22730297). Also acts as a DNA ligase in case of DNA damage by splicing 'dirty' DNA breaks, characterized by 3'-PO4 (or cyclic-PO4) and 5'-OH ends that cannot be sealed by classical DNA ligases (PubMed:24218597). Mn(2+) Binds 2 manganese ions per subunit. Monomer. Expression is repressed by RtcR. In contrast to the vertebrate homolog, ligation does not seem to require ATP, while GTP stimulates activity. Ligation proceeds through 3 nucleotidyl transfer steps, with 2',3'-cyclic phosphate termini being hydrolyzed to 3'-P termini in a step that precedes 3'-P activation with GMP. In the first nucleotidyl transfer step, RtcB reacts with GTP to form a covalent RtcB-histidine-GMP intermediate with release of PPi; in the second step, the GMP moiety is transferred to the RNA 3'-P; in the third step, the 5'-OH from the opposite RNA strand attacks the activated 3'-P to form a 3',5'-phosphodiester bond and release GMP (PubMed:22474365). Acts as a DNA ligase by attaching a GMP nucleotide to the DNA 3'-PO4 end to activate it for nucleophilic attack by the 5'-OH (PubMed:24218597). Belongs to the RtcB family. Complete proteome DNA damage DNA repair Ligase Manganese Metal-binding Reference proteome H A N Q R G MNYELLTTENAPVKMWTKGVPVEADARQQLINTAKMPFIFKHIAVMPDVHLGKGSTIGSV IPTKGAIIPAAVGVDIGCGMNALRTALTAEDLPENLAELRQAIETAVPHGRTTGRCKRDK GAWENPPVNVDAKWAELEAGYQWLTQKYPRFLNTNNYKHLGTLGTGNHFIEICLDESDQV WIMLHSGSRGIGNAIGTYFIDLAQKEMQETLETLPSRDLAYFMEGTEYFDDYLKAVAWAQ LFASLNRDAMMENVVTALQSITQKTVRQPQTLAMEEINCHHNYVQKEQHFGEEIYVTRKG AVSARAGQYGIIPGSMGAKSFIVRGLGNEESFCSCSHGAGRVMSRTKAKKLFSVEDQIRA TAHVECRKDAEVIDEIPMAYKDIDAVMAAQSDLVEVIYTLRQVVCVKG P77318 P78159 YDEN_ECOLI Uncharacterized sulfatase YdeN 3.1.6.- ydeN b1498 JW5243 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Ca(2+) Binds 1 Ca(2+) ion per subunit. The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity. Belongs to the sulfatase family. Calcium Complete proteome Hydrolase Metal-binding Reference proteome Signal MKSALKKSVVSTSISLILASGMAAFAAHAADDVKLKATKTNVAFSDFTPTEYSTKGKPNI IVLTMDDLGYGQLPFDKGSFDPKTMENREVVDTYKIGIDKAIEAAQKSTPTLLSLMDEGV RFTNGYVAHGVSGPSRAAIMTGRAPARFGVYSNTDAQDGIPLTETFLPELFQNHGYYTAA VGKWHLSKISNVPVPEDKQTRDYHDNFTTFSAEEWQPQNRGFDYFMGFHAAGTAYYNSPS LFKNRERVPAKGYISDQLTDEAIGVVDRAKTLDQPFMLYLAYNAPHLPNDNPAPDQYQKQ FNTGSQTADNYYASVYSVDQGVKRILEQLKKNGQYDNTIILFTSDNGAVIDGPLPLNGAQ KGYKSQTYPGGTHTPMFMWWKGKLQPGNYDKLISAMDFYPTALDAADISIPKDLKLDGVS LLPWLQDKKQGEPHKNLTWITSYSHWFDEENIPFWDNYHKFVRHQSDDYPHNPNTEDLSQ FSYTVRNNDYSLVYTVENNQLGLYKLTDLQQKDNLAAANPQVVKEMQGVVREFIDSSQPP LSEVNQEKFNNIKKALSEAK P0AD10 P52092 P76307 YECJ_ECOLI Uncharacterized protein YecJ yecJ b4537 JW1891 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 / EMG2 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 IDENTIFICATION Complete proteome Reference proteome MSQPLNADQELVSDVVACQLVIKQILDVLDVIAPVEVREKMSSQLKNIDFTNHPAAADPV TMRAIQKAIALIELKFTPQGESH P76137 A0A385XJH7 Q79EJ5 YDET_ECOLI Fimbrial usher domain-containing protein YdeT ydeT b1505 JW1499 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 DISRUPTION PHENOTYPE K12 / BW25113 Increased biofilm formation. Complete proteome Reference proteome MSGYTVKPPTGDTNEQTQFIDYFNLFYSKRGQEQISISQQLGNYGTTFFSASRQSYWNTS RSDQQISFGLNVPFGDITTSLNYSYSNNIWQNDRDHLLAFTLNVPFSHWMRTDSQSAFRN SNASYSMSNDLKGGMTNLSGVYGTLLPDNNLNYSVQVGNTHGGNTSSGTSGYSSLNYRGA YGNTNVGYSRSGDSSQIYYGMSGGIIAHADGITFGQPLGDTMVLVKAPGADNVKIENQTG IHTDWRGYAILPFATEYRENRVALNANSLADNVELDETVVTVIPTHGAIARATFNAQIGG KVLMTLKYGNKSVPFGAIVTHGENKNGSIVAENGQVYLTGLPQSGQLQVSWGKDKNSNCI VEYKLPEVSPGTLLNQQTAICR P32693 Q2M6Q7 YJBL_ECOLI Uncharacterized protein YjbL yjbL b4047 JW4007 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Complete proteome Reference proteome MLKIIPGATGYFNKTLNSNQFDNEDAIKDKLDNRGSIKGKLNNIYGKSIDYAALRHRDII IAKIDLFIQRITHNLWHARKKMCF P07024 P78274 Q2MBU7 USHA_ECOLI Protein UshA UDP-sugar hydrolase 3.6.1.45 UDP-sugar diphosphatase UDP-sugar pyrophosphatase 5'-nucleotidase 5'-NT 3.1.3.5 ushA b0480 JW0469 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] PROTEIN SEQUENCE OF 26-27 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-41 K12 / DH5-alpha PROTEIN SEQUENCE OF 26-37 K12 / EMG2 X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 26-550 X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE; PRODUCT AND INHIBITOR X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE Degradation of external UDP-glucose to uridine monophosphate and glucose-1-phosphate, which can then be used by the cell. UDP-sugar + H(2)O = UMP + alpha-D-aldose 1-phosphate. a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate Zn(2+) Binds 2 Zn(2+) ions per subunit. The activity of this protein is inhibited by an intracellular protein inhibitor. Monomer. Periplasm Exported from the cell, except a small proportion that is internally localized. Belongs to the 5'-nucleotidase family. 3D-structure Complete proteome Direct protein sequencing Disulfide bond Hydrolase Metal-binding Nucleotide-binding Periplasm Reference proteome Signal Zinc P T MKLLQRGVALALLTTFTLASETALAYEQDKTYKITVLHTNDHHGHFWRNEYGEYGLAAQK TLVDGIRKEVAAEGGSVLLLSGGDINTGVPESDLQDAEPDFRGMNLVGYDAMAIGNHEFD NPLTVLRQQEKWAKFPLLSANIYQKSTGERLFKPWALFKRQDLKIAVIGLTTDDTAKIGN PEYFTDIEFRKPADEAKLVIQELQQTEKPDIIIAATHMGHYDNGEHGSNAPGDVEMARAL PAGSLAMIVGGHSQDPVCMAAENKKQVDYVPGTPCKPDQQNGIWIVQAHEWGKYVGRADF EFRNGEMKMVNYQLIPVNLKKKVTWEDGKSERVLYTPEIAENQQMISLLSPFQNKGKAQL EVKIGETNGRLEGDRDKVRFVQTNMGRLILAAQMDRTGADFAVMSGGGIRDSIEAGDISY KNVLKVQPFGNVVVYADMTGKEVIDYLTAVAQMKPDSGAYPQFANVSFVAKDGKLNDLKI KGEPVDPAKTYRMATLNFNATGGDGYPRLDNKPGYVNTGFIDAEVLKAYIQKSSPLDVSV YEPKGEVSWQ P0AG27 P37688 Q2M7S5 YIBN_ECOLI Uncharacterized protein YibN yibN b3611 JW3586 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-91 IDENTIFICATION BY MASS SPECTROMETRY K12 / JW1106 K12 / MG1655 / ATCC 47076 Acetylation Complete proteome Reference proteome MQEIMQFVGRHPILSIAWIALLVAVLVTTFKSLTSKVKVITRGEATRLINKEDAVVVDLR QRDDFRKGHIAGSINLLPSEIKANNVGELEKHKDKPVIVVDGSGMQCQEPANALTKAGFA QVFVLKEGVAGWAGENLPLVRGK P76485 Q2MAM4 YFBO_ECOLI Uncharacterized protein YfbO yfbO b2274 JW2269 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Complete proteome Reference proteome MTPLERITQLVNINGDVNNPDTPRPLLSLEDFFIDNNIHGSICCNVIPEQSPQAIYHHFL KIRERNNVSDVLVEITMFDDPDWPFSESILVITTASPEEVQSWFVEEIAPDECWEGWSED TEHGWVEVPVGMHPVTCWWD P37342 P37341 Q2M5T7 YJJI_ECOLI Uncharacterized protein YjjI yjjI yjjH b4380 JW4343 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-167 K12 PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-289 P0A6Y8 dnaK false 2 To H.influenzae HI_0521. Complete proteome Reference proteome MPTSHENALQQRCQQIVTSPVLSPEQKRHFLALEAENNLPYPQLPAEARRALDEGVICDM FEGHAPYKPRYVLPDYARFLANGSEWLELEGAKDLDDALSLLTILYHHVPSVTSMPVYLG QLDALLQPYVRILTQDEIDVRIKRFWRYLDRTLPDAFMHANIGPSDSPITRAILRADAEL KQVSPNLTFIYDPEITPDDLLLEVAKNICECSKPHIANGPVHDKIFTKGGYGIVSCYNSL PLAGGGSTLVRLNLKAIAERSESLDDFFTRTLPHYCQQQIAIIDARCEFLYQQSHFFENS FLVKEGLINPERFVPMFGMYGLAEAVNLLCEKEGIAARYGKEAAANEVGYRISAQLAEFV ANTPVKYGWQKRAMLHAQSGISSDIGTTPGARLPYGDEPDPITHLQTVAPHHAYYYSGIS DILTLDETIKRNPQALVQLCLGAFKAGMREFTANVSGNDLVRVTGYMVRLSDLEKYRAEG SRTNTTWLGEEAARNTRILERQPRVISHEQQMRFSQ P0AF36 P32164 Q2M8M4 ZAPB_ECOLI Cell division protein ZapB zapB yiiU b3928 JW3899 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-10 IDENTIFICATION BY MASS SPECTROMETRY K12 / JW1106 K12 / MG1655 / ATCC 47076 FUNCTION IN CELL DIVISION COILED-COIL DOMAIN SUBUNIT INTERACTION WITH FTSZ SUBCELLULAR LOCATION K12 / MG1655 / ATCC 47076 Non-essential, abundant cell division factor that is required for proper Z-ring formation. It is recruited early to the divisome by direct interaction with FtsZ, stimulating Z-ring assembly and thereby promoting cell division earlier in the cell cycle. Its recruitment to the Z-ring requires functional FtsA or ZipA. Homodimer. The ends of the coiled-coil dimer bind to each other, forming polymers. Interacts with FtsZ. P0ADS2 zapA false 4 Cytoplasm Localizes to the septum at mid-cell, in a FtsZ-like pattern. Belongs to the ZapB family. 3D-structure Acetylation Cell cycle Cell division Coiled coil Complete proteome Cytoplasm Reference proteome Septation MTMSLEVFEKLEAKVQQAIDTITLLQMEIEELKEKNNSLSQEVQNAQHQREELERENNHL KEQQNGWQERLQALLGRMEEV P0C8K0 P42903 Q2M977 KBAZ_ECOLI D-tagatose-1,6-bisphosphate aldolase subunit KbaZ kbaZ agaZ yhaX b3132 JW3101 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 DISCUSSION OF SEQUENCE FUNCTION AS A TAGBP ALDOLASE COMPONENT COMPLEX WITH KBAY Component of the tagatose-1,6-bisphosphate aldolase KbaYZ that is required for full activity and stability of the Y subunit. Could have a chaperone-like function for the proper and stable folding of KbaY. When expressed alone, KbaZ does not show any aldolase activity. Carbohydrate metabolism; D-tagatose 6-phosphate degradation; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-tagatose 6-phosphate: step 2/2. Forms a complex with KbaY. In contrast to E.coli strains C and EC3132, K-12 strains cannot grow on N-acetylgalactosamine and D-galactosamine, because they carry a deletion and thus lack active PTS systems specific for these compounds. Therefore, KbaYZ in K-12 strains is not involved in the degradation of these compounds. Belongs to the GatZ/KbaZ family. KbaZ subfamily. Was originally thought to be a tagatose 6-phosphate kinase. Complete proteome Reference proteome MKHLTEMVRQHKAGKTNGIYAVCSAHPLVLEAAIRYASANQTPLLIEATSNQVDQFGGYT GMTPADFRGFVCQLADSLNFPQDALILGGDHLGPNRWQNLPAAQAMANADDLIKSYVAAG FKKIHLDCSMSCQDDPIPLTDDIVAERAARLAKVAEETCLEHFGEADLEYVIGTEVPVPG GAHETLSELAVTTPDAARATLEAHRHAFEKQGLNAIWPRIIALVVQPGVEFDHTNVIDYQ PAKASALSQMVENYETLIFEAHSTDYQTPQSLRQLVIDHFAILKVGPALTFALREALFSL AAIEEELVPAKACSGLRQVLEDVMLDRPEYWQSHYHGDGNARRLARGYSYSDRVRYYWPD SQIDDAFAHLVRNLADSPIPLPLISQYLPLQYVKVRSGELQPTPRELIINHIQDILAQYH TACEGQ P09833 MODC_ECOLI Molybdenum import ATP-binding protein ModC 7.3.2.5 modC chlD narD b0765 JW0748 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 / MC1000 / ATCC 39531 NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Part of the ABC transporter complex ModABC involved in molybdenum import. Responsible for energy coupling to the transport system. ATP + H2O + molybdate(out) = ADP + H(+) + molybdate(in) + phosphate The complex is composed of two ATP-binding proteins (ModC), two transmembrane proteins (ModB) and a solute-binding protein (ModA). Cell inner membrane Peripheral membrane protein Belongs to the ABC transporter superfamily. Molybdate importer (TC 3.A.1.8) family. ATP-binding Cell inner membrane Cell membrane Complete proteome Membrane Molybdenum Nucleotide-binding Reference proteome Translocase Transport PHYAMTA SALRDDR AALRIRIQASDVSLVLQPPQQTSIRNVLRAKVVNSYDDNGQVEVELEVGGKTLWARISPWARDELAIKPGLWLYAQIKSVSITA LRYYPHSGFRCFSWFYNRRSKPAFVTIAGKSC MLELNFSQTLGNHCLTINETLPANGITAIFGVSGAGKTSLINAISGLTRPQKGRIVLNGR VLNDAEKGICLTPEKRRVGYVFQDARLFPHYKVRGNLRYGMSKSMVDQFDKLVALLGIEP LLDRLPGSLSGGEKQRVAIGRALLTAPELLLLDEPLASLDIPRKRELLPYLQRLTREINI PMLYVSHSLDEILHLADRVMVLENGQVKAFGALEEVWGSSVMNPWLPKEQQSSILKVTVL EHHPHYAMTALALGDQHLWVNKLDEPLQAALRIRIQASDVSLVLQPPQQTSIRNVLRAKV VNSYDDNGQVEVELEVGGKTLWARISPWARDELAIKPGLWLYAQIKSVSITA P0C079 P07007 RELB_ECOLI Antitoxin RelB relB b1564 JW1556 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] OPERON MUTAGENESIS OF ALA-39 AND PRO-45 K12 / CS520 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION AS AN ANTITOXIN FUNCTION AS A TRANSCRIPTIONAL REPRESSOR INDUCTION FUNCTION SUBUNIT DNA-BINDING FUNCTION CLEAVAGE BY LON PROTEASE INDUCTION DISRUPTION PHENOTYPE FUNCTION AS AN ANTITOXIN K12 FUNCTION INDUCTION DOMAIN DNA-BINDING K12 FUNCTION SUBUNIT INDUCTION CLEAVAGE BY LON PROTEASE DNA-BINDING MUTAGENESIS OF ARG-7; ILE-8; LYS-13 AND SER-28 K12 DISRUPTION PHENOTYPE K12 / MC4100 / ATCC 35695 / DSM 6574 FUNCTION IN CELL DEATH DISRUPTION PHENOTYPE K12 / MC4100 / ATCC 35695 / DSM 6574 FUNCTION K12 / MG1655 / ATCC 47076 INDUCTION BY OTHER TA SYSTEMS K12 / BW25113 STRUCTURE BY NMR OF 1-50 FUNCTION DNA-BINDING SUBUNIT INDUCTION DOMAINS MUTAGENESIS OF ARG-7; 66-LEU--LEU-79 AND 71-PRO--LEU-79 STRUCTURE BY NMR OF 47-79 IN COMPLEX WITH RELE SUBUNIT X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) IN COMPLEX WITH RELB FUNCTION SUBUNIT INDUCTION Antitoxin component of a type II toxin-antitoxin (TA) system. Counteracts the effect of cognate toxin RelE via direct protein-protein interaction, preventing RelE from entering the ribosome A site and thus inhibiting its endoribonuclease activity. An autorepressor of relBE operon transcription. 2 RelB dimers bind to 2 operator sequences; DNA-binding and repression is stronger when complexed with toxin/corepressor RelE by conditional cooperativity (PubMed:18501926, PubMed:22981948). Increased transcription rate of relBE and activation of relE is consistent with a lower level of RelB in starved cells due to degradation of RelB by protease Lon. Seems to be a principal mediator of cell death in liquid media. Homotetramer formed by dimerization of dimers in solution (PubMed:19747491, PubMed:18501926). Forms an RelB(2)-RelE(2) heterotetramer (PubMed:18501926, PubMed:22981948). Also forms an RelB(2)-RelE heterotrimer (PubMed:18532983, PubMed:19747491). The RelB(2)-RelE complex is probably the one that binds DNA and represses transcription, possibly as 2 heterotrimers, 1 bound to each of 2 operators (PubMed:22981948, PubMed:19747491). P0C077 relE false 3 By amino acid starvation, by glucose starvation and by chloramphenicol; induction is independent of ppGpp. Autorepressed by RelB, RelE acts as a corepressor (PubMed:9767574, PubMed:19747491, PubMed:18501926, PubMed:22981948). Member of the relBEF operon (PubMed:2990907). Operon induced by ectopic expression of toxins HicA, HipA, MazF, MqsR and RelE, but not by YafQ (PubMed:23432955). Dimerizes and binds DNA via its N-terminus (residues 1-50), binds toxin RelE via the C-terminus (residues 47-79) (PubMed:18501926, PubMed:18532983). Tetramerization probably requires amino acids between residues 66 and 71 (PubMed:18501926). Probably degraded by Lon protease during amino acid starvation (PubMed:11717402). Degraded in vitro by Lon (PubMed:19747491). Essential, it cannot be deleted if a copy of relE remains in the cell. Cells missing relBE have a higher steady-state level of translation during amino acid starvation than wild-type cells. They survive antibiotic treatment in log phase better than wild-type cells. Cells missing mazE-mazF survive hydroxyurea treatment better than wild-type; further disruption of relE-relB and tonB yields even better survival (PubMed:20005847). A number of site directed mutants give rise to a delayed relaxed phenotype; RNA synthesis resumes 10 minutes after amino acid starvation, an unusually slow recovery from periods of starvation, accumulation of a translation inhibitor. There are estimated to be 550-1100 RelB and 50-100 RelE molecules in rapidly growing cells of MG1655; as they have quite high affinity for each other (dissociation constant of 0.33 nM) there is probably less than 1 free RelE molecule per cell. The RelB(2)-RelE complex has a half-life of over 70 minutes. Belongs to the RelB/DinJ antitoxin family. 3D-structure Complete proteome DNA-binding Reference proteome Repressor Stress response Toxin-antitoxin system Transcription Transcription regulation R A I A K A S L R A T P L P T MGSINLRIDDELKARSYAALEKMGVTPSEALRLMLEYIADNERLPFKQTLLSDEDAELVE IVKERLRNPKPVRVTLDEL P76422 THID_ECOLI Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase 2.7.1.49 2.7.4.7 Hydroxymethylpyrimidine kinase HMP kinase Hydroxymethylpyrimidine phosphate kinase HMP-P kinase HMP-phosphate kinase HMPP kinase thiD thiJ b2103 JW2090 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] PROTEIN SEQUENCE OF 1-10 FUNCTION CATALYTIC ACTIVITY SUBUNIT K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P. Shows no activity with pyridoxal, pyridoxamine or pyridoxine. 4-amino-5-hydroxymethyl-2-methylpyrimidine + ATP = 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + ADP + H(+) 4-amino-2-methyl-5-(phosphooxymethyl)pyrimidine + ATP = 4-amino-2-methyl-5-(diphosphooxymethyl)pyrimidine + ADP Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-ribosyl)imidazole: step 2/3. Cofactor biosynthesis; thiamine diphosphate biosynthesis; 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5-phospho-D-ribosyl)imidazole: step 3/3. Monomer. Belongs to the ThiD family. ATP-binding Complete proteome Direct protein sequencing Kinase Nucleotide-binding Reference proteome Thiamine biosynthesis Transferase MKRINALTIAGTDPSGGAGIQADLKTFSALGAYGCSVITALVAQNTRGVQSVYRIEPDFV AAQLDSVFSDVRIDTTKIGMLAETDIVEAVAERLQRYQIQNVVLDTVMLAKSGDPLLSPS AVATLRSRLLPQVSLITPNLPEAAALLDAPHARTEQEMLEQGRSLLAMGCGAVLMKGGHL DDEQSPDWLFTREGEQRFTAPRIMTKNTHGTGCTLSAALAALRPRHTNWADTVQEAKSWL SSALAQADTLEVGHGIGPVHHFHAWW P75676 P71286 Q9R2D9 YAFX_ECOLI Uncharacterized protein YafX yafX b0248 JW5022 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Belongs to the antirestriction protein family. Complete proteome Reference proteome MTTQTQHDLAPANQPEFELTVTPVPDEQRIDFWPQYFGAIPQWLLLEPHIFAWMDRFCEG YSGGIWSFYTLSNGGAFMSPEPDNDETWRLFNCLNGNDAQMSAEAAGIAVCLIAYSHHAC RTECDAMTAHYYRLREYAMQHPEAHAILRIID P75788 Q9R7R9 YBIR_ECOLI Inner membrane protein YbiR ybiR b0818 JW0802 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 TOPOLOGY [LARGE SCALE ANALYSIS] K12 / MG1655 / ATCC 47076 Cell inner membrane Multi-pass membrane protein Belongs to the CitM (TC 2.A.11) transporter family. Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix Transport MSLPFLRTLQGDRFFQLLILVGIGLSFFVPFAPKSWPAAIDWHTIITLSGLMLLTKGVEL SGYFDVLGRKMVRRFATERRLAMFMVLAAALLSTFLTNDVALFIVVPLTITLKRLCEIPV NRLIIFEALAVNAGSLLTPIGNPQNILIWGRSGLSFAGFIAQMAPLAGAMMLTLLLLCWC CFPGKAMQYHTGVQTPEWKPRLVWSCLGLYIVFLTALEFKQELWGLVIVAAGFALLARRV VLSVDWTLLLVFMAMFIDVHLLTQLPALQGVLGNVSHLSEPGLWLTAIGLSQVISNVPST ILLLNYVPPSLLLVWAVNVGGFGLLPGSLANLIALRMANDRRIWWRFHLYSIPMLLWAAL VGYVLLVILPAN P39901 YBFI_ECOLI Putative uncharacterized protein YbfI ybfI b4636 b0691.1 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-46 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 46-65 K12 IDENTIFICATION CONCEPTUAL TRANSLATION Could be the product of a pseudogene. Translated as Xaa. Translated as Xaa. Complete proteome DNA-binding Reference proteome Transcription Transcription regulation MIALSVCWQIVRYLCRIRQMXGLNAIEHSNYLRNYMGHLRQKLEQDPARPRHFITETGIG YRFML Q47268 A5A606 YLCH_ECOLI Uncharacterized protein YlcH ylcH b4588 b0546.1 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 Encoded by the cryptic lambdoid prophage DLP12. To equivalent protein in phage 82. Complete proteome Reference proteome MRTYNPNSLLPSQMQKCTCNSLHLAFDLCGGEA P77219 Q2MCA6 YAHC_ECOLI Uncharacterized protein YahC yahC b0317 JW0309 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Cell membrane Multi-pass membrane protein To E.coli YcdZ. Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MNGLTATGVTVGICAGLWQLVSSHVGLSQGWELLGTIGFVAFCSFYAAGGGKSGFIRSLA VNYSGMVWAFFAALTAGWLASVSGLSAFWASVITTVPFSAVVVWQGRFWLLSFIPGGFLG MTLFFASGMNWTVTLLGFLAGNCVGVISEYGGQKLSEATTKRDGY P37018 P75661 YADM_ECOLI Uncharacterized fimbrial-like protein YadM yadM b0138 JW0134 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION INDUCTION DISRUPTION PHENOTYPE K12 / MG1655 / ATCC 47076 Part of the yadCKLM-htrE-yadVN fimbrial operon. Could contribute to adhesion to various surfaces in specific environmental niches. Fimbrium Repressed by H-NS. Deletion of the operon under classical laboratory conditions does not result in any major effect on E.coli capacity to form biofilms compared with the wild-type strain. The operon is cryptic under classical laboratory conditions, but is functional when constitutively expressed. Belongs to the fimbrial protein family. Complete proteome Fimbrium Reference proteome Signal MIKTTPHKIVILMGILLSPSVFATDINVEFTATVKATTCNITLTGNNVTNDGNNNYTLRI PKMGLDKIANKTTESQADFKLVASGCSSGISWIDTTLTGNASSSSPKLIIPQSGDSSSTT SNIGMGFKKRTTDDATFLKPNSAEKIRWSTDEMQPDKGLEMTVALRETDAGQGVPGNFRA LATFNFIYQ P39263 P76493 P77678 YFCC_ECOLI Putative basic amino acid antiporter YfcC yfcC b2298 JW2295 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-90 K12 / KH131 IDENTIFICATION FUNCTION K12 / MC4100 / ATCC 35695 / DSM 6574 Metabolomic profiling of different yfcC over-expression and deletion strains suggests that it may affect the glyoxylate shunt. Cell inner membrane Multi-pass membrane protein To H.influenzae HI_0594. To B.subtilis YcgA. Antiport Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix Transport MSAITESKPTRRWAMPDTLVIIFFVAILTSLATW MLFNQPCHL GDERP AMNAR MSAITESKPTRRWAMPDTLVIIFFVAILTSLATWVVPVGMFDSQEVQYQVDGQTKTRKVV DPHSFRILTNEAGEPEYHRVQLFTTGDERPGLMNFPFEGLTSGSKYGTAVGIIMFMLVIG GAFGIVMRTGTIDNGILALIRHTRGNEILFIPALFILFSLGGAVFGMGEEAVAFAIIIAP LMVRLGYDSITTVLVTYIATQIGFASSWMNPFCVVVAQGIAGVPVLSGSGLRIVVWVIAT LIGLIFTMVYASRVKKNPLLSRVHESDRFFREKQADVEQRPFTFGDWLVLIVLTAVMVWV IWGVIVNAWFIPEIASQFFTMGLVIGIIGVVFRLNGMTVNTMASSFTEGARMMIAPALLV GFAKGILLLVGNGEAGDASVLNTILNSIANAISGLDNAVAAWFMLLFQAVFNFFVTSGSG QAALTMPLLAPLGDLVGVNRQVTVLAFQFGDGFSHIIYPTSASLMATLGVCRVDFRNWLK VGATLLGLLFIMSSVVVIGAQLMGYH P0A7T3 P02372 P77006 RS16_ECOLI 30S ribosomal protein S16 Small ribosomal subunit protein bS16 rpsP b2609 JW2590 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia PROTEIN SEQUENCE SUBUNIT K NUCLEOTIDE SEQUENCE [GENOMIC DNA] OPERON STRUCTURE K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] SEQUENCE REVISION K12 / W3110 / ATCC 27325 / DSM 5911 PROTEIN SEQUENCE OF 1-15 FUNCTION AS AN ENDONUCLEASE PROTEIN SEQUENCE OF 1-12 K12 / EMG2 IDENTIFICATION BY 2D-GEL FUSION WITH RIBOSOME MATURATION FACTOR RIMM MW100 MASS SPECTROMETRY SUBUNIT K12 / ATCC 25404 / DSM 5698 / NCIMB 11290 NOMENCLATURE 3D-STRUCTURE MODELING SUBUNIT STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS) SUBUNIT MRE-600 X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES SUBUNIT MRE-600 STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) OF 70S RIBOSOME IN COMPLEX WITH ARFA AND RF2 SUBUNIT STRUCTURE BY ELECTRON MICROSCOPY (3.1 ANGSTROMS) OF 70S RIBOSOME IN COMPLEX WITH ARFA AND RF2 SUBUNIT STRUCTURE BY ELECTRON MICROSCOPY (2.97 ANGSTROMS) OF 70S RIBOSOME IN COMPLEX WITH ARFA AND RF2 SUBUNIT STRUCTURE BY ELECTRON MICROSCOPY (3.52 ANGSTROMS) OF 70S RIBOSOME IN COMPLEX WITH ARFA AND RF2 SUBUNIT In addition to being a ribosomal protein, S16 also has a cation-dependent endonuclease activity. In-frame fusions with the ribosome maturation factor rimM suppress mutations in the latter (probably due to increased rimM expression) and are found in translationally active 70S ribosomes. Part of the 30S ribosomal subunit (PubMed:336510, PubMed:10094780, PubMed:12244297, PubMed:12809609, PubMed:16272117, PubMed:27934701, PubMed:27906160, PubMed:27906161). Part of the rpsP-rimM-trmD-rplS operon. Belongs to the bacterial ribosomal protein bS16 family. 3D-structure Complete proteome Direct protein sequencing Endonuclease Hydrolase Nuclease Reference proteome Ribonucleoprotein Ribosomal protein MVTIRLARHGAKKRPFYQVVVADSRNARNGRFIERVGFFNPIASEKEEGTRLDLDRIAHW VGQGATISDRVAALIKEVNKAA P0A867 P78258 P80218 TALA_ECOLI Transaldolase A 2.2.1.2 talA b2464 JW2448 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 PRESENCE OF TWO TRANSALDOLASES IN E.COLI Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = beta-D-fructose 6-phosphate + D-erythrose 4-phosphate Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3. Homodimer. Cytoplasm Belongs to the transaldolase family. Type 1 subfamily. Complete proteome Cytoplasm Pentose shunt Reference proteome Schiff base Transferase MNELDGIKQFTTVVADSGDIESIRHYHPQDATTNPSLLLKAAGLSQYEHLIDDAIAWGKK NGKTQEQQVVAACDKLAVNFGAEILKIVPGRVSTEVDARLSFDKEKSIEKARHLVDLYQQ QGVEKSRILIKLASTWEGIRAAEELEKEGINCNLTLLFSFAQARACAEAGVFLISPFVGR IYDWYQARKPMDPYVVEEDPGVKSVRNIYDYYKQHHYETIVMGASFRRTEQILALTGCDR LTIAPNLLKELQEKVSPVVRKLIPPSQTFPRPAPMSEAEFRWEHNQDAMAVEKLSEGIRL FAVDQRKLEDLLAAKL Q46824 Q2M9U5 YGFX_ECOLI Inner membrane protein YgfX Toxin CptA ygfX cptA b2896 JW2864 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 PRELIMINARY (INCORRECT) FUNCTION AS A TOXIN SUBCELLULAR LOCATION INTERACTION WITH FTSZ AND MREB B / BL21-DE3 K12 / BW25113 FUNCTION K12 / BW25113 NOT A TOXIN-ANTITOXIN SYSTEM FUNCTION K12 / BW25113 A probable inner membrane protein. Has been shown not to be a toxin, no effects on growth are seen in LB or minimal medium up to 6 or 21 hours (respectively) after induction of expression (PubMed:23657679). Interacts with cytoskeletal proteins FtsZ and MreB; inhibits FtsZ GTP-dependent polymerization as well as MreB ATP-dependent polymerization (PubMed:22239607). Restores production of prodigiosin antibiotic (Pig) in Serratia strains with deletions of sdhE-ygfX; overexpression of this protein and CptB also restores Pig production to a slightly lesser extent in Serratia (PubMed:22474332). Interacts with MreB and FtsZ; interaction with the latter requires FtsZ residues 33-49 (PubMed:22239607). Cell inner membrane Multi-pass membrane protein Was originally thought to be the toxic component of a type II toxin-antitoxin (TA) system; overexpression was shown to lead to growth arrest after 5 hours, with initial elongation of cells, followed by swelling (PubMed:22239607). The toxic effects were abrogated by coexpression with antitoxin CptB (now sdhE) (PubMed:22239607). However subsequent studies have been unable to show the toxic effect upon overexpression, nor is the Serratia ortholog a toxin (PubMed:23657679). Cell inner membrane Cell membrane Cell shape Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MVLWQSDLRVSWRAQWLSLLIHGLVAAVILLMPWPLSYTPLWMVLLSLVVFDCVRSQRRI NARQGEIRLLMDGRLRWQGQEWSIVKAPWMIKSGMMLRLRSDGGKRQHLWLAADSMDEAE WRDLRRILLQQETQR P0A9M5 P00501 XGPT_ECOLI Xanthine phosphoribosyltransferase 2.4.2.22 Xanthine-guanine phosphoribosyltransferase XGPRT gpt gpp gxu b0238 JW0228 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-49 PROTEIN SEQUENCE OF 66-76 X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANT ALA-59 IN COMPLEX WITH MAGNESIUM MASS SPECTROMETRY COFACTOR FUNCTION BIOPHYSICOCHEMICAL PROPERTIES SUBUNIT BIOPHYSICOCHEMICAL PROPERTIES ACTIVITY REGULATION MUTAGENESIS OF CYS-59 CRYSTALLIZATION OF WILD-TYPE AND OF MUTANT ALA-59 X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF MUTANT ALA-59 IN COMPLEXES WITH GUANINE; XANTHINE; 5-PHOSPHO-ALPHA-D-RIBOSE-1-DIPHOSPHATE AND MAGNESIUM SUBUNIT Acts on guanine, xanthine and to a lesser extent hypoxanthine. diphosphate + XMP = 5-phospho-alpha-D-ribose 1-diphosphate + xanthine Mg(2+) Binds 1 Mg(2+) ion per subunit. Inhibited by thioguanine, GMP and, to a lesser extent, by thioxanthine, azaxanthine and azaguanine. 4.3 uM for guanine 30.5 uM for xanthine 90.8 uM for hypoxanthine Purine metabolism; XMP biosynthesis via salvage pathway; XMP from xanthine: step 1/1. Homotetramer. Cell inner membrane Peripheral membrane protein The measured mass is that of mutant Ala-59. Belongs to the purine/pyrimidine phosphoribosyltransferase family. XGPT subfamily. 3D-structure Cell inner membrane Cell membrane Complete proteome Direct protein sequencing Glycosyltransferase Magnesium Membrane Metal-binding Purine salvage Reference proteome Transferase C A V G MSEKYIVTWDMLQIHARKLASRLMPSEQWKGIIAVSRGGLVPGALLARELGIRHVDTVCI SSYDHDNQRELKVLKRAEGDGEGFIVIDDLVDTGGTAVAIREMYPKAHFVTIFAKPAGRP LVDDYVVDIPQDTWIEQPWDMGVVFVPPISGR P0AD12 P76370 Q2MAY8 YEEZ_ECOLI Protein YeeZ yeeZ b2016 JW1998 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 IDENTIFICATION BY MASS SPECTROMETRY B / BL21 ATP-binding Complete proteome Nucleotide-binding Reference proteome Signal MKKVAIVGLGWLGMPLAMSLSARGWQVTGSKTTQDGVEAARMSGIDSYLLRMEPELVCDS DDLDALMDADALVITLPARRSGPGDEFYLQAVQELVDSALAHRIPRIIFTSSTSVYGDAQ GTVKETTPRNPVTNSGRVLEELEDWLHNLPGTSVDILRLAGLVGPGRHPGRFFAGKTAPD GEHGVNLVHLEDVIGAITLLLQAPKGGHIYNICAPAHPARNVFYPQMARLLGLEPPQFRN SLDSGKGKIIDGSRICNELGFEYQYPDPLVMPLE P69346 P46147 P76371 YEFM_ECOLI Antitoxin YefM yefM b2017 JW5835 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 PRELIMINARY PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] IDENTIFICATION FUNCTION FUNCTION AS AN ANTITOXIN DISRUPTION PHENOTYPE K12 / MG1655 / ATCC 47076 SUBUNIT K12 / MC1061 / ATCC 53338 / DSM 7140 INDUCTION IN PERSISTER CELLS K12 FUNCTION AS A TRANSCRIPTIONAL REPRESSOR DNA-BINDING SUBUNIT INDUCTION FUNCTION AS A TRANSCRIPTIONAL REPRESSOR DNA-BINDING MUTAGENESIS OF ARG-10 AND ARG-31 INDUCTION BY VAPC K12 / MG1655 / ATCC 47076 X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH YOEB SUBUNIT K12 Antitoxin component of a type II toxin-antitoxin (TA) system. Antitoxin that counteracts the effect of the YoeB toxin. YefM binds to the promoter region of the yefM-yeoB operon to repress transcription, YeoB acts as a corepressor. In solution exists as both a monomer and a dimer; the monomeric state is more predominant. It has been described as being a YefM-YeoB(2) heterotrimer (PubMed:15980067) and as a YefM(2)-YoeB heterotrimer (PubMed:16109374 and PubMed:17170003). When complexed with YoeB inhibits the toxin activity. Represses its own promoter; more strongly repressed by the YefM(2)YoeB heterotrimer. Induced in persister cells. Ectopic expression of Salmonella or Shigella toxin VapC induces the yefM-yoeB operon and also induces Yoeb toxin activity in a Lon protease-dependent manner. No visible phenotype under standard growth conditions. Delays Lon protease-dependent lethality upon overexpression of Lon, but does not fully suppress it. Has been described as natively unfolded and proteolytically unstable in vivo (PubMed:14672926), but also as structured following overexpression in vitro (PubMed:17170003). Has a half-life of approximately 1 hour in vivo. Belongs to the phD/YefM antitoxin family. 3D-structure Complete proteome DNA-binding Reference proteome Repressor Toxin-antitoxin system Transcription Transcription regulation R A R A MRTISYSEARQNLSATMMKAVEDHAPILITRQNGEACVLMSLEEYNSLEETAYLLRSPAN ARRLMDSIDSLKSGKGTEKDIIE P0AB26 P09995 YCEB_ECOLI Uncharacterized lipoprotein YceB yceB b1063 JW1050 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Cell membrane Lipid-anchor 3D-structure Cell membrane Complete proteome Lipoprotein Membrane Palmitate Reference proteome Signal MNKFLFAAALIVSGLLVGCNQLTQYTITEQEINQSLAKHNNFSKDIGLPGVADAHIVLTN LTSQIGREEPNKVTLTGDANLDMNSLFGSQKATMKLKLKALPVFDKEKGAIFLKEMEVVD ATVQPEKMQTVMQTLLPYLNQALRNYFNQQPAYVLREDGSQGEAMAKKLAKGIEVKPGEI VIPFTD Q46821 Q2M9V3 UACT_ECOLI Uric acid transporter UacT uacT ygfU b2888 JW5470 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 TOPOLOGY [LARGE SCALE ANALYSIS] K12 / MG1655 / ATCC 47076 FUNCTION ACTIVITY REGULATION BIOPHYSICOCHEMICAL PROPERTIES SUBCELLULAR LOCATION GENE NAME MUTAGENESIS OF HIS-37; THR-100; SER-256; THR-259; GLU-270; LEU-278; ASP-298; SER-317; GLN-318; ASN-319; VAL-320; ARG-327 AND SER-426 K12 Proton-dependent high-capacity transporter for uric acid. Shows also a low capacity for transport of xanthine at 37 degrees Celsius but not at 25 degrees Celsius. Inhibited in the presence of the protonophore carbonyl cyanide m-chlorophenyl hydrazone. 0.5 mM for uric acid 0.3 mM for xanthine 715 nmol/min/mg enzyme with acid uric as substrate 14 nmol/min/mg enzyme with xanthine as substrate (at 37 degrees Celsius) Cell inner membrane Multi-pass membrane protein Belongs to the xanthine/uracil permease family. Nucleobase:cation symporter-2 (NCS2) (TC 2.A.40) subfamily. Translation N-terminally shortened. Cell inner membrane Cell membrane Complete proteome Hydrogen ion transport Ion transport Membrane Reference proteome Symport Transmembrane Transmembrane helix Transport H K L H N T A T S S Q T V E D N Q L T D E D N S A Q E N N D Q V N R G S N MSAIDSQLPSSSGQDRPTDEVDRILSPGKLIILGLQHVLVMYAGAVAVPLMIGDRLGLSK EAIAMLISSDLFCCGIVTLLQCIGIGRFMGIRLPVIMSVTFAAVTPMIAIGMNPDIGLLG IFGATIAAGFITTLLAPLIGRLMPLFPPLVTGVVITSIGLSIIQVGIDWAAGGKGNPQYG NPVYLGISFAVLIFILLITRYAKGFMSNVAVLLGIVFGFLLSWMMNEVNLSGLHDASWFA IVTPMSFGMPIFDPVSILTMTAVLIIVFIESMGMFLALGEIVGRKLSSHDIIRGLRVDGV GTMIGGTFNSFPHTSFSQNVGLVSVTRVHSRWVCISSGIILILFGMVPKMAVLVASIPQF VLGGAGLVMFGMVLATGIRILSRCNYTTNRYNLYIVAISLGVGMTPTLSHDFFSKLPAVL QPLLHSGIMLATLSAVVLNVFFNGYQHHADLVKESVSDKDLKVRTVRMWLLMRKLKKNEH GE P32703 Q2M6N9 YJCE_ECOLI Uncharacterized Na(+)/H(+) exchanger YjcE yjcE b4065 JW4026 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Cell inner membrane Multi-pass membrane protein Belongs to the monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family. Antiport Cell inner membrane Cell membrane Complete proteome Ion transport Membrane Reference proteome Sodium Sodium transport Transmembrane Transmembrane helix Transport MEIFFTILIMTLVVSLSGVVTRVMPFQIPLPLMQIAIGALLAWPTFGLHVEFDPELFLVL FIPPLLFADGWKTPTREFLEHGREIFGLALALVVVTVVGIGFLIYWVVPGIPLIPAFALA AVLSPTDAVALSGIVGEGRIPKKIMGILQGEALMNDASGLVSLKFAVAVAMGTMIFTVGG ATVEFMKVAIGGILAGFVVSWLYGRSLRFLSRWGGDEPATQIVLLFLLPFASYLIAEHIG VSGILAAVAAGMTITRSGVMRRAPLAMRLRANSTWAMLEFVFNGMVFLLLGLQLPGILET SLMAAEIDPNVEIWMLFTNIILIYAALMLVRFGWLWTMKKFSNRFLKKKPMEFGSWTTRE ILIASFAGVRGAITLAGVLSIPLLLPDGNVFPARYELVFLAAGVILFSLFVGVVMLPILL QHIEVADHSQQLKEERIARAATAEVAIVAIQKMEERLAADTEENIDNQLLTEVSSRVIGN LRRRADGRNDVESSVQEENLERRFRLAALRSERAELYHLRATREISNETLQKLLHDLDLL EALLIEENQ P31470 Q2M836 Q6BF12 YIEK_ECOLI Uncharacterized protein YieK yieK b3718 JW5613 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] SEQUENCE REVISION TO N-TERMINUS K12 / MG1655 / ATCC 47076 SEQUENCE REVISION NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Belongs to the glucosamine/galactosamine-6-phosphate isomerase family. Complete proteome Reference proteome AAAELALG VPQN MKLIITEDYQEMSRVAAHHLLGYMSKTRRVNLAITAGSTPKGMYEYLTTLVKGKPWYDNC YFYNFDEIPFRGKEGEGVTITNLRNLFFTPAGIKEENIQKLTIDNYREHDQKLAREGGLD LVVLGLGADGHFCGNLPNTTHFHEQTVEFPIQGEMVDIVAHGELGGDFSLVPDSYVTMGP KSIMAAKNLLIIVSGAGKAQALKNVLQGPVTEDVPASVLQLHPSLMVIADKAAAAELALG P46852 Q2M7A2 YHHW_ECOLI Quercetin 2,3-dioxygenase Quercetinase 1.13.11.24 Pirin-like protein YhhW yhhW b3439 JW3402 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 IDENTIFICATION BY MASS SPECTROMETRY B / BL21 X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) IN COMPLEX WITH CADMIUM IONS FUNCTION CATALYTIC ACTIVITY COFACTOR ACTIVITY REGULATION DOMAIN METAL-BINDING K12 Has quercetin 2,3-dioxygenase activity in vitro. Its physiological role is unknown; however, may provide a mechanism that would avoid inhibition of key cellular proteins, such as DNA gyrase, by quercetin. O2 + quercetin = 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO Zn(2+) Co(2+) Fe(2+) Binds 1 divalent metal cation, Zn(2+), Co(2+) or Fe(2+). Inhibited by kojic acid, sodium diethyldithiocarbamate and 1,10-phenanthroline monohydrochloride. Flavonoid metabolism; quercetin degradation. Is composed of two structurally similar domains arranged face to face. Quercetin is a flavonoid compound synthesized by a variety of plants, including foods for human consumption. Belongs to the pirin family. 3D-structure Complete proteome Copper Dioxygenase Iron Metal-binding Oxidoreductase Reference proteome Zinc MIYLRKANERGHANHGWLDSWHTFSFANYYDPNFMGFSALRVINDDVIEAGQGFGTHPHK DMEILTYVLEGTVEHQDSMGNKEQVPAGEFQIMSAGTGIRHSEYNPSSTERLHLYQIWIM PEENGITPRYEQRRFDAVQGKQLVLSPDARDGSLKVHQDMELYRWALLKDEQSVHQIAAE RRVWIQVVKGNVTINGVKASTSDGLAIWDEQAISIHADSDSEVLLFDLPPV P76116 Q2MBB1 YNCE_ECOLI Uncharacterized protein YncE yncE b1452 JW1447 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 INDUCTION IDENTIFICATION BY MASS SPECTROMETRY SUBSTRATE FOR SECB K12 / MC4100 PRELIMINARY CRYSTALLIZATION SUBUNIT Monomer. Repressed by Fur. Preliminary crystallization indicates the presence of a single beta-propeller domain that contains 7 4-stranded beta-sheets. 3D-structure Complete proteome Reference proteome Signal MHLRHLFSSRLRGSLLLGSLLVVSSFSTQAAEEMLRKAVGKGAYEMAYSQQENALWLATS QSRKLDKGGVVYRLDPVTLEVTQAIHNDLKPFGATINNTTQTLWFGNTVNSAVTAIDAKT GEVKGRLVLDDRKRTEEVRPLQPRELVADDATNTVYISGIGKESVIWVVDGGNIKLKTAI QNTGKMSTGLALDSEGKRLYTTNADGELITIDTADNKILSRKKLLDDGKEHFFINISLDT ARQRAFITDSKAAEVLVVDTRNGNILAKVAAPESLAVLFNPARNEAYVTHRQAGKVSVID AKSYKVVKTFDTPTHPNSLALSADGKTLYVSVKQKSTKQQEATQPDDVIRIAL Q2EES3 A0A385XJJ5 Q2MAY9 YOEF_ECOLI Protein YoeF yoeF b4538 JW5328 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Encoded by the CP4-44 prophage. Complete proteome Reference proteome MAGVRQHGWRAIPAVCSEYGADTLPDRYRSDGRCLLFWQQAGISALKQELEVKTPYRAMN HPVIGVVTKADLASMEQISLVKSWLREAGAHNVLVTSAVNNNGVTELFALLHTEEGCC P33634 P76592 P76998 YFIE_ECOLI Uncharacterized HTH-type transcriptional regulator YfiE yfiE b2577 JW2561 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-208 K12 / W3110 / ATCC 27325 / DSM 5911 Belongs to the LysR transcriptional regulatory family. Complete proteome DNA-binding Reference proteome Transcription Transcription regulation RITVENTIELISIESIKRCVAANIGVSYLPRFAVAKELECGELIELPFGEQSQTITAMCAHHAGKAVSPAMHTFIQCVEESFVAG DHGGKHH MDLRRFITLKTVVEEGSFLRASQKLCCTQSTVTFHIQQLEQEFSVQLFEKIGRRMCLTRE GKKLLPHIYELTRVMDTLREAAKKESDPDGELRVVSGETLLSYRMPQVLQRFRQRAPKVR LSLQSLNCYVIRDALLNDEADVGVFYRVGNDDALNRRELGEQSLVLVASPQIADVDFTEP GRHNACSFIINEPQCVFRQIFESTLRQRRITVENTIELISIESIKRCVAANIGVSYLPRF AVAKELECGELIELPFGEQSQTITAMCAHHAGKAVSPAMHTFIQCVEESFVAG P0DSG4 YQHJ_ECOLI Protein YqhJ yqhJ b4786 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 IDENTIFICATION INDUCTION K12 / MG1655 / ATCC 47076 Expressed equally in exponential and stationary phase in rich medium (at protein level). A shorter isoform that starts downstream at a TTG codon (yielding a 13 residue peptide) may also be expressed. Encoded antisense to yghE; it is entirely within the yghE coding region. Complete proteome Reference proteome MKYLAFLIKGKTTHFDVGK P0DSH8 YTGA_ECOLI Protein YtgA ytgA b4800 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 IDENTIFICATION INDUCTION K12 / MG1655 / ATCC 47076 Expressed equally in exponential and stationary phase in rich medium (at protein level). Complete proteome Reference proteome MSIIILATISTTQENK P78271 YFES_ECOLI Uncharacterized protein YfeS yfeS b2420 JW2413 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Complete proteome Reference proteome MKKRFIYHDEKSNKFWWIDYEGDSLAVNYGKVGSIGKFQTKEFDNEEQCLKEASKLIAAK MKKGYQEDPKFNFMDRYYFDDEEIGLHVKTSHPNFQCHFTDPLYMCCWDEESPFGSDEGA DALNVLENSLRKEPDLDCADFPQMLIETMWGMKYIAMDSILEEDVRAQLLVDEMSTIQSN MITYATAFGQIKVMGKISHKLKKMGLNALARHQLTAKILQWGDGQDSPILQKMIDDLTAF PHEN P52134 Q2MAD6 YPJK_ECOLI Uncharacterized protein YpjK ypjK b2635 JW5888 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 To E.coli YkfL. Translation N-terminally extended. Complete proteome Reference proteome Signal MPVIAIIAIVIIVIILNKTGVSDSLTALTLATVAALLTGGGAAGAASVALTPFVGVPVGI FVGIYVFAKVVRLISGKK P77206 Q47686 Q9R2D7 YAFZ_ECOLI UPF0380 protein YafZ yafZ b0252 JW0242 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Belongs to the UPF0380 family. Translation N-terminally shortened. Complete proteome Reference proteome MTRLASRFGAANLIRRDRPLTREELFRVVPSVFSEDKHESRSERYTYIPTISLLDSLQRE GFQPFFACQTRVRDPGRREHTKHMLRLRREGQITGKQVPEIILLNSHDGTSSYQMLPGLF RAVCQNGLVCGESFGEVRVPHKGDVVSQVIEGAYEVLGIFDRVEEKRDAMQSLLLPPPAQ QALAKAALTYRFGEDHQPVTESQILSPRRWQDESNDLWTTYQRIQENLIKGGLSGRNAKG GRSHTRAVRGIDGDVKLNRALWVMAEALLTQLQ P0A8D3 P52088 P75703 Q2MC38 Q8XEB0 YAII_ECOLI UPF0178 protein YaiI yaiI b0387 JW0378 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-134 K12 / EMG2 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 120-152 K12 P77390 citC false 2 Belongs to the UPF0178 family. Translation N-terminally shortened. Complete proteome Reference proteome MTIWVDADACPNVIKEILYRAAERMQMPLVLVANQSLRVPPSRFIRTLRVAAGFDVADNE IVRQCEAGDLVITADIPLAAEAIEKGAAALNPRGERYTPATIRERLTMRDFMDTLRASGI QTGGPDSLSQRDRQAFAAELEKWWLEVQRSRG P0DSF1 YNAN_ECOLI Protein YnaN ynaN b4773 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 IDENTIFICATION INDUCTION K12 / MG1655 / ATCC 47076 Expressed in both exponential and stationary phase in rich medium; expression is slightly higher in stationary phase (at protein level). Complete proteome Reference proteome MLRNRARRLDYKIMR P39220 A0A385XMP4 P75632 Q8KJP8 YABP_ECOLI Protein YabP yabP b4659 JW0055 b0056 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 IDENTIFICATION May be missing up to 80 C-terminal residues compared to orthologs. Complete proteome Reference proteome MKVSVPGMPVTLLNMSKNDIYKMVSGDKMDVKMNIFQRLWETLRHLFWSDKQTEAYKLLF NFVNNQTGNINASEYFTGAINENEREKFINSLELFNKLKTCAKNPDELVAKGNMRWVAQT FGDIELSVTFFIEKNKICTQTLQLHKGQGNLGVDLRKAYLPGVDMRDCYLGKKTMKGSND ILYERPGWNANLGVLPRTVLPRTVLTRTVLTWTVLP P0A8A0 P24237 YEBC_ECOLI Probable transcriptional regulatory protein YebC yebC b1864 JW1853 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 IDENTIFICATION BY MASS SPECTROMETRY B / BL21 X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) Cytoplasm Belongs to the TACO1 family. 3D-structure Complete proteome Cytoplasm DNA-binding Reference proteome Transcription Transcription regulation MAGHSKWANTRHRKAAQDAKRGKIFTKIIRELVTAAKLGGGDPDANPRLRAAVDKALSNN MTRDTLNRAIARGVGGDDDANMETIIYEGYGPGGTAIMIECLSDNRNRTVAEVRHAFSKC GGNLGTDGSVAYLFSKKGVISFEKGDEDTIMEAALEAGAEDVVTYDDGAIDVYTAWEEMG KVRDALEAAGLKADSAEVSMIPSTKADMDAETAPKLMRLIDMLEDCDDVQEVYHNGEISD EVAATL P45472 Q2M955 YHBQ_ECOLI UPF0213 protein YhbQ yhbQ b3155 JW3124 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Belongs to the UPF0213 family. Complete proteome Reference proteome MTPWFLYLIRTADNKLYTGITTDVERRYQQHQSGKGAKALRGKGELTLVFSAPVGDRSLA LRAEYRVKQLTKRQKERLVAEGAGFAELLSSLQTPEIKSD P33020 P76443 Q2MAR9 YEII_ECOLI Uncharacterized sugar kinase YeiI 2.7.1.- yeiI b2160 JW2147 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / BHB2600 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26 K12 Belongs to the carbohydrate kinase PfkB family. Complete proteome Kinase Reference proteome Transferase CAAISRASGSLNNPTLSADNALSLVPMV ARQFRAPAAA MNNREKEILAILRRNPLIQQNEIADMLQISRSRVAAHIMDLMRKGRIKGKGYILTEQEYC VVVGTINMDIRGMADIRYPQSASHPGTIHCSAGGVGRNIAHNLALLGRDVHLLSVIGDDF YGEMLLEETRRAGVNVSGCVRLHGQSTSTYLAIANRDDQTVLAINDTHLLEQLTPQLLNG SRDLLRHAGVVLADCNLTAEALEWVFTLADEIPVFVDTVSEFKAGKIKHWLAHIHTLKPT LPELEILWGQAITSDADRNTAVNALHQQGVQQLFVYLPDESVYCSEKDGEQFLLTAPAHT TVDSFGADDGFMAGLVYSFLEGYSFRDSARFAVACAAISRASGSLNNPTLSADNALSLVP MV P75821 YBJS_ECOLI Uncharacterized protein YbjS ybjS b0868 JW5819 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Belongs to the NAD(P)-dependent epimerase/dehydratase family. Complete proteome Reference proteome MKVLVTGATSGLGRNAVEFLCQKGISVRATGRNEAMGKLLEKMGAEFVPADLTELVSSQA KVMLAGIDTLWHCSSFTSPWGTQQAFDLANVRATRRLGEWAVAWGVRNFIHISSPSLYFD YHHHRDIKEDFRPHRFANEFARSKAASEEVINMLSQANPQTRFTILRPQSLFGPHDKVFI PRLAHMMHHYGSILLPHGGSALVDMTYYENAVHAMWLASQEACDKLPSGRVYNITNGEHR TLRSIVQKLIDELNIDCRIRSVPYPMLDMIARSMERLGRKSAKEPPLTHYGVSKLNFDFT LDITRAQEELGYQPVITLDEGIEKTAAWLRDHGKLPR P27837 P76756 Q2M8A4 Q6BEZ8 YIFK_ECOLI Probable transport protein YifK yifK b3795 JW5595 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] SEQUENCE REVISION TO 68 AND 74-75 K12 / MG1655 / ATCC 47076 SEQUENCE REVISION TO 68 AND 346-349 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 TOPOLOGY [LARGE SCALE ANALYSIS] K12 / MG1655 / ATCC 47076 Probable amino-acid or metabolite transport protein. Cell inner membrane Multi-pass membrane protein Belongs to the amino acid-polyamine-organocation (APC) superfamily. Amino-acid transport Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix Transport GS VA GSCL AHAW MADNKPELQRGLEARHIELIALGGTIGVGLFMGAASTLKWAGPSVLLAYIIAGLFVFFIM RSMGEMLFLEPVTGSFAVYAHRYMSPFFGYLTAWSYWFMWMAVGISEITAIGVYVQFWFP EMAQWIPALIAVALVALANLAAVRLYGEIEFWFAMIKVTTIIVMIVIGLGVIFFGFGNGG QSIGFSNLTEHGGFFAGGWKGFLTALCIVVASYQGVELIGITAGEAKNPQVTLRSAVGKV LWRILIFYVGAIFVIVTIFPWNEIGSNGSPFVLTFAKIGITAAAGIINFVVLTAALSGCN SGMYSCGRMLYALAKNRQLPAAMAKVSRHGVPVAGVAVSIAILLIGSCLNYIIPNPQRVF VYVYSASVLPGMVPWFVILISQLRFRRAHKAAIASHPFRSILFPWANYVTMAFLICVLIG MYFNEDTRMSLFVGIIFMLAVTAIYKVFGLNRHGKAHKLEE P36661 P75889 YCCE_ECOLI Uncharacterized protein YccE ORF-D yccE b1001 JW0986 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-242 K12 Complete proteome Reference proteome MGSNIHGISCTANNYLKQAWNDIKNEYEKNQTYSITLFENTLVCFMRLYNELRRKVNEED TPCLECESLEKEFEEMQNDNDLSLFMRILRTNDTQIYSGVSGGITYTIQYVRDIDIVRVS LPGRASESITDFKGYYWYNFMEYIENINACDDVFSEYCFDDENISVQPERINTPGISDLD SDIDLSGISFIQRETNQALGLKYAPVDGDGYCLLRAILVLKQHDYSWALVSYKMQKEVYN EFIKMVDKKTIEALVDTAFYNLREDVKTLFGVDLQSDNQIQGQSSLMSWSFLFFKKQFID SCLNNEKCILHLPEFIFNDNKNLLALDTDTSDRIKAVKNFLVVLSDSICSLFIVNSNVAS ISLGNESFSTDEDLEYGYLMNTGNHYDVYLPPELFAQAYKLNNKEMNAQLDYLNRYAI P0AB12 P37065 P75871 YCCF_ECOLI Inner membrane protein YccF yccF b0961 JW0944 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-35 IDENTIFICATION TOPOLOGY [LARGE SCALE ANALYSIS] K12 / MG1655 / ATCC 47076 Cell inner membrane Multi-pass membrane protein Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MRTVLNILNFVLGGFATTLGWLLATLVSIVLIFTLPLTRSCWEITKLSLVPYGNEAIHVD ELNPAGKNVLLNTGGTVLNIFWLIFFGWWLCLMHIATGIAQCISIIGIPVGIANFKIAAI ALWPVGRRVVSVETAQAAREANARRRFE P32157 Q2M8K7 YIIM_ECOLI Protein YiiM yiiM b3910 JW5559 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS) SUBUNIT Monomer. Translation N-terminally shortened. 3D-structure Complete proteome Reference proteome MRYPVDVYTGKIQAYPEGKPSAIAKIQVDGELMLTELGLEGDEQAEKKVHGGPDRALCHY PREHYLYWAREFPEQAELFVAPAFGENLSTDGLTESNVYMGDIFRWGEALIQVSQPRSPC YKLNYHFDISDIAQLMQNTGKVGWLYSVIAPGKVSADAPLELVSRVSDVTVQEAAAIAWH MPFDDDQYHRLLSAAGLSKSWTRTMQKRRLSGKIEDFSRRLWGK P64515 P76289 Q2MB08 YECN_ECOLI Inner membrane protein YecN yecN b1869 JW5308 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 TOPOLOGY [LARGE SCALE ANALYSIS] K12 / MG1655 / ATCC 47076 Cell inner membrane Single-pass membrane protein Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MVSALYAVLSALLLMKFSFDVVRLRMQYRVAYGDGGFSELQSAIRIHGNAVEYIPIAIVL MLFMEMNGAETWMVHICGIVLLAGRLMHYYGFHHRLFRWRRSGMSATWCALLLMVLANLW YMPWELVFSLR P77294 YDER_ECOLI Uncharacterized fimbrial-like protein YdeR ydeR b1503 JW1497 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Fimbrium Belongs to the fimbrial protein family. Complete proteome Disulfide bond Fimbrium Reference proteome Signal MKRLHKRFLLATFCALFTATLQAADVTITVNGRVVAKPCTIQTKEANVNLGDLYTRNLQQ PGSASGWHNITLSLTDCPVETSAVTAIVTGSTDNTGYYKNEGTAENIQIELRDDQDAALK NGDSKTVIVDEITRNAQFPLKARAITVNGNASQGTIEALINVIYTWQ P0AF45 P32686 Q2M6S8 Q9Z3E1 YJBE_ECOLI Uncharacterized protein YjbE yjbE b4026 JW3986 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Complete proteome Reference proteome Signal MKKVLYGIFAISALAATSAWAAPVQVGEAAGSAATSVSAGSSSATSVSTVSSAVGVALAA TGGGDGSNTGTTTTTTTSTQ P64476 P76195 Q2MB55 YDIH_ECOLI Uncharacterized protein YdiH ydiH b1685 JW1675 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Complete proteome Reference proteome MSTQLDPTQLAIEFLRRDQSNLSPAQYLKRLKQLELEFADLLTLSSAELKEEIYFAWRLG VH P76322 Q2MB03 YEDM_ECOLI Uncharacterized protein YedM yedM b1935 JW1920 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] JA11 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Complete proteome Reference proteome MFPLNDLSLKTQPVQLNKVTSNTESTIKQHELVSDDAIINELSSELVSCLGNGKFTPISE DSKLFNMLSEFKLLHSEYFEWGDYSLWFQDFSIYNKIGFIMIEKIRELVTHPFGIN P07650 Q2M5T5 TYPH_ECOLI Thymidine phosphorylase 2.4.2.4 TdRPase deoA tpp ttg b4382 JW4345 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 377-440 K12 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18 X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) The enzymes which catalyze the reversible phosphorolysis of pyrimidine nucleosides are involved in the degradation of these compounds and in their utilization as carbon and energy sources, or in the rescue of pyrimidine bases for nucleotide synthesis. phosphate + thymidine = 2-deoxy-alpha-D-ribose 1-phosphate + thymine Pyrimidine metabolism; dTMP biosynthesis via salvage pathway; dTMP from thymine: step 1/2. Homodimer. Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family. 3D-structure Complete proteome Glycosyltransferase Reference proteome Transferase MFLAQEIIRKKRDGHALSDEEIRFFINGIRDNTISEGQIAALAMTIFFHDMTMPERVSLT MAMRDSGTVLDWKSLHLNGPIVDKHSTGGVGDVTSLMLGPMVAACGGYIPMISGRGLGHT GGTLDKLESIPGFDIFPDDNRFREIIKDVGVAIIGQTSSLAPADKRFYATRDITATVDSI PLITASILAKKLAEGLDALVMDVKVGSGAFMPTYELSEALAEAIVGVANGAGVRTTALLT DMNQVLASSAGNAVEVREAVQFLTGEYRNPRLFDVTMALCVEMLISGKLAKDDAEARAKL QAVLDNGKAAEVFGRMVAAQKGPTDFVENYAKYLPTAMLTKAVYADTEGFVSEMDTRALG MAVVAMGGGRRQASDTIDYSVGFTDMARLGDQVDGQRPLAVIHAKDENNWQEAAKAVKAA IKLADKAPESTPTVYRRISE P37908 P76600 P76601 P77009 Q6BF70 YFJD_ECOLI UPF0053 inner membrane protein YfjD yfjD ypjE b4461 JW5415 b2612/b2613 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 SEQUENCE REVISION NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 322-428 B178 IDENTIFICATION TOPOLOGY [LARGE SCALE ANALYSIS] K12 / MG1655 / ATCC 47076 Cell inner membrane Multi-pass membrane protein Belongs to the UPF0053 family. CBS domain Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Repeat Transmembrane Transmembrane helix MEHISTTTLIIILIIMVVISAYFSGSETGMMTLNRYRLRHMAKQGNRSAKRVEKLLRKPD RLISLVLIGNNLVNILASALGTIVGMRLYGDAGVAIATGVLTFVVLVFAEVLPKTIAALY PEKVAYPSSFLLAPLQILMMPLVWLLNAITRMLMRMMGIKTDIVVSGSLSKEELRTIVHE SRSQISRRNQDMLLSVLDLEKMTVDDIMVPRSEIIGIDINDDWKSILRQLSHSPHGRIVL YRDSLDDAISMLRVREAWRLMSEKKEFTKETMLRAADEIYFVPEGTPLSTQLVKFQRNKK KVGLVVNEYGDIQGLVTVEDILEEIVGDFTTSMSPTLAEEVTPQNDGSVIIDGTANVREI NKAFNWHLPEDDARTVNGVILEALEEIPVAGTRVRIGEYDIDILDVQDNMIKQVKVFPVK PLRESVAE P76463 Q2MAN6 YFAQ_ECOLI Uncharacterized protein YfaQ yfaQ b2226 JW2220 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Complete proteome Reference proteome Signal MNWRRIVWLLALVTLPTLAEETPLQLVLRGAQHDQLYQLSSSGVTKVSALPDSLTTPLGS LWKLYVYAWLEDTHQPEQPYQCRGNSPEEVYCCQAGESITRDTALVRSCGLYFAPQRLHI GADVWGQYWQQRQAPAWLASLTTLKPETSVTVKSLLDSLATLPAQNKAQEVLLDVVLDEA KIGVASMLGSRVRVKTWSWFADDKQEIRQGGFAGWLTDGTPLWVTGSGTSKTVLTRYATV LNRVLPVPTQVASGQCVEVELFARYPLKKITAEKSTTAVNPGVLNGRYRVTFTNGNHITF VSHGETTLLSEKGKLKLQSHLDREEYVARVLDREAKSTPPEAAKAMTVAIRTFLQQNANR EGDCLTIPDSSATQRVSASPATTGARTMTAWTQDLIYAGDPVHYHGSRATEGTLSWRQAT AQAGQGERYDQILAFAYPDNSLSRWGAPRSTCQLLPKAKAWLAKKMPQWRRILQAETGYN EPDVFAVCRLVSGFPYTDRQQKRLFIRNFFTLQDRLDLTHEYLHLAFDGYPTGLDENYIE TLTRQLLMD P76482 Q2MAM7 YFBL_ECOLI Uncharacterized protein YfbL yfbL b2271 JW2266 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Membrane Single-pass membrane protein Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MKKIIFAFIILFVFLLPMIIFYQPWVNALPSTPRHASPEQLEKTVRYLTQTVHPRSADNI DNLNRSAEYIKEVFVSSGARVTSQDVPITGGPYKNIVADYGPADGPLIIIGAHYDSASSY ENDQLTYTPGADDNASGVAGLLELARLLHQQVPKTGVQLVAYASEEPPFFRSDEMGSAVH AASLERPVKLMIALEMIGYYDSAPGSQNYPYPAMSWLYPDRGDFIAVVGRIQDINAVRQV KAALLSSQDLSVYSMNTPGFIPGIDFSDHLNYWQHDIPAIMITDTAFYRNKQYHLPGDTA DRLNYQKMAQVVDGVITLLYNSK P75977 Q2MBH6 YMFM_ECOLI Uncharacterized protein YmfM ymfM b1148 JW1134 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Complete proteome Reference proteome MNSLTTHYRRSQLIALPVPGGKAKVEYCYAVNVPGDREIVTHSFAEWAVGDFNRQKETVL CDKLTAGSKITTECPSESFVGSRKHNGLSTSAKVMSMNASARSNSFVVNSGK P0ACS5 P36676 Q2M6V7 ZNTR_ECOLI HTH-type transcriptional regulator ZntR Zn(II)-responsive regulator of zntA zntR yhdM b3292 JW3254 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 CHARACTERIZATION X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) Zinc-responsive transcriptional regulator of zntA. Homodimer. P75959 nagK false 2 3D-structure Complete proteome DNA-binding Metal-binding Reference proteome Transcription Transcription regulation Zinc MYRIGELAKMAEVTPDTIRYYEKQQMMEHEVRTEGGFRLYTESDLQRLKFIRHARQLGFS LESIRELLSIRIDPEHHTCQESKGIVQERLQEVEARIAELQSMQRSLQRLNDACCGTAHS SVYCSILEALEQGASGVKSGC P33941 P33942 YOJI_ECOLI ABC transporter ATP-binding/permease protein YojI yojI yojJ b2211 JW2199 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / BHB2600 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION IN MICROCIN J25 RESISTANCE DISRUPTION PHENOTYPE K12 Mediates resistance to the antibacterial peptide microcin J25, when expressed from a multicopy vector. Functions as an efflux pump for microcin J25, with the help of the outer membrane channel TolC. Cell inner membrane Multi-pass membrane protein Disruption increases sensitivity of cells to microcin J25. Belongs to the ABC transporter superfamily. Antibiotic resistance ATP-binding Cell inner membrane Cell membrane Complete proteome Membrane Nucleotide-binding Reference proteome Transmembrane Transmembrane helix Transport MELLVLVWRQYRWPFISVMALSLASAALGIGLIAFINQRLIETADTSLLVLPEFLGLLLL LMAVTLGSQLALTTLGHHFVYRLRSEFIKRILDTHVERIEQLGSASLLAGLTSDVRNITI AFVRLPELVQGIILTIGSAAYLWMLSGKMLLVTAIWMAITIWGGFVLVARVYKHMATLRE TEDKLYTDFQTVLEGRKELTLNRERAEYVFNNLYIPDAQEYRHHIIRADTFHLSAVNWSN IMMLGAIGLVFWMANSLGWADTNVAATYSLTLLFLRTPLLSAVGALPTLLTAQVAFNKLN KFALAPFKAEFPRPQAFPNWQTLELRNVTFAYQDNAFSVGPINLTIKRGELLFLIGGNGS GKSTLAMLLTGLYQPQSGEILLDGKPVSGEQPEDYRKLFSAVFTDVWLFDQLLGPEGKPA NPQLVEKWLAQLKMAHKLELSNGRIVNLKLSKGQKKRVALLLALAEERDIILLDEWAADQ DPHFRREFYQVLLPLMQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSELTGEERDAASR DAVARTA P0AFU2 P76935 P77741 YFBS_ECOLI Uncharacterized transporter YfbS yfbS b2292 JW2289 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Cell inner membrane Multi-pass membrane protein Belongs to the CitM (TC 2.A.11) transporter family. Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Repeat Transmembrane Transmembrane helix Transport MNGELIWVLSLLAVAIVLFATGRVRMDAVALFVIVAFALSGTLTVPEVFSGFSDPNVVLI AALFIIGDGLVRTGVATVMGTWLVKVAGNSEIKMLVLLMLTVAGLGAFMSSTGVVAIFIP VVLSVAMRMQTSPSRLMMPLSFAGLISGMMTLVATPPNLVVNSELLREGYHGFSFFSVTP IGLVVLVLGILYMLVMRFMLKGDTQTPQREGWTRRTFRDLIREYRLTGRARRLAIRPGSP MIGQRLDDLKLRERYGANVIGVERWRRFRRVIVNVNGVSEFRARDVLLIDMSAADVDLRQ FCSEQLLEPMVLRGEYFSDQALDVGMAEISLIPESELIGKSVREIGFRTRYGLNVVGLKR NGVALEGSLADEPLLLGDIILVVGNWKLIGMLAKQGRDFVALNLPEEVSEASPAHSQAPH AIFCLVLMVALMLTDEIPNPVAAIIACLLMGKFRCIDAESAYKSIHWPSIILIVGMMPFA VALQKTGGVALAVKGLMDIGGGYGPHMMLGCLFVLSAVIGLFISNTATAVLMAPIALAAA KTMGVSPYPFAMVVAMAASAAFMTPVSSPVNTLVLGPGNYSFSDFVKLGVPFTIIVMAVC VVMIPMLFPF P0A8W8 P76492 Q2MAM1 YFBU_ECOLI UPF0304 protein YfbU yfbU b2294 JW2291 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 IDENTIFICATION BY MASS SPECTROMETRY B / BL21 INDUCTION K12 / MC4100 / ATCC 35695 / DSM 6574 Only a leaderless mRNA has been detected in vivo, the first nucleotide is the beginning of the start codon. Belongs to the UPF0304 family. Complete proteome Reference proteome MEMTNAQRLILSNQYKMMTMLDPANAERYRRLQTIIERGYGLQMRELDREFGELKEETCR TIIDIMEMYHALHVSWSNLQDQQSIDERRVTFLGFDAATEARYLGYVRFMVNVEGRYTHF DAGTHGFNAQTPMWEKYQRMLNVWHACPRQYHLSANEINQIINA P77562 Q2MC47 YAIW_ECOLI Uncharacterized protein YaiW yaiW b0378 JW0369 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Complete proteome Reference proteome MSRVNPLSSLSLLAVLVLAGCSSQAPQPLKKGEKAIDVASVVRQKMPASVKDRDAWAKDL ATTFESQGLAPTLENVCSVLAVAQQESNYQADPAVPGLSKIAWQEIDRRAERMHIPAFLV HTALKIKSPNGKSYSERLDSVRTEKQLSAIFDDLINMVPMGQTLFGSLNPVRTGGPMQVS IAFAEQHTKGYPWKMDGTVRQEVFSRRGGLWFGTYHLLNYPASYSAPIYRFADFNAGWYA SRNAAFQNAVSKASGVKLALDGDLIRYDSKEPGKTELATRKLAAKLGMSDSEIRRQLEKG DSFSFEETALYKKVYQLAETKTGKSLPREMLPGIQLESPKITRNLTTAWFAKRVDERRAR CMKQ P64574 Q2M9J7 Q46848 YGHW_ECOLI Uncharacterized protein YghW yghW b2998 JW2966 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Complete proteome Reference proteome MNNHFGKGLMAGLKATHADSAVNVTKFCADYKRGFVLGYSHRMYEKTGDRQLSAWEAGIL TRRYGLDKEMVMDFFRENNSCSTLRFFMAGYRLEN Q46861 Q2M9I4 Q46862 Q6BF53 YGIQ_ECOLI UPF0313 protein YgiQ ygiQ ygiR b4469 JW5501 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 SEQUENCE REVISION NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 [4Fe-4S] cluster Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. Belongs to the UPF0313 family. 4Fe-4S Complete proteome Iron Iron-sulfur Metal-binding Reference proteome S-adenosyl-L-methionine MSSISLIQPDRDLFSWPQYWAACFGPAPFLPMSREEMDQLGWDSCDIILVTGDAYVDHPS FGMAICGRMLEAQGFRVGIIAQPDWSSKDDFMRLGKPNLFFGVTAGNMDSMINRYTADRR LRHDDAYTPDNVAGKRPDRATLVYTQRCKEAWKDVPVILGGIEASLRRTAHYDYWSDTVR RSVLVDSKADMLMFGNGERPLVEVAHRLAMGEPISEIRDVRNTAIIVKEALPGWSGVDST RLDTPGKIDPIPHPYGEDLPCADNKPVAPKKQEAKAVTVQPPRPKPWEKTYVLLPSFEKV KGDKVLYAHASRILHHETNPGCARALMQKHGDRYVWINPPAIPLSTEEMDSVFALPYKRV PHPAYGNARIPAYEMIRFSVNIMRGCFGGCSFCSITEHEGRIIQSRSEDSIINEIEAIRD TVPGFTGVISDLGGPTANMYMLRCKSPRAEQTCRRLSCVYPDICPHMDTNHEPTINLYRR ARDLKGIKKILIASGVRYDIAVEDPRYIKELATHHVGGYLKIAPEHTEEGPLSKMMKPGM GSYDRFKELFDTYSKQAGKEQYLIPYFISAHPGTRDEDMVNLALWLKKHRFRLDQVQNFY PSPLANSTTMYYTGKNPLAKIGYKSEDVFVPKGDKQRRLHKALLRYHDPANWPLIRQALE AMGKKHLIGSRRDCLVPAPTIEEMREARRQNRNTRPALTKHTPMATQRQTPATAKKASST QSRPVNAGAKKRPKAAVGR P76115 Q2MBB2 YNCD_ECOLI Probable TonB-dependent receptor YncD yncD b1451 JW1446 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Probable receptor, TonB-dependent. Cell outer membrane Peripheral membrane protein Belongs to the TonB-dependent receptor family. Cell outer membrane Complete proteome Membrane Receptor Reference proteome Signal TonB box Transmembrane Transmembrane beta strand MKIFSVRQTVLPALLVLSPVVFAADEQTMIVSAAPQVVSELDTPAAVSVVDGEEMRLATP RINLSESLTGVPGLQVQNRQNYAQDLQLSIRGFGSRSTYGIRGIRLYVDGIPATMPDGQG QTSNIDLSSVQNVEVLRGPFSALYGNASGGVMNVTTQTGQQPPTIEASSYYGSFGSWRYG LKATGATGDGTQPGDVDYTVSTTRFTTHGYRDHSGAQKNLANAKLGVRIDEASKLSLIFN SVDIKADDPGGLTKAEWKANPQQAPRAEQYDTRKTIKQTQAGLRYERSLSSRDDMSVMMY AGERETTQYQSIPMAPQLNPSHAGGVITLQRHYQGIDSRWTHRGELGVPVTFTTGLNYEN MSENRKGYNNFRLNSGMPEYGQKGELRRDERNLMWNIDPYLQTQWQLSEKLSLDAGVRYS SVWFDSNDHYVTPGNGDDSGDASYHKWLPAGSLKYAMTDAWNIYLAAGRGFETPTINELS YRADGQSGMNLGLKPSTNDTIEIGSKTRIGDGLLSLALFQTDTDDEIVVDSSSGGRTTYK NAGKTRRQGAELAWDQRFAGDFRVNASWTWLDATYRSNVCNEQDCNGNRMPGIARNMGFA SIGYVPEDGWYAGTEARYMGDIMADDENTAKAPSYTLVGLFTGYKYNYHNLTVDLFGRVD NLFDKEYVGSVIVNESNGRYYEPSPGRNYGVGMNIAWRFE P05847 P33130 Q2M9E4 TTDA_ECOLI L(+)-tartrate dehydratase subunit alpha L-TTD alpha 4.2.1.32 ttdA ygjA b3061 JW3033 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] CATALYTIC ACTIVITY SUBUNIT COFACTOR K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 INDUCTION (2R,3R)-tartrate = H2O + oxaloacetate iron-sulfur cluster Tetramer of two alpha and two beta subunits. P0ACL0 glpR false 2 Induced by tartrate, via TtdR. Belongs to the class-I fumarase family. 4Fe-4S Complete proteome Iron Iron-sulfur Lyase Metal-binding Reference proteome V L EL DV MMSESNKQQAVNKLTEIVANFTAMISTRMPDDVVDKLKQLKDAETSSMGKIIYHTMFDNM QKAIDLNRPACQDTGEIMFFVKVGSRFPLLGELQSILKQAVEEATVKAPLRHNAVEIFDE VNTGKNTGSGVPWVTWDIIPDNDDAEIEVYMAGGGCTLPGRSKVLMPSEGYEGVVKFVFE NISTLAVNACPPVLVGVGIATSVETAAVLSRKAILRPIGSRHPNPKAAELELRLEEGLNR LGIGPQGLTGNSSVMGVHIESAARHPSTIGVAVSTGCWAHRRGTLLVHADLTFENLSHTR SAL P76498 Q2MAL7 YFCO_ECOLI Uncharacterized protein YfcO yfcO b2332 JW2329 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION INDUCTION DISRUPTION PHENOTYPE K12 / MG1655 / ATCC 47076 Part of the yfcOPQRSUV fimbrial operon. Could contribute to adhesion to various surfaces in specific environmental niches. Increases adhesion to eukaryotic T24 bladder epithelial cells in the absence of fim genes. Expression is negatively regulated by H-NS and subjected to cAMP receptor protein (CRP)-mediated catabolite repression. Deletion of the operon under classical laboratory conditions does not result in any major effect on E.coli capacity to form biofilms compared with the wild-type strain. The operon is cryptic under classical laboratory conditions, but is functional when constitutively expressed. To S.typhimurium YadU. Complete proteome Reference proteome Signal MKILRWLFALVMLIATTEAMAAGHSVDVYYGYNGDSRNIATFNLKIMMPSAVYVGEYKSS QWLMTGEILQNVSWSGPPPAPSVKLIGYHQNINKASCPGLPSGWNCGYYTFEVIVSAEIE SYFSCPWLVIMNDSEASPGGVTYQGPDSHDTICPSVSVQPYDVSWNENYVSKSKLLTLQS TGGVVEKTLSTYLMKDGKLCDSTQMNETGGYCRWVAQMITFTASGCDKAEVSVTPNRHPI TDKQLHDMVVRVDTSSMQPIDSTCRFQYILNEL A5A621 YPFM_ECOLI Uncharacterized protein YpfM ypfM b4606 JW2454.1 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 SUBCELLULAR LOCATION INDUCTION K12 / MG1655 / ATCC 47076 INDUCTION K12 / MG1655 / ATCC 47076 Cytoplasm Constitutively expressed (PubMed:19121005), increases in stationary phase and at 45 degrees Celsius (PubMed:19121005) (at protein level). Complete proteome Cytoplasm Reference proteome Stress response MIERELGNWKDFIEVMLRK P0A8D6 P75918 YMDB_ECOLI O-acetyl-ADP-ribose deacetylase 3.5.1.- Regulator of RNase III activity ymdB b1045 JW1032 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION SUBUNIT INTERACTION WITH RIBONUCLEASE 3 INDUCTION FUNCTION CATALYTIC ACTIVITY BIOPHYSICOCHEMICAL PROPERTIES MUTAGENESIS OF GLY-124 FUNCTION INTERACTION WITH RNASE III MUTAGENESIS OF ARG-40 FUNCTION FUNCTION INDUCTION X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-176 X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF WILD-TYPE AND MUTANTS ALA-25/ALA-35 AND ALA-126 IN COMPLEXES WITH ADP-RIBOSE FUNCTION CATALYTIC ACTIVITY BIOPHYSICOCHEMICAL PROPERTIES ACTIVE SITE MUTAGENESIS OF ASN-25; ASP-35 AND TYR-126 Deacetylates O-acetyl-ADP ribose to yield ADP-ribose and free acetate (PubMed:21257746, PubMed:26481419). Down-regulates ribonuclease 3 (RNase III) activity. Acts by interacting directly with the region of the ribonuclease that is required for dimerization/activation (PubMed:19141481). Overexpression inhibits biofilm formation via an RNase III-independent pathway. This inhibition is RpoS-dependent (PubMed:24267348, PubMed:28582517). Overexpression also results in increased susceptibility to apramycin (PubMed:28034758, PubMed:28582517). 2''-O-acetyl-ADP-D-ribose + H2O = acetate + ADP-D-ribose + H(+) 270 uM for O-acetyl-ADP-ribose 430 uM for O-acetyl-ADP-ribose kcat is 0.48 sec(-1) (PubMed:21257746). kcat is 1.31 sec(-1) (PubMed:26481419). Homodimer (PubMed:19141481). Interacts with RNase III (PubMed:19141481, PubMed:25546632). Interaction with the ribonuclease decreases homodimer formation (PubMed:19141481). Expression is induced by both entry into stationary phase, via RpoS, and cold-shock stress. Belongs to the YmdB family. 3D-structure Complete proteome Hydrolase Reference proteome Stress response N A D A R A G E Y A Y F MKTRIHVVQGDITKLAVDVIVNAANPSLMGGGGVDGAIHRAAGPALLDACLKVRQQQGDC PTGHAVITLAGDLPAKAVVHTVGPVWRGGEQNEDQLLQDAYLNSLRLVAANSYTSVAFPA ISTGVYGYPRAAAAEIAVKTVSEFITRHALPEQVYFVCYDEENAHLYERLLTQQGDE P0A8H3 P24198 Q2M9G0 ZUPT_ECOLI Zinc transporter ZupT zupT ygiE b3040 JW3008 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 CHARACTERIZATION FUNCTION Mediates zinc uptake. May also transport other divalent cations such as copper and cadmium ions. Cell membrane Multi-pass membrane protein Belongs to the ZIP transporter (TC 2.A.5) family. ZupT subfamily. Cell membrane Complete proteome Ion transport Membrane Reference proteome Transmembrane Transmembrane helix Transport Zinc Zinc transport MSVPLILTILAGAATFIGAFLGVLGQKPSNRLLAFSLGFAAGIMLLISLMEMLPAALAAE GMSPVLGYGMFIFGLLGYFGLDRMLPHAHPQDLMQKSVQPLPKSIKRTAILLTLGISLHN FPEGIATFVTASSNLELGFGIALAVALHNIPEGLAVAGPVYAATGSKRTAILWAGISGLA EILGGVLAWLILGSMISPVVMAAIMAAVAGIMVALSVDELMPLAKEIDPNNNPSYGVLCG MSVMGFSLVLLQTAGIG P0AE45 P39319 Q2M687 YTFL_ECOLI UPF0053 inner membrane protein YtfL ytfL b4218 JW4177 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 TOPOLOGY [LARGE SCALE ANALYSIS] K12 / MG1655 / ATCC 47076 Cell inner membrane Multi-pass membrane protein Belongs to the UPF0053 family. CBS domain Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Repeat Transmembrane Transmembrane helix MLNSILVILCLIAVSAFFSMSEISLAASRKIKLKLLADEGNINAQRVLNMQENPGMFFTV VQIGLNAVAILGGIVGDAAFSPAFHSLFSRYMSAELSEQLSFILSFSLVTGMFILFADLT PKRIGMIAPEAVALRIINPMRFCLYVCTPLVWFFNGLANIIFRIFKLPMVRKDDITSDDI YAVVEAGALAGVLRKQEHELIENVFELESRTVPSSMTPRENVIWFDLHEDEQSLKNKVAE HPHSKFLVCNEDIDHIIGYVDSKDLLNRVLANQSLALNSGVQIRNTLIVPDTLTLSEALE SFKTAGEDFAVIMNEYALVVGIITLNDVMTTLMGDLVGQGLEEQIVARDENSWLIDGGTP IDDVMRVLDIDEFPQSGNYETIGGFMMFMLRKIPKRTDSVKFAGYKFEVVDIDNYRIDQL LVTRIDSKATALSPKLPDAKDKEESVA Q2EET0 A0A385XJL1 Q2MAK3 YPDJ_ECOLI Protein YpdJ ypdJ b4545 JW5386 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION DISRUPTION PHENOTYPE K12 / BW25113 May be involved in H(2) production during fermentative growth. Loss of H(2) production on minimal glucose, complex glucose and complex formate medium. Alters production of organic acids when grown on minimal glucose medium. This phenotype was not complemented by reintroduction of the ypdJ gene. It is missing about 100 C-terminal amino acids compared to orthologs. Encoded by the CPS-53 (KpLE1) prophage. Complete proteome Reference proteome MGYDSRLDHLAATSWYPFFNNVTTRGEIIEPYSLTLDEACQFLKIS Q47534 Q2MC66 YAIO_ECOLI Outer membrane protein YaiO yaiO b0358 JW0349 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 SUBCELLULAR LOCATION K12 / MG1655 / ATCC 47076 Cell outer membrane Cell outer membrane Complete proteome Membrane Reference proteome Signal MIKRTLLAAAIFSALPAYAGLTSITAGYDFTDYSGDHGNRNLAYAELVAKVENATLLFNL SQGRRDYETEHFNATRGQGAVWYKWNNWLTTRTGIAFADNTPVFARQDFRQDINLALLPK TLFTTGYRYTKYYDDVEVDAWQGGVSLYTGPVITSYRYTHYDSSDAGGSYSNMISVRLND PRGTGYTQLWLSRGTGAYTYDWTPETRYGSMKSVSLQRIQPLTEQLNLGLTAGKVWYDTP TDDFNGLQLAARLTWKF P77328 Q2MBR5 YBBY_ECOLI Putative purine permease YbbY ybbY glxB4 b0513 JW0501 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 / ECL1 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 TOPOLOGY [LARGE SCALE ANALYSIS] K12 / MG1655 / ATCC 47076 Cell inner membrane Multi-pass membrane protein By glyoxylate. Belongs to the xanthine/uracil permease family. Nucleobase:cation symporter-2 (NCS2) (TC 2.A.40) subfamily. Translation N-terminally shortened. Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix Transport MFNFAVSRESLLSGFQWFFFIFCNTVVVPPTLLSAFQLPQSSLLTLTQYAFLATALACFA QAFCGHRRAIMEGPGGLWWGTILTITLGEASRGTPINDIATSLAVGIALSGVLTMLIGFS GLGHRLARLFTPSVMVLFMLMLGAQLTTIFFKGMLGLPFGIADPNFKIQLPPFALSVAVM CLVLAMIIFLPQRFARYGLLVGTITGWLLWYFCFPSSHSLSGELHWQWFPLGSGGALSPG IILTAVITGLVNISNTYGAIRGTDVFYPQQGAGNTRYRRSFVATGFMTLITVPLAVIPFS PFVSSIGLLTQTGDYTRRSFIYGSVICLLVALVPALTRLFCSIPLPVSSAVMLVSYLPLL FSALVFSQQITFTARNIYRLALPLFVGIFLMALPPVYLQDLPLTLRPLLSNGLLVGILLA VLMDNLIPWERIE P45581 P75983 STFP_ECOLI Uncharacterized protein StfP Uncharacterized protein StfP from lambdoid prophage e14 region stfP ycfK b1154 JW1140 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 98-209 K12 IDENTIFICATION To E.coli YfdL and M.jannaschii MJ0347. Complete proteome Reference proteome MHRIDTKTAQKDKFGAGKNGFTRGNPQTGTPATDLDDDYFDMLQEELCSVVEASGASLEK GRHDQLLTALRALLLSRKNPFGDIKSDGTVQTALENLGLGEGAKLNAATATLGRTGFIAI PVMIGGIEQSVIIQWGWNAAKASASGGDGNTVVFPVAFNNACVAVVANYDNVSAPINAVA TGGYTTTSFLLRCAAQTGSYYYNWIAIGY P0AD05 P06979 P76310 YECA_ECOLI Uncharacterized protein YecA yecA b1908 JW1896 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-76 Complete proteome Reference proteome FM AL MKTGPLNESELEWLDDILTKYNTDHAILDVAELDGLLTAVLSSPQEIEPEQWLVAVWGGA DYVPRWASEKEMTRFMNLAFQHMADTAERLNEFPEQFEPLFGLREVDGSELTIVEEWCFG YMRGVALSDWSTLPDSLKPALEAIALHGTEENFERVEKMSPEAFEESVDAIRLAALDLHA YWMAHPQEKAVQQPIKAEEKPGRNDPCPCGSGKKFKQCCLH P0ADD5 P39402 Q2M5V2 YJJP_ECOLI Inner membrane protein YjjP yjjP b4364 JW5796 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 TOPOLOGY [LARGE SCALE ANALYSIS] K12 / MG1655 / ATCC 47076 INDUCTION CSH50 OPERON STRUCTURE INDUCTION K12 / BW25113 Cell inner membrane Multi-pass membrane protein Has 2 promoters, 1 of which is repressed by H-NS. Activated by LeuO. A monocistronic operon. To H.influenzae HI_0108. Translation N-terminally shortened. Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MQTEQQRAVTRLCIQCGLFLLQHGAESALVDELSSRLGRALGMDSVESSISSNAIVLTTI KDGQCLTSTRKNHDRGINMHVVTEVQHIVILAEHHLLDYKGVEKRFSQIQPLRYPRWLVA LMVGLSCACFCKLNNGGWDGAVITFFASTTAMYIRQLLAQRHLHPQINFCLTAFAATTIS GLLLQLPTFSNTPTIAMAASVLLLVPGFPLINAVADMFKGHINTGLARWAIASLLTLATC VGVVMALTIWGLRGWV P41039 YBII_ECOLI Uncharacterized protein YbiI ybiI b0803 JW0788 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 3D-structure Complete proteome Metal-binding Reference proteome Zinc Zinc-finger MASGWANDDAVNEQINSTIEDAIARARGEIPRGESLDECEECGAPIPQARREAIPGVRLC IHCQQEKDLQKPAYTGYNRRGSKDSQLR P0AAQ0 P77273 Q2MC45 YAIZ_ECOLI Uncharacterized protein YaiZ yaiZ b0380 JW5053 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Cell membrane Multi-pass membrane protein Translation N-terminally shortened. Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MNLPVKIRRDWHYYAFAIGLIFILNGVVGLLGFEAKGWQTYAVGLVTWVISFWLAGLIIR RRDEETENAQ P39832 P76286 ZNUB_ECOLI High-affinity zinc uptake system membrane protein ZnuB znuB yebI b1859 JW1848 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-92 K12 / EMG2 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 80-261 IDENTIFICATION CHARACTERIZATION TOPOLOGY [LARGE SCALE ANALYSIS] K12 / MG1655 / ATCC 47076 Involved in the high-affinity zinc uptake transport system. Cell inner membrane Multi-pass membrane protein Belongs to the ABC-3 integral membrane protein family. Cell inner membrane Cell membrane Complete proteome Ion transport Membrane Reference proteome Transmembrane Transmembrane helix Transport Zinc Zinc transport MIELLFPGWLAGIMLACAAGPLGSFVVWRRMSYFGDTLAHASLLGVAFGLLLDVNPFYAV IAVTLLLAGGLVWLEKRPQLAIDTLLGIMAHSALSLGLVVVSLMSNIRVDLMAYLFGDLL AVTPEDLISIAIGVVIVVAILFWQWRNLLSMTISPDLAFVDGVKLQRVKLLLMLVTALTI GVAMKFVGALIITSLLIIPAATARRFARTPEQMAGVAVLVGMVAVTGGLTFSAVYDTPAG PSVVLCAALLFILSMMKKQAS Q47679 Q9R2E1 YAFV_ECOLI Omega-amidase YafV 3.5.1.3 yafV b0219 JW5019 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Hydrolyzes alpha-ketoglutaramate (a-KGM) to alpha-ketoglutarate (alpha-KG) and ammonia, has weak activity on L-glutamine, almost no activity on deaminated glutathione (dGSH) and none on glutathione (By similarity). May function as a metabolite repair enzyme (By similarity). a monoamide of a dicarboxylate + H2O = a dicarboxylate + NH4(+) Belongs to the carbon-nitrogen hydrolase superfamily. NIT1/NIT2 family. Complete proteome Hydrolase Reference proteome MPGLKITLLQQPLVWMDGPANLRHFDRQLEGITGRDVIVLPEMFTSGFAMEAAASSLAQD DVVNWMTAKAQQCNALIAGSVALQTESGSVNRFLLVEPGGTVHFYDKRHLFRMADEHLHY KAGNARVIVEWRGWRILPLVCYDLRFPVWSRNLNDYDLALYVANWPAPRSLHWQALLTAR AIENQAYVAGCNRVGSDGNGCHYRGDSRVINPQGEIIATADAHQATRIDAELSMAALREY REKFPAWQDADEFRLW P0AAX3 P41038 YBIJ_ECOLI Uncharacterized protein YbiJ ybiJ b0802 JW0787 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Periplasm Belongs to the BhsA/McbA family. Complete proteome Periplasm Reference proteome Signal MKTINTVVAAMALSTLSFGVFAAEPVTASQAQNMNKIGVVSADGASTLDALEAKLAEKAA AAGASGYSITSATNNNKLSGTAVIYK P0CB62 YMIA_ECOLI Protein YmiA ymiA b4522 JW1267.1 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 PROTEIN SEQUENCE OF 3-13 K12 / BW25113 SUBCELLULAR LOCATION INDUCTION K12 / MG1655 / ATCC 47076 POSSIBLE FUNCTION SEQUENCE REVISION TO N-TERMINUS K12 / MG1655 / ATCC 47076 Cell inner membrane Single-pass membrane protein Constitutively expressed (at protein level). Translation N-terminally shortened. Cell inner membrane Cell membrane Complete proteome Direct protein sequencing Membrane Reference proteome Transmembrane Transmembrane helix MRLAMPSGNQEPRRDPELKRKAWLAVFLGSALFWVVVALLIWKVWG P0A9X1 P52648 P76285 ZNUC_ECOLI Zinc import ATP-binding protein ZnuC 3.6.3.- znuC yebM b1858 JW1847 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 / EMG2 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION IN ZINC TRANSPORT INDUCTION ATPASE ACTIVITY ACTIVITY REGULATION K12 INDUCTION K12 / W3110 / ATCC 27325 / DSM 5911 Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system. ATP(in) + H2O(in) + Zn(2+)(out) = ADP(in) + H(+)(in) + phosphate(in) + Zn(2+)(in) Inhibited by arsenate. The complex is composed of two ATP-binding proteins (ZnuC), two transmembrane proteins (ZnuB) and a solute-binding protein (ZnuA). Cell inner membrane Peripheral membrane protein Transcriptionally repressed by zur (zinc uptake regulator), in response to high extracellular zinc concentrations. Belongs to the ABC transporter superfamily. Zinc importer (TC 3.A.1.15.5) family. ATP-binding Cell inner membrane Cell membrane Complete proteome Hydrolase Ion transport Membrane Nucleotide-binding Reference proteome Transport Zinc Zinc transport TTLP STLS L W V A G W VLM ALL MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVTPDEGV IKRNGKLRIGYVPQKLYLDTTLPLTVNRFLRLRPGTHKEDILPALKRVQAGHLINAPMQK LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCGVLMVSHD LHLVMAKTDEVLCLNHHICCSGTPEVVSLHPEFISMFGPRGAEQLGIYRHHHNHRHDLQG RIVLRRGNDRS P36680 P75645 Q8KJQ6 Q8KMZ7 ZAPD_ECOLI Cell division protein ZapD Z ring-associated protein D zapD yacF b0102 JW0099 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] SEQUENCE REVISION K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION SUBUNIT INTERACTION WITH FTSZ SUBCELLULAR LOCATION DISRUPTION PHENOTYPE GENE NAME K12 / MG1655 / ATCC 47076 Cell division factor that enhances FtsZ-ring assembly. Directly interacts with FtsZ and promotes bundling of FtsZ protofilaments, with a reduction in FtsZ GTPase activity. Mostly homodimer in solution. Interacts with the C-terminal tail of FtsZ. false 2 P0A9A6 ftsZ false 3 Cytoplasm Localizes to mid-cell in an FtsZ-dependent manner. Localization does not require FtsA, ZipA, ZapA or ZapC. Mutants are viable, with no discernible division phenotypes. Belongs to the ZapD family. 3D-structure Cell cycle Cell division Complete proteome Cytoplasm Reference proteome Septation I T MQTQVLFEHPLNEKMRTWLRIEFLIQQLTVNLPIVDHAGALHFFRNVSELLDVFERGEVR TELLKELDRQQRKLQTWIGVPGVDQSRIEALIQQLKAAGSVLISAPRIGQFLREDRLIAL VRQRLSIPGGCCSFDLPTLHIWLHLPQAQRDSQVETWIASLNPLTQALTMVLDLIRQSAP FRKQTSLNGFYQDNGGDADLLRLNLSLDSQLYPQISGHKSRFAIRFMPLDTENGQVPERL DFELACC P0DSF4 YNFU_ECOLI Putative zinc-binding protein YnfU ynfU b4776 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 IDENTIFICATION INDUCTION K12 / MG1655 / ATCC 47076 Zn(2+) Might bind 1 zinc ion. Expressed equally in exponential and stationary phase in rich medium (at protein level). Encoded in the Qin prophage. Complete proteome Metal-binding Reference proteome Zinc MSERKNSKSRRNYLVKCSCPNCTQESEHSFSRVQKGALLICPHCNKVFQTNLKAVA P77735 Q2MC07 YAJO_ECOLI 1-deoxyxylulose-5-phosphate synthase YajO 1.1.-.- yajO b0419 JW0409 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 OVEREXPRESSION K12 / MG1655 / ATCC 47076 FUNCTION CATALYTIC ACTIVITY ACTIVITY REGULATION OVEREXPRESSION K12 / MG1655 / ATCC 47076 Catalyzes the conversion of ribulose 5-phosphate (Ru5P) to 1-deoxy-D-xylulose 5-phosphate (DXP), providing a direct route from pentoses to terpenes. May play a role in biosynthesis of DXP under conditions of thiamine starvation. AH2 + D-ribulose 5-phosphate = 1-deoxy-D-xylulose 5-phosphate + A + H2O NADH, NADPH or ATP do not increase activity. Overexpression supports cell viability in the absence of the essential dxs-encoded 1-deoxy-D-xylulose-5-phosphate synthase (PubMed:25326299). Overexpression confers resistance to the 4-amino-2-methyl 5-hydroxymethylpyrimidine (HMP) analogs bacimethrin and 4-amino-2-trifluoromethyl 5-hydroxymethylpyrimidine (CF(3)-HMP) (PubMed:15292217). Belongs to the aldo/keto reductase family. Aldo/keto reductase 2 subfamily. Translation N-terminally shortened. Complete proteome Oxidoreductase Reference proteome MQYNPLGKTDLRVSRLCLGCMTFGEPDRGNHAWTLPEESSRPIIKRALEGGINFFDTANS YSDGSSEEIVGRALRDFARREDVVVATKVFHRVGDLPEGLSRAQILRSIDDSLRRLGMDY VDILQIHRWDYNTPIEETLEALNDVVKAGKARYIGASSMHASQFAQALELQKQHGWAQFV SMQDHYNLIYREEEREMLPLCYQEGVAVIPWSPLARGRLTRPWGETTARLVSDEVGKNLY KESDENDAQIAERLTGVSEELGATRAQVALAWLLSKPGIAAPIIGTSREEQLDELLNAVD ITLKPEQIAELETPYKPHPVVGFK P0ADT5 P24196 Q2M9G2 YGIC_ECOLI Putative acid--amine ligase YgiC 6.3.1.- ygiC b3038 JW3006 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 LACK OF GLUTATHIONYLSPERMIDINE SYNTHETASE ACTIVITY FUNCTION ATP-BINDING DISRUPTION PHENOTYPE K12 May be a ligase forming an amide bond. Shows ATPase activity. Despite its similarity to the C-terminal synthetase domain of Gss, is not a glutathionylspermidine (Gsp) synthetase. Cannot synthesize Gsp, glutathione (GSH), or GSH intermediates, from GSH and spermidine, cysteine and glutamate, gamma-glutamylcysteine and spermidine, and gamma-glutamylcysteine and glycine. Does not bind to Gsp. Deletion of this gene does not affect the ability to synthesize glutathionylspermidine. There is no visible differences between wild-type and mutant strain growth in LB media. Belongs to the glutathionylspermidine synthase preATP-grasp family. ATP-binding Complete proteome Ligase Magnesium Metal-binding Nucleotide-binding Reference proteome MERVSITERPDWREKAHEYGFNFHTMYGEPYWCEDAYYKLTLAQVEKLEEVTAELHQMCL KVVEKVIASDELMTKFRIPKHTWSFVRQSWLTHQPSLYSRLDLAWDGTGEPKLLENNADT PTSLYEAAFFQWIWLEDQLNAGNLPEGSDQFNSLQEKLIDRFVELREQYGFQLLHLTCCR DTVEDRGTIQYLQDCATEAEIATEFLYIDDIGLGEKGQFTDLQDQVISNLFKLYPWEFML REMFSTKLEDAGVRWLEPAWKSIISNKALLPLLWEMFPNHPNLLPAYFAEDDHPQMEKYV VKPIFSREGANVSIIENGKTIEAAEGPYGEEGMIVQQFHPLPKFGDSYMLIGSWLVNDQP AGIGIREDRALITQDMSRFYPHIFVE P39295 Q2M6C0 YJFM_ECOLI Uncharacterized protein YjfM yjfM b4185 JW4143 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Complete proteome Reference proteome MARKRKSRNNSKIGHGAISRIGRPNNPFEPCRNRYAQKYLTLALMGGAAFFVLKGCSDSS DVDNDGDGTFYATVQDCIDDGNNADICARGWNNAKTAFYADVPKNMTQQNCQSKYENCYY DNVEQSWIPVVSGFLLSRVIRKDRDEPFVYNSGGSSFASRPVWRSTSGDYSWRSGSGKKE SYSSGGFTTKKASTVSRGGYGRSSSARGHWGG P46130 P75765 YBHC_ECOLI Putative acyl-CoA thioester hydrolase YbhC 3.1.2.- ybhC b0772 JW0755 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 33-427 K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-300 K12 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39 IDENTIFICATION IDENTIFICATION BY MASS SPECTROMETRY FUNCTION X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 29-427 ABSENCE OF PECTINASE ACTIVITY ABSENCE OF PECTIN BINDING ABSENCE OF ACYL COENZYME A ESTERASE ACTIVITY DISULFIDE BOND FUNCTION Putative thioesterase. Does not bind pectin, and has no pectinesterase activity. Cell outer membrane Lipid-anchor Belongs to the pectinesterase family. Lacks the conserved Asp residue in position 252 essential for pectinase activity. Likewise, most of the residues involved in substrate binding are not conserved. Was originally (PubMed:15808744) thought to have palmitoyl-CoA thioesterase activity, but PubMed:19452549 were unable to detect any pectinase or palmitoyl-CoA thioesterase activity. Its enzyme activity is therefore unsure. 3D-structure Aspartyl esterase Cell outer membrane Complete proteome Disulfide bond Hydrolase Lipoprotein Membrane Palmitate Reference proteome Signal N Q MNTFSVSRLALALAFGVTLTACSSTPPDQRPSDQTAPGTSSRPILSAKEAQNFDAQHYFA SLTPGAAAWNPSPITLPAQPDFVVGPAGTQGVTHTTIQAAVDAAIIKRTNKRQYIAVMPG EYQGTVYVPAAPGGITLYGTGEKPIDVKIGLSLDGGMSPADWRHDVNPRGKYMPGKPAWY MYDSCQSKRSDSIGVLCSAVFWSQNNGLQLQNLTIENTLGDSVDAGNHPAVALRTDGDQV QINNVNILGRQNTFFVTNSGVQNRLETNRQPRTLVTNSYIEGDVDIVSGRGAVVFDNTEF RVVNSRTQQEAYVFAPATLSNIYYGFLAVNSRFNAFGDGVAQLGRSLDVDANTNGQVVIR DSAINEGFNTAKPWADAVISNRPFAGNTGSVDDNDEIQRNLNDTNYNRMWEYNNRGVGSK VVAEAKK P0DPM5 A0A385XJA8 YABR_ECOLI Protein YabR yabR b4726 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 IDENTIFICATION INDUCTION Expressed at low levels in stationary phase (at protein level). Complete proteome Reference proteome MKRNDKILHYRGLN P0A8C1 P75819 YBJQ_ECOLI UPF0145 protein YbjQ ybjQ b0866 JW0850 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 P67910 hldD false 2 Belongs to the UPF0145 family. Complete proteome Reference proteome MQFSTTPTLEGQTIVEYCGVVTGEAILGANIFRDFFAGIRDIVGGRSGAYEKELRKAREI AFEELGSQARALGADAVVGIDIDYETVGQNGSMLMVSVSGTAVKTRR P75764 Q9R7S5 YBHJ_ECOLI Uncharacterized protein YbhJ ybhJ b0771 JW5103 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 [4Fe-4S] cluster Binds 1 [4Fe-4S] cluster per subunit. Belongs to the aconitase/IPM isomerase family. Complete proteome Iron Iron-sulfur Metal-binding Reference proteome MIKLSEKGVFLASNNEIIAEEHFTGEIKKEEAKKGTIAWSILSSHNTSGNMDKLKIKFDS LASHDITFVGIVQTAKASGMERFPLPYVLTNCHNSLCAVGGTINGDDHVFGLSAAQRYGG IFVPPHIAVIHQYMREMMAGGGKMILGSDSHTRYGALGTMAVGEGGGELVKQLLNDTWDI DYPGVVAVHLTGKPAPYVGPQDVALAIIGAVFKNGYVKNKVMEFVGPGVSALSTDFRNSV DVMTTETTCLSSVWQTDEEVHNWLALHGRGQDYCQLNPQPMAYYDGCISVDLSAIKPMIA LPFHPSNVYEIDTLNQNLTDILREIEIESERVAHGKAKLSLLDKVENGRLKVQQGIIAGC SGGNYENVIAAANALRGQSCGNDTFSLAVYPSSQPVFMDLAKKGVVADLIGAGAIIRTAF CGPCFGAGDTPINNGLSIRHTTRNFPNREGSKPANGQMSAVALMDARSIAATAANGGYLT SASELDCWDNVPEYAFDVTPYKNRVYQGFVKGATQQPLIYGPNIKDWPELGALTDNIVLK VCSKILDEVTTTDELIPSGETSSYRSNPIGLAEFTLSRRDPGYVSRSKATAELENQRLAG NVSELTEVFARIKQIAGQEHIDPLQTEIGSMVYAVKPGDGSAREQAASCQRVIGGLANIA EEYATKRYRSNVINWGMLPLQMAEVPTFEVGDYIYIPGIKAALDNPGTTFKGYVIHEDAP VTEITLYMESLTAEEREIIKAGSLINFNKNRQM P39393 P27301 P39392 Q6BEW7 YJIV_ECOLI Putative uncharacterized protein YjiV yjiV mcrD b4486 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] SEQUENCE REVISION K12 / MG1655 / ATCC 47076 SEQUENCE REVISION NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 624-906 K12 A portion of this ORF was originally annotated as mcrD, and reported to inhibit mcrE restriction. Could be the product of a pseudogene. Complete proteome Reference proteome MYVNQRQNCDCGSPVYEVAFCNDCNEPHLLARDKKGKLVQWENKGGDEFSLQDEVPVEHD ATEEKVEKENSFQPPLIIAAGETSEAGYTLQRLDRQTRRIGVINNDSIPLIINDIEQVCS ASGCGYRGMSGKQPFRRALLGGPFYVTNIVPTVLEYCQDFTSDEGKEGVGPDSLPGRGRR LITFTDSRQGTARMAVRMQQEAERSRLRGSVVEILSWHQRTQTSTAPNANADLEKLAARA KQAREQAEEYRSWGMPDQAKLSQAQAEQLEQAYQAATGGKAATILVSRTWTEMVNELKER ADIRGPVLQYNHYLKPEVFNENGGPLKLSEMLLFREFMRRPKRTNSLETQGLVQVGYQGL EKIHKSPLHWQEKGLTLDDWRDFLKVTLDHYVRESNFTQLDDELKNWIGSRFSSKFVRNP ESKDPEDNQNRRWPQIRNGNVSHRLAKLLMLGAGFKTVNAATIDIINTWLKEAWAQLTGP LAVLKPDGNRFYLPKEHMTFSLITDAWICPVTNKILDTAFKGLTPYLPTHISFEHLTLAQ YDTFVAQKVTMPEIWKLDRSQEDYAEGLAKARDWVSHDPLIAQLRSENVWTDINDRVVEG GFYYRTAEHSAQQSSERLQSYEKMFKNGQLNVLNCSTTMEMGVDTDRVMTLASRSQQATI PGPEWHLNDELVVRSLGYKTVELNEFILPAKATNAVERVKDIQIHKQLNGPLSQFGQRFW DVLFNDHEEAQSLMNNTRITGVHYTDRYLQNPVALALLGSILRPLKTKLTDGAEVTLDTL FKDKDRPGNRPFHDWMSIADFQDFADQWFAAALGRPVELTVFDSPRDIPHHRKLTVTFED GQVLKIRFDQGMGYWRINFSSQWHYFDFRDDVSFQLVKMAQACKEGNVANSEESWATDVL VEVIAS P29217 P75930 YCEH_ECOLI UPF0502 protein YceH G20.3 yceH b1067 JW1054 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 / MC4100 / ATCC 35695 / DSM 6574 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-133 K12 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-80 IDENTIFICATION BY MASS SPECTROMETRY K12 / JW1106 K12 / MG1655 / ATCC 47076 Belongs to the UPF0502 family. Acetylation Complete proteome Reference proteome V E A G MKYQLTALEARVIGCLLEKQVTTPEQYPLSVNGVVTACNQKTNREPVMNLSESEVQEQLD NLVKRHYLRTVSGFGNRVTKYEQRFCNSEFGDLKLSAAEVALITTLLLRGAQTPGELRSR AARMYEFSDMAEVESTLEQLANREDGPFVVRLAREPGKRENRYMHLFSGEVEDQPAVTDM SNAVDGDLQARVEALEIEVAELKQRLDSLLAHLGD P42598 Q2M9C0 YGJQ_ECOLI Uncharacterized protein YgjQ ygjQ b3086 JW3057 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Membrane Single-pass membrane protein To E.coli SanA. Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MLRAFARLLLRICFSRRTLKIACLLLLVAGATILIADRVMVNASKQLTWSDVNAVPARNV GLLLGARPGNRYFTRRIDTAAALYHAGKVKWLLVSGDNGRKNYDEASGMQQALIAKGVPA KVIFCDYAGFSTLDSVVRAKKVFGENHITIISQEFHNQRAIWLAKQYGIDAIGFNAPDLN MKHGFYTQLREKLARVSAVIDAKILHRQPKYLGPSVMIGPFSEHGCPAQK P0DP22 P39387 P39388 Q2M5X5 YJIQ_ECOLI Putative inactive recombination-promoting nuclease-like protein YjiQ yjiQ rpnD b4339 JW4302 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION K12 ERRATUM FUNCTION K12 This pseudogene is the C-terminal fragment of low activity DNA endonuclease RpnD which probably yields 3'-hydroxyl ends (By similarity). The intact protein can be seen in this entry (AC B7NGZ6). Expression of the repaired protein increases the frequency of recA-independent recombination, but also decreases viability probably via DNA damage; in a RecA strain expression has no effect on viability but does induce the SOS repair response (PubMed:26162088, PubMed:26618540). May play a role in horizontal gene transfer (PubMed:26162088, PubMed:26618540, PubMed:28096446). Belongs to the Rpn/YhgA-like nuclease family. Could be the product of a pseudogene. Experiments were performed with a repaired version of the protein (AC B7NGZ6) (PubMed:26162088). Complete proteome Reference proteome MLFYHGSRSPYPWSLCWLDEFADPTTARKLYNAAFPLVDVTVVPDDEIVQHRRVALLELI QKHIRQRDLMGLIDQLVVLLVTECANDSQITALLNYILLTGDEARFNEFISELTRRMPQH RERIMTIAERIHNDGYIKGEQRILRLLLQNGADPEWIQKITGLSAEQMQALRQPLPERER YSWLKS P39390 Q2M5X3 YJIS_ECOLI Uncharacterized protein YjiS yjiS b4341 JW4304 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Complete proteome Reference proteome MEFHENRAKAPFIGLVQLWQAVRRWRRQMQTRRVLQQMSDERLKDIGLRREDVE P0AAW5 P75773 YBHQ_ECOLI Inner membrane protein YbhQ ybhQ b0791 JW0774 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 TOPOLOGY [LARGE SCALE ANALYSIS] K12 / MG1655 / ATCC 47076 Cell inner membrane Multi-pass membrane protein Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MKWQQRVRVATGLSCWQIMLHLLVVALLVVGWMSKTLVHVGVGLCALYCVTVVMMLVFQR HPEQRWREVADVLEELTTTWYFGAALIVLWLLSRVLENNFLLAIAGLAILAGPAVVSLLA KDKKLHHLTSKHRVRR P76318 Q2MB05 YEDK_ECOLI SOS response-associated protein YedK 3.4.-.- yedK yedG b1931 JW1916 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] JA11 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 SEQUENCE REVISION NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 IDENTIFICATION ACTIVITY IN VITRO FUNCTION DNA-BINDING Sensor of abasic sites in single-stranded DNA (ssDNA) required to preserve genome integrity by promoting error-free repair of abasic sites (PubMed:30554877). Recognizes and binds abasic sites in ssDNA at replication forks and chemically modifies the lesion by forming a covalent cross-link with DNA (PubMed:30554877). May act as a protease: mediates autocatalytic processing of its N-terminal methionine in order to expose the catalytic cysteine (By similarity). Belongs to the SOS response-associated peptidase family. Was reported to act as an endonuclease that specifically cleaves 5-hydroxymethylcytosine (5hmC)-containing DNA in vitro (PubMed:29020633). Additional experiments are however required to confirm this activity as this protein is present in many organisms that do not utilize methylcytosine for epigenetic control. 3D-structure Complete proteome DNA damage DNA-binding Hydrolase Protease Reference proteome SOS response MCGRFAQSQTREDYLALLAEDIERDIPYDPEPIGRYNVAPGTKVLLLSERDEHLHLDPVF WGYAPGWWDKPPLINARVETAATSRMFKPLWQHGRAICFADGWFEWKKEGDKKQPFFIYR ADGQPIFMAAIGSTPFERGDEAEGFLIVTAAADQGLVDIHDRRPLVLSPEAAREWMRQEI SGKEASEIAASGCVPANQFSWHPVSRAVGNVKNQGAELIQPV P38035 Q2M786 RTCR_ECOLI Transcriptional regulatory protein RtcR rtcR yhgB b3422 JW3385 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 343-532 K12 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 346-532 K12 IDENTIFICATION IDENTIFICATION FUNCTION Transcriptional repressor of the rtcAB genes. Interacts with sigma-54. Translated as Leu. ATP-binding Complete proteome DNA-binding Nucleotide-binding Reference proteome Repressor Transcription Transcription regulation Two-component regulatory system MRKTVAFGFVGTVLDYAGRGSQRWSKWRPTLCLCQQESLVIDRLELLHDARSRSLFETLK RDIASVSPETEVVSVEIELHNPWDFEEVYACLHDFARGYEFQPEKEDYLIHITTGTHVAQ ICWFLLAEARYLPARLIQSSPPRKKEQPRGPGEVTIIDLDLSRYNAIASRFAEERQQTLD FLKSGIATRNPHFNRMIEQIEKVAIKSRAPILLNGPTGAGKSFLARRILELKQARHQFSG AFVEVNCATLRGDTAMSTLFGHVKGAFTGARESREGLLRSANGGMLFLDEIGELGADEQA MLLKAIEEKTFYPFGSDRQVSSDFQLIAGTVRDLRQLVAEGKFREDLYARINLWTFTLPG LRQRQEDIEPNLDYEVERHASLTGDSVRFNTEARRAWLAFATSPQATWRGNFRELSASVT RMATFATSGRITLDVVEDEINRLRYNWQESRPSALTALLGAEAENIDLFDRMQLEHVIAI CRQAKSLSAAGRQLFDVSRQGKASVNDADRLRKYLARFGLTWEAVQDQHSSS P37440 P76963 P77140 P77442 UCPA_ECOLI Oxidoreductase UcpA 1.-.-.- ucpA yfeF b2426 JW5394 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 180-263 K12 IDENTIFICATION P0A796 pfkA false 2 Belongs to the short-chain dehydrogenases/reductases (SDR) family. Complete proteome Oxidoreductase Reference proteome T Q MGKLTGKTALITGALQGIGEGIARTFARHGANLILLDISPEIEKLADELCGRGHRCTAVV ADVRDPASVAAAIKRAKEKEGRIDILVNNAGVCRLGSFLDMSDDDRDFHIDINIKGVWNV TKAVLPEMIARKDGRIVMMSSVTGDMVADPGETAYALTKAAIVGLTKSLAVEYAQSGIRV NAICPGYVRTPMAESIARQSNPEDPESVLTEMAKAIPMRRLADPLEVGELAAFLASDESS YLTGTQNVIDGGSTLPETVSVGI P75931 YCEM_ECOLI Putative oxidoreductase YceM 1.-.-.- yceM mviM b1068 JW1055 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 2-307 Belongs to the Gfo/Idh/MocA family. 3D-structure Complete proteome Oxidoreductase Reference proteome MKKLRIGVVGLGGIAQKAWLPVLAAASDWTLQGAWSPTRAKALPICESWRIPYADSLSSL AASCDAVFVHSSTASHFDVVSTLLNAGVHVCVDKPLAENLRDAERLVELAARKKLTLMVG FNRRFAPLYGELKTQLATAASLRMDKHRSNSVGPHDLYFTLLDDYLHVVDTALWLSGGKA SLDGGTLLTNDAGEMLFAEHHFSAGPLQITTCMHRRAGSQRETVQAVTDGALIDITDMRE WREERGQGVVHKPIPGWQSTLEQRGFVGCARHFIECVQNQTVPQTAGEQAVLAQRIVDKI WRDAMSE P0DP63 P39874 P77104 P77192 YBEH_ECOLI Putative protein YbeH ybeH b4581 JW0620 b0625 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52 K12 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 31-75 K12 / EMG2 Pseudogene resulting from a nucleotide deletion that introduces a premature stop codon at position 66. This is the N-terminal fragment. The intact protein (AC A0A140NCB4) hydrolyzes deaminated glutathione (dGSH, 2-oxoglutaramate) to alpha-ketoglutarate (alpha-KG) and cysteinylglycine, has less activity against alpha-ketoglutaramate (a-KGM) and no activity on glutathione or L-glutamine (By similarity). May function as a metabolite repair enzyme (By similarity). Belongs to the carbon-nitrogen hydrolase superfamily. NIT1/NIT2 family. Could be the product of a pseudogene. Translation N-terminally shortened. Complete proteome Reference proteome MLVAAGQFAVTSVWEKNAEICASLMAQAAENDASLFALPEALLARDDHDADLSVKSAQLL EGEFLGLYGEKVNVT P0AF56 P32713 Q2M6M6 YJCO_ECOLI Sel1-repeat-containing protein YjcO yjcO b4078 JW4039 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Complete proteome Reference proteome Repeat Signal MKKIIALMLFLTFFAHANDSEPGSQYLKAAEAGDRRAQYFLADSWFSSGDLSKAEYWAQK AADSGDADACALLAQIKITNPVSLDYPQAKVLAEKAAQAGSKEGEVTLAHILVNTQAGKP DYPKAISLLENASEDLENDSAVDAQMLLGLIYANGVGIKADDDKATWYFKRSSAISRTGY SEYWAGMMFLNGEEGFIEKNKQKALHWLNLSCMEGFDTGCEEFEKLTNG Q46796 Q2M9X7 YGEP_ECOLI Putative protein YgeP ygeP b2862 JW2831 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Could be the product of a pseudogene. Is missing N- and possibly C-terminal residues compared to orthologs. Complete proteome Reference proteome MTSGLERLSNLLSKKDSVFVSDLLREAKVNELDETLSTTRLNHLIDKGYERITLQLDLGG ESPGYLEKDKHYREADAALLNVIYPTNLSKINTRRKEQV P46853 Q2M7A3 YHHX_ECOLI Uncharacterized oxidoreductase YhhX 1.-.-.- yhhX b3440 JW3403 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 IDENTIFICATION BY MASS SPECTROMETRY B / BL21 Belongs to the Gfo/Idh/MocA family. Biliverdin reductase subfamily. 3D-structure Complete proteome Oxidoreductase Reference proteome MVINCAFIGFGKSTTRYHLPYVLNRKDSWHVAHIFRRHAKPEEQAPIYSHIHFTSDLDEV LNDPDVKLVVVCTHADSHFEYAKRALEAGKNVLVEKPFTPTLAQAKELFALAKSKGLTVT PYQNRRFDSCFLTAKKAIESGKLGEIVEVESHFDYYRPVAETKPGLPQDGAFYGLGVHTM DQIISLFGRPDHVAYDIRSLRNKANPDDTFEAQLFYGDLKAIVKTSHLVKIDYPKFIVHG KKGSFIKYGIDQQETSLKANIMPGEPGFAADDSVGVLEYVNDEGVTVREEMKPEMGDYGR VYDALYQTITHGAPNYVKESEVLTNLEILERGFEQASPSTVTLAK P0A8Y3 P32145 Q2M8I2 YIHX_ECOLI Alpha-D-glucose 1-phosphate phosphatase YihX Alpha-D-glucose-1-P phosphatase 3.1.3.10 Alpha-D-glucose-1-phosphatase Haloacid dehalogenase-like phosphatase 4 HAD4 yihX b3885 JW5566 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION AS A PHOSPHATASE FUNCTION CATALYTIC ACTIVITY BIOPHYSICOCHEMICAL PROPERTIES SUBSTRATE SPECIFICITY COFACTOR FUNCTION CATALYTIC ACTIVITY SUBSTRATE SPECIFICITY BIOPHYSICOCHEMICAL PROPERTIES BIOTECHNOLOGY X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE Catalyzes the dephosphorylation of alpha-D-glucose 1-phosphate (Glc1P) and, to a lesser extent, of other sugar phosphates (PubMed:16990279) (PubMed:25484615). Has no activity with the beta form of Glc1P. In addition, YihX has significant phosphatase activity against pyridoxal phosphate (PLP) and low beta-phosphoglucomutase activity (PubMed:16990279). alpha-D-glucose 1-phosphate + H2O = D-glucose + phosphate Mg(2+) Mn(2+) Co(2+) Zn(2+) Magnesium. Can also use other divalent metal cations such as manganese, cobalt or zinc. 0.028 mM for imido-di-P (with magnesium ions as cofactor and at pH 9) 0.24 mM for alpha-D-glucose-1-phosphate (with magnesium ions as cofactor and at pH 9) 1.6 mM for alpha-fructose-1-phosphate (with manganese ions as cofactor and at pH 9) 3.6 mM for acetyl-phosphate (with magnesium ions as cofactor and at pH 9) kcat is 10.2 sec(-1) with alpha-Glc-1-P as substrate. kcat is 1.26 sec(-1) with alpha-Man-1-P as substrate. kcat is 0.98 sec(-1) with alpha-Gal-1-P as substrate. kcat is 0.09 sec(-1) with Glc-6-P as substrate (at pH 7.0 and 37 degrees Celsius). Optimum pH is 5.0-7.0. Optimum temperature is 40 degrees Celsius. Is proposed to be a useful catalyst for hydrolytic transformation (e.g. removal) of alpha-Glc-1-P from complex substrate solutions containing multiple sugar phosphates. Belongs to the HAD-like hydrolase superfamily. YihX family. Translation N-terminally shortened. 3D-structure Complete proteome Hydrolase Magnesium Manganese Metal-binding Reference proteome MLYIFDLGNVIVDIDFNRVLGAWSDLTRIPLASLKKSFHMGEAFHQHERGEISDEAFAEA LCHEMALPLSYEQFSHGWQAVFVALRPEVIAIMHKLREQGHRVVVLSNTNRLHTTFWPEE YPEIRDAADHIYLSQDLGMRKPEARIYQHVLQAEGFSPSDTVFFDDNADNIEGANQLGIT SILVKDKTTIPDYFAKVLC P75838 Q9R2W0 YCAO_ECOLI Ribosomal protein S12 methylthiotransferase accessory factor YcaO ycaO b0905 JW0888 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 FUNCTION INTERACTION WITH RIBOSOME DISRUPTION PHENOTYPE K12 / W3110 / ATCC 27325 / DSM 5911 Involved in beta-methylthiolation of ribosomal protein S12. Interacts with the ribosomal small subunit. Mutant shows a decrease in the ratio of methylthiolated to unmodified S12 and a decrease in transcription of a subset of genes. 3D-structure Complete proteome Reference proteome MTQTFIPGKDAALEDSIARFQQKLSDLGFQIEEASWLNPVPNVWSVHIRDKECALCFTNG KGATKKAALASALGEYFERLSTNYFFADFWLGETIANGPFVHYPNEKWFPLTENDDVPEG LLDDRLRAFYDPENELTGSMLIDLQSGNEDRGICGLPFTRQSDNQTVYIPMNIIGNLYVS NGMSAGNTRNEARVQGLSEVFERYVKNRIIAESISLPEIPADVLARYPAVVEAIETLEAE GFPIFAYDGSLGGQYPVICVVLFNPANGTCFASFGAHPDFGVALERTVTELLQGRGLKDL DVFTPPTFDDEEVAEHTNLETHFIDSSGLISWDLFKQDADYPFVDWNFSGTTEEEFATLM AIFNKEDKEVYIADYEHLGVYACRIIVPGMSDIYPAEDLWLANNSMGSHLRETILSLPGS EWEKEDYLNLIEQLDEEGFDDFTRVRELLGLATGSDNGWYTLRIGELKAMLALAGGDLEQ ALVWTEWTMEFNSSVFSPERANYYRCLQTLLLLAQEEDRQPLQYLNAFVRMYGADAVEAA SAAMSGEAAFYGLQPVDSDLHAFAAHQSLLKAYEKLQRAKAAFWAK P46837 P76689 Q2M772 YHGF_ECOLI Protein YhgF yhgF b3407 JW3370 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 IDENTIFICATION BY MASS SPECTROMETRY B / BL21 Wrong choice of frame. Translation N-terminally extended. Complete proteome Reference proteome RNA-binding QP HA MMNDSFCRIIAGEIQARPEQVDAAVRLLDEGNTVPFIARYRKEITGGLDDTQLRNLETRL SYLRELEERRQAILKSISEQGKLTDDLAKAINATLSKTELEDLYLPYKPKRRTRGQIAIE AGLEPLADLLWSDPSHTPEVAAAQYVYADKGVADTKAALDGARYILMERFAEDAALLAKV RDYLWKNAHLVSTVVSGKEEEGAKFRDYFDHHEPLSTVPSHRALAMFRGRNEGVLQLSLN ADPQFDEPPKESYCEQIIMDHLGLRLNNAPADSWRKGVVSWTWRIKVLMHLETELMGTVR ERAEDEAINVFARNLHDLLMAAPAGLRATMGLDPGLRTGVKVAVVDATGKLVATDTIYPH TGQAAKAAMTVAALCEKHNVELVAIGNGTASRETERFYLDVQKQFPKVTAQKVIVSEAGA SVYSASELAAQEFPDLDVSLRGAVSIARRLQDPLAELVKIDPKSIGVGQYQHDVSQTQLA RKLDAVVEDCVNAVGVDLNTASVPLLTRVAGLTRMMAQNIVAWRDENGQFQNRQQLLKVS RLGPKAFEQCAGFLRINHGDNPLDASTVHPEAYPVVERILAATQQALKDLMGNSSELRNL KASDFTDEKFGVPTVTDIIKELEKPGRDPRPEFKTAQFADGVETMNDLQPGMILEGAVTN VTNFGAFVDIGVHQDGLVHISSLSNKFVEDPHTVVKAGDIVKVKVLEVDLQRKRIALTMR LDEQPGETNARRGGGNERPQNNRPAAKPRGREAQPAGNSAMMDALAAAMGKKR P0AB18 P45572 P75878 TUSE_ECOLI Sulfurtransferase TusE 2.8.1.- tRNA 2-thiouridine synthesizing protein E tusE yccK b0969 JW0952 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-55 IDENTIFICATION FUNCTION MUTAGENESIS OF CYS-108 SUBUNIT Part of a sulfur-relay system required for 2-thiolation of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at tRNA wobble positions. Could accept sulfur from TusD. Interacts with the TusBCD complex. Interacts with MnmA. Cytoplasm Belongs to the DsrC/TusE family. Complete proteome Cytoplasm Reference proteome Transferase tRNA processing C S MLIFEGKEIETDTEGYLKESSQWSEPLAVVIAENEGISLSPEHWEVVRFVRDFYLEFNTS PAIRMLVKAMANKFGEEKGNSRYLYRLFPKGPAKQATKIAGLPKPVKCI P76180 Q2MB71 YDGK_ECOLI Inner membrane protein YdgK ydgK b1626 JW1618 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 TOPOLOGY [LARGE SCALE ANALYSIS] K12 / MG1655 / ATCC 47076 Cell inner membrane Multi-pass membrane protein To Synechocystis PCC 6803 sll0481. Cell inner membrane Cell membrane Complete proteome Membrane Reference proteome Transmembrane Transmembrane helix MTTTTPQRIGGWLLGPLAWLLVALLSTTLALLLYTAALSSPQTFQTLGGQALTTQILWGV SFITAIALWYYTLWLTIAFFKRRRCVPKHYIIWLLISVLLAVKAFAFSPVEDGIAVRQLL FTLLATALIVPYFKRSSRVKATFVNP P22787 Q2M876 YIFB_ECOLI Uncharacterized protein YifB yifB b3765 JW3738 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 Belongs to the Mg-chelatase subunits D/I family. ComM subfamily. Complete proteome Reference proteome MSLSIVHTRAALGVNAPPITVEVHISKGLPGLTMVGLPETTVKEARDRVRSAIINSGYEY PAKKITINLAPADLPKEGGRYDLPIAIALLAASEQLTANKLDEYELVGELALTGALRGVP GAISSATEAIKSGRKIIVAKDNEDEVGLINGEGCLIADHLQAVCAFLEGKHALERPKPTD AVSRALQHDLSDVIGQEQGKRGLEITAAGGHNLLLIGPPGTGKTMLASRINGLLPDLSNE EALESAAILSLVNAESVQKQWRQRPFRSPHHSASLTAMVGGGAIPGPGEISLAHNGVLFL DELPEFERRTLDALREPIESGQIHLSRTRAKITYPARFQLVAAMNPSPTGHYQGNHNRCT PEQTLRYLNRLSGPFLDRFDLSLEIPLPPPGILSKTVVPGESSATVKQRVMAARERQFKR QNKLNAWLDSPEIRQFCKLESEDAMWLEGTLIHLGLSIRAWQRLLKVARTIADIDQSDII TRQHLQEAVSYRAIDRLLIHLQKLLT P0A8Z3 P08999 YBGC_ECOLI Acyl-CoA thioester hydrolase YbgC Acyl-CoA thioesterase 3.1.2.- ybgC b0736 JW0726 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-20 K12 / MG1655 / ATCC 47076 IDENTIFICATION BY MASS SPECTROMETRY B / BL21 ACYL-COA THIOESTERASE ACTIVITY FUNCTION IN PHOSPHOLIPID METABOLISM SUBCELLULAR LOCATION INTERACTION WITH ACP; PLSB AND PSSA K12 / W3110 / ATCC 27325 / DSM 5911 X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) Thioesterase that appears to be involved in phospholipid metabolism. Some specific acyl-ACPs could be physiological substrates. Displays acyl-CoA thioesterase activity on malonyl-CoA in vitro, catalyzing the hydrolysis of the thioester bond. Interacts with ACP, PlsB and PssA, forming altogether a complex at the inner membrane. P0A6A8 acpP false 7 O32591 espP true 2 P0ADZ0 rplW false 2 P10408 secA false 2 Cell inner membrane Peripheral membrane protein Cytoplasmic side Belongs to the 4-hydroxybenzoyl-CoA thioesterase family. 3D-structure Cell inner membrane Cell membrane Complete proteome Hydrolase Lipid metabolism Membrane Reference proteome MNTTLFRWPVRVYYEDTDAGGVVYHASYVAFYERARTEMLRHHHFSQQALMAERVAFVVR KMTVEYYAPARLDDMLEIQTEITSMRGTSLVFTQRIVNAENTLLNEAEVLVVCVDPLKMK PRALPKSIVAEFKQ P0DPN2 A0A385XJA2 YKID_ECOLI Protein YkiD ykiD b4732 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 IDENTIFICATION INDUCTION Expressed approximately equally in exponential and stationary phases (at protein level). Complete proteome Reference proteome MTQRPWSKLQRKTHNIAALKIIARRSE P0A8E7 P77482 Q2MC00 YAJQ_ECOLI UPF0234 protein YajQ yajQ b0426 JW5058 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 IDENTIFICATION BY MASS SPECTROMETRY B / BL21 SUBUNIT NUCLEOTIDE BINDING K12 Binds nucleotides, may bind tRNA. Monomer. P0A988 dnaN false 2 P0A9I5 napD false 4 Belongs to the UPF0234 family. Complete proteome Nucleotide-binding Reference proteome MPSFDIVSEVDLQEARNAVDNASREVESRFDFRNVEASFELNDASKTIKVLSESDFQVNQ LLDILRAKLLKRGIEGSSLDVPENIVHSGKTWFVEAKLKQGIESATQKKIVKMIKDSKLK VQAQIQGDEIRVTGKSRDDLQAVMAMVRGGDLGQPFQFKNFRD P76502 P77784 SIXA_ECOLI Phosphohistidine phosphatase SixA 3.1.3.- RX6 sixA yfcW b2340 JW2337 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 / MC4100 / ATCC 35695 / DSM 6574 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] SEQUENCE REVISION TO 80 K12 / W3110 / ATCC 27325 / DSM 5911 Exhibits phosphohistidine phosphatase activity towards the HPt domain of the ArcB sensor involved in the multistep His-Asp phosphorelay. Q2EES9 torI false 3 Belongs to the SixA phosphatase family. 3D-structure Complete proteome Hydrolase Protein phosphatase Reference proteome T K MQVFIMRHGDAALDAASDSVRPLTTNGCDESRLMANWLKGQKVEIERVLVSPFLRAEQTL EEVGDCLNLPSSAEVLPELTPCGDVGLVSAYLQALTNEGVASVLVISHLPLVGYLVAELC PGETPPMFTTSAIASVTLDESGNGTFNWQMSPCNLKMAKAI P06992 Q2MCG8 RSMA_ECOLI Ribosomal RNA small subunit methyltransferase A 2.1.1.182 16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase 16S rRNA dimethyladenosine transferase 16S rRNA dimethylase High level kasugamycin resistance protein KsgA Kasugamycin dimethyltransferase S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase rsmA ksgA b0051 JW0050 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] FUNCTION DISRUPTION PHENOTYPE NUCLEOTIDE SEQUENCE [GENOMIC DNA] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-62 K12 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-67 PROTEIN SEQUENCE OF 2-11 FUNCTION AS A DNA GLYCOSYLASE/AP LYASE IDENTIFICATION BY 2D-GEL SUPPRESSES AN ERA MUTANT PARTIALLY SUPPRESSES AN RSGA DISRUPTION MUTANT K12 FUNCTION DISRUPTION PHENOTYPE MUTAGENESIS OF GLU-66 X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 17-268 STRUCTURE BY ELECTRON MICROSCOPY (13.5 ANGSTROMS) OF 17-268 IN COMPLEX WITH THE 30S RIBOSOMAL SMALL SUBUNIT RNA-BINDING Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits. Has also a DNA glycosylase/AP lyase activity that removes C mispaired with oxidized T from DNA, and may play a role in protection of DNA against oxidative stress. adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = 4 H(+) + N(6)-dimethyladenosine(1518)/N(6)-dimethyladenosine(1519) in 16S rRNA + 4 S-adenosyl-L-homocysteine Cytoplasm Inactivation leads to kasugamycin resistance. Cells lacking this gene show cold-sensitivity phenotype, altered ribosome profiles, and small subunit rRNA-processing defects. When overexpressed partially suppresses the slow growth and decreased 70S ribosome phenotype of an rsgA knockout; RsgA may be involved in 30S ribosomal subunit biogenesis. Upon overexpression also restores cold-sensitive growth of a missense mutation in Era. Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family. RsmA subfamily. 3D-structure Antibiotic resistance Complete proteome Cytoplasm Direct protein sequencing Methyltransferase Reference proteome RNA-binding rRNA processing S-adenosyl-L-methionine Transferase E A MNNRVHQGHLARKRFGQNFLNDQFVIDSIVSAINPQKGQAMVEIGPGLAALTEPVGERLD QLTVIELDRDLAARLQTHPFLGPKLTIYQQDAMTFNFGELAEKMGQPLRVFGNLPYNIST PLMFHLFSYTDAIADMHFMLQKEVVNRLVAGPNSKAYGRLSVMAQYYCNVIPVLEVPPSA FTPPPKVDSAVVRLVPHATMPHPVKDVRVLSRITTEAFNQRRKTIRNSLGNLFSVEVLTG MGIDPAMRAENISVAQYCQMANYLAENAPLQES P0A8M0 P17242 SYN_ECOLI Asparagine--tRNA ligase 6.1.1.22 Asparaginyl-tRNA synthetase AsnRS asnS tss b0930 JW0913 Escherichia coli (strain K12) Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia NUCLEOTIDE SEQUENCE [GENOMIC DNA] PROTEIN SEQUENCE OF 2-12 AND 243-256 CE1215 NUCLEOTIDE SEQUENCE [GENOMIC DNA] K12 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / MG1655 / ATCC 47076 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] K12 / W3110 / ATCC 27325 / DSM 5911 PROTEIN SEQUENCE OF 2-13 K12 / EMG2 ATP-BINDING SITE MUTANT TEMPERATURE-SENSITIVE HO202 IDENTIFICATION BY 2D-GEL ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + H(+) + L-asparaginyl-tRNA(Asn) Homodimer. Cytoplasm Belongs to the class-II aminoacyl-tRNA synthetase family.