ID YDEP_ECOLI Reviewed; 759 AA.
AC P77561; P78160;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 27-MAR-2024, entry version 158.
DE RecName: Full=Protein YdeP;
GN Name=ydeP; OrderedLocusNames=b1501, JW1495;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, AND INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=12399493; DOI=10.1128/jb.184.22.6225-6234.2002;
RA Masuda N., Church G.M.;
RT "Escherichia coli gene expression responsive to levels of the response
RT regulator EvgA.";
RL J. Bacteriol. 184:6225-6234(2002).
RN [5]
RP FUNCTION, AND INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=12694615; DOI=10.1046/j.1365-2958.2003.03477.x;
RA Masuda N., Church G.M.;
RT "Regulatory network of acid resistance genes in Escherichia coli.";
RL Mol. Microbiol. 48:699-712(2003).
CC -!- FUNCTION: Probably involved in acid resistance.
CC {ECO:0000269|PubMed:12399493, ECO:0000269|PubMed:12694615}.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000250};
CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC bis-MGD) cofactor per subunit. {ECO:0000250};
CC -!- INDUCTION: By EvgA. {ECO:0000269|PubMed:12399493,
CC ECO:0000269|PubMed:12694615}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; U00096; AAC74574.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15174.1; -; Genomic_DNA.
DR PIR; H64903; H64903.
DR RefSeq; NP_416018.1; NC_000913.3.
DR RefSeq; WP_000726691.1; NZ_SSZK01000001.1.
DR AlphaFoldDB; P77561; -.
DR SMR; P77561; -.
DR BioGRID; 4260213; 9.
DR BioGRID; 850416; 1.
DR DIP; DIP-28057N; -.
DR IntAct; P77561; 11.
DR STRING; 511145.b1501; -.
DR PaxDb; 511145-b1501; -.
DR EnsemblBacteria; AAC74574; AAC74574; b1501.
DR GeneID; 946055; -.
DR KEGG; ecj:JW1495; -.
DR KEGG; eco:b1501; -.
DR PATRIC; fig|1411691.4.peg.765; -.
DR EchoBASE; EB3559; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_16_1_6; -.
DR InParanoid; P77561; -.
DR OMA; TFNPVRE; -.
DR OrthoDB; 5287431at2; -.
DR PhylomeDB; P77561; -.
DR BioCyc; EcoCyc:G6791-MONOMER; -.
DR PRO; PR:P77561; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0010447; P:response to acidic pH; IMP:EcoCyc.
DR CDD; cd02787; MopB_CT_ydeP; 1.
DR CDD; cd02767; MopB_ydeP; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR037951; MopB_CT_YdeP.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR010046; Mopterin_OxRdtse_a_bac.
DR InterPro; IPR041953; YdeP_MopB.
DR NCBIfam; TIGR01701; Fdhalpha-like; 1.
DR PANTHER; PTHR43105:SF4; PROTEIN YDEP; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR PIRSF; PIRSF000144; CbbBc; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
PE 2: Evidence at transcript level;
KW 4Fe-4S; Iron; Iron-sulfur; Metal-binding; Molybdenum; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..759
FT /note="Protein YdeP"
FT /id="PRO_0000063227"
FT BINDING 49
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
SQ SEQUENCE 759 AA; 83495 MW; 4DE7C14068FB66DD CRC64;
MKKKIESYQG AAGGWGAVKS VANAVRKQMD IRQDVIAMFD MNKPEGFDCP GCAWPDPKHS
ASFDICENGA KAIAWEVTDK QVNASFFAEN TVQSLLTWGD HELEAAGRLT QPLKYDAVSD
CYKPLSWQQA FDEIGARLQS YSDPNQVEFY TSGRTSNEAA FLYQLFAREY GSNNFPDCSN
MCHEPTSVGL AASIGVGKGT VLLEDFEKCD LVICIGHNPG TNHPRMLTSL RALVKRGAKM
IAINPLQERG LERFTAPQNP FEMLTNSETQ LASAYYNVRI GGDMALLKGM MRLLIERDDA
ASAAGRPSLL DDEFIQTHTV GFDELRRDVL NSEWKDIERI SGLSQTQIAE LADAYAAAER
TIICYGMGIT QHEHGTQNVQ QLVNLLLMKG NIGKPGAGIC PLRGHSNVQG DRTVGITEKP
SAEFLARLGE RYGFTPPHAP GHAAIASMQA ICTGQARALI CMGGNFALAM PDREASAVPL
TQLDLAVHVA TKLNRSHLLT ARHSYILPVL GRSEIDMQKN GAQAVTVEDS MSMIHASRGV
LKPAGVMLKS ECAVVAGIAQ AALPQSVVAW EYLVEDYDRI RNDIEAVLPE FADYNQRIRH
PGGFHLINAA AERRWMTPSG KANFITSKGL LEDPSSAFNS KLVMATVRSH DQYNTTIYGM
DDRYRGVFGQ RDVVFMSAKQ AKICRVKNGE RVNLIALTPD GKRSSRRMDR LKVVIYPMAD
RSLVTYFPES NHMLTLDNHD PLSGIPGYKS IPVELEPSN
//
