ID   YDEP_ECO57              Reviewed;         759 AA.
AC   Q8XAX1; Q7AE09;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 3.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Protein YdeP;
GN   Name=ydeP; OrderedLocusNames=Z2207, ECs2106;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Probably involved in acid resistance. {ECO:0000250}.
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:0000250}.
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000305}.
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DR   EMBL; AE005174; AAG56267.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB35529.1; -; Genomic_DNA.
DR   PIR; B90892; B90892.
DR   PIR; G85725; G85725.
DR   RefSeq; NP_310133.1; NC_002695.1.
DR   RefSeq; WP_000726734.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; Q8XAX1; -.
DR   SMR; Q8XAX1; -.
DR   STRING; 155864.EDL933_2138; -.
DR   EnsemblBacteria; AAG56267; AAG56267; Z2207.
DR   EnsemblBacteria; BAB35529; BAB35529; ECs_2106.
DR   GeneID; 917305; -.
DR   KEGG; ece:Z2207; -.
DR   KEGG; ecs:ECs_2106; -.
DR   PATRIC; fig|386585.9.peg.2212; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_000422_16_1_6; -.
DR   OMA; PRSLKCH; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   CDD; cd02787; MopB_CT_ydeP; 1.
DR   CDD; cd02767; MopB_ydeP; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR037951; MopB_CT_YdeP.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   InterPro; IPR010046; Mopterin_OxRdtse_a_bac.
DR   InterPro; IPR041953; YdeP_MopB.
DR   PANTHER; PTHR43105:SF4; PTHR43105:SF4; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   SUPFAM; SSF50692; SSF50692; 1.
DR   TIGRFAMs; TIGR01701; Fdhalpha-like; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Iron; Iron-sulfur; Metal-binding; Molybdenum; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..759
FT                   /note="Protein YdeP"
FT                   /id="PRO_0000063229"
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;  83553 MW;  CCE56EC47AF01058 CRC64;
     MKKKIESYQG AAGGWGAVKS VANAVRKQMD IRQDVIAMFD MNKPEGFDCP GCAWPDPKHS
     ASFDICENGA KAIAWEVTDK QVNASFFAQN 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
     SVEFLARLGE RYGFTPPHVP GHAAIASMQA ICTGQARALI CMGGNFALAM PDREASAVPL
     TQLDLAVHVA TKLNRSHLLT ARHSYILPVL GRSEIDMQKS GAQAVTVEDS MSMIHASRGV
     LKPAGVMLKS ECAVVAGIAQ ATLPQSVVAW EYLVEDYDRI RNDIEAVLPE FADYNQRIRH
     PGGFHLINAA AERRWMTPSG KANFITSKGL LEDPSSAFNS KLVMATVRSH DQYNTTIYGM
     DDRYRGVFGQ RDVVFMSAKQ AKICRVKNGE RVNLIALTPD GKRSSRRMDR LKVVIYPMAD
     RSLVTYFPES NHMLTLDNHD PLSGIPGYKS IPVELEPSN