ID   HMC6_DESVH              Reviewed;         461 AA.
AC   P33393;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Protein DVU_0531;
DE   AltName: Full=HMC operon ORF 6;
GN   OrderedLocusNames=DVU_0531;
OS   Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS   B-1760 / Hildenborough).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8335628; DOI=10.1128/jb.175.15.4699-4711.1993;
RA   Rossi M., Pollock W.B.R., Reij M.W., Keon R.G., Fu R., Voordouw G.;
RT   "The hmc operon of Desulfovibrio vulgaris subsp. vulgaris Hildenborough
RT   encodes a potential transmembrane redox protein complex.";
RL   J. Bacteriol. 175:4699-4711(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX   PubMed=15077118; DOI=10.1038/nbt959;
RA   Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA   Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA   Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA   Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA   Wall J.D., Voordouw G., Fraser C.M.;
RT   "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT   Desulfovibrio vulgaris Hildenborough.";
RL   Nat. Biotechnol. 22:554-559(2004).
CC   -!- FUNCTION: HMWC (high-molecular-weight cytochrome c precursor), ORF2,
CC       ORF3, ORF4, ORF5, ORF6 in the HMC operon form a transmembrane protein
CC       complex that allows electron flow from the periplasmic hydrogenase to
CC       the cytoplasmic enzymes that catalyze reduction of sulfates. ORF6 is a
CC       redox protein.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L16784; AAA71999.1; -; Unassigned_DNA.
DR   EMBL; AE017285; AAS95013.1; -; Genomic_DNA.
DR   PIR; F40605; F40605.
DR   RefSeq; WP_010937837.1; NZ_CABHLV010000001.1.
DR   RefSeq; YP_009754.1; NC_002937.3.
DR   AlphaFoldDB; P33393; -.
DR   STRING; 882.DVU_0531; -.
DR   PaxDb; P33393; -.
DR   EnsemblBacteria; AAS95013; AAS95013; DVU_0531.
DR   KEGG; dvu:DVU_0531; -.
DR   PATRIC; fig|882.5.peg.507; -.
DR   eggNOG; COG0247; Bacteria.
DR   HOGENOM; CLU_023081_6_0_7; -.
DR   OMA; MFAGDWE; -.
DR   PhylomeDB; P33393; -.
DR   Proteomes; UP000002194; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1060.10; -; 1.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR004017; Cys_rich_dom.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   Pfam; PF02754; CCG; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
PE   4: Predicted;
KW   4Fe-4S; Cytoplasm; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW   Reference proteome; Repeat; Transport.
FT   CHAIN           1..461
FT                   /note="Protein DVU_0531"
FT                   /id="PRO_0000159256"
FT   DOMAIN          54..84
FT                   /note="4Fe-4S ferredoxin-type 1"
FT   DOMAIN          112..140
FT                   /note="4Fe-4S ferredoxin-type 2"
FT   BINDING         63
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         66
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         69
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         73
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         121
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         123
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         124
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         127
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   461 AA;  52730 MW;  21EC00F1984D0A7C CRC64;
     MPEGKFCNRK PVNTEEDLKA LLGDKGGAQY YKEMEELEVD QEALWANIEK TCQSRTKTWL
     EICAHCGMCA DSCFLYRVND RDPKQVPAYK IQSTLGEIIR RKGKVDTQFM LHAMEVAWSQ
     CTCCNRCGQY CPHGIDMGVM FSYLRGLLYS QGFVPWELKI GSGMHRVYGA QMDVTTEDWV
     ETCEWMAEEQ QEEWPGLEIP VDVENADIMY VLNAREPKHY PEDVAEAAIL FHIAGENWTV
     PSEGWEQTSL AMFAGDWAAC KMQVERVYAA IERLKPKCVV GTECGHAHRA SAIEGPYWAG
     YEDGKTPAPW LHYVEWVAMA LRTGKIKIDP EKRIKEPVTL QDSCNYIRNH GLAKCTREIM
     SYIADDFREM TPNREHNYCC GGGGGFNGIG KFRKQRNKAL QTKRDQILAT GAKLVVAPCH
     NCWDAIRDLE EEYRIGIRWS FLKPLIIKMA IIPEHLRPEE E