ID   HMC4_DESVH              Reviewed;          47 AA.
AC   P33391;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Protein DVU_0533;
DE   AltName: Full=HMC operon ORF 4;
GN   OrderedLocusNames=DVU_0533;
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), ORF2, ORF3, ORF4,
CC       ORF5 and ORF6 in the HMC operon form a transmembrane protein complex
CC       that allows electron flow from the periplasmic hydrogenase to the
CC       cytoplasmic enzymes that catalyze reduction of sulfates.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein.
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DR   EMBL; L16784; AAA71997.1; -; Unassigned_DNA.
DR   EMBL; AE017285; AAS95015.1; -; Genomic_DNA.
DR   PIR; D40605; D40605.
DR   RefSeq; WP_010937839.1; NZ_CABHLV010000001.1.
DR   RefSeq; YP_009756.1; NC_002937.3.
DR   AlphaFoldDB; P33391; -.
DR   SMR; P33391; -.
DR   STRING; 882.DVU_0533; -.
DR   PaxDb; P33391; -.
DR   EnsemblBacteria; AAS95015; AAS95015; DVU_0533.
DR   KEGG; dvu:DVU_0533; -.
DR   PATRIC; fig|882.5.peg.509; -.
DR   eggNOG; ENOG503189B; Bacteria.
DR   HOGENOM; CLU_213739_0_0_7; -.
DR   Proteomes; UP000002194; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
PE   4: Predicted;
KW   Cell membrane; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..47
FT                   /note="Protein DVU_0533"
FT                   /id="PRO_0000084004"
FT   TRANSMEM        18..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   47 AA;  5773 MW;  30D4C1585B3C7209 CRC64;
     MDQAIYTLHE FMLHTKNWTY ILMGVTLLVY VGYWLFLTGR DEKIRKY