HMC5_DESVH
ID HMC5_DESVH Reviewed; 226 AA.
AC P33392;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Protein DVU_0532;
DE AltName: Full=HMC operon ORF 5;
GN OrderedLocusNames=DVU_0532;
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 -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
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DR EMBL; L16784; AAA71998.1; -; Unassigned_DNA.
DR EMBL; AE017285; AAS95014.1; -; Genomic_DNA.
DR PIR; E40605; E40605.
DR RefSeq; WP_010937838.1; NZ_CABHLV010000001.1.
DR RefSeq; YP_009755.1; NC_002937.3.
DR AlphaFoldDB; P33392; -.
DR STRING; 882.DVU_0532; -.
DR PaxDb; P33392; -.
DR EnsemblBacteria; AAS95014; AAS95014; DVU_0532.
DR KEGG; dvu:DVU_0532; -.
DR PATRIC; fig|882.5.peg.508; -.
DR eggNOG; COG2181; Bacteria.
DR HOGENOM; CLU_107083_0_0_7; -.
DR OMA; GIKRGGM; -.
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.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR036197; NarG-like_sf.
DR SUPFAM; SSF103501; SSF103501; 1.
PE 4: Predicted;
KW Cell membrane; Heme; Iron; Membrane; Metal-binding; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..226
FT /note="Protein DVU_0532"
FT /id="PRO_0000084005"
FT TRANSMEM 1..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..164
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..222
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 226 AA; 25275 MW; A4C8C9270001C507 CRC64;
MYAFLTGPML WASLLVFFGG LLARVIWYIR GLDWRLDRVA YKPHLAIGLQ GAVQSALKWL
VPFGTYSWRQ QPFFTVAFFL FHIGAVLVPL FLAGHNVILE ERFGFSLPAL PMGVADTLTV
LAIIGLVMIA LRRIALTEVR ILTTGYDWFI LAVSAAPFVT GFLARLHVGD YDTWLLAHII
TGELFLIVAP FTKLSHIVLF FMSRGQLGMD YAIKRGGATR GPAFPW
