HMC2_DESVH
ID HMC2_DESVH Reviewed; 370 AA.
AC P33389;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Protein DVU_0535;
DE AltName: Full=HMC operon ORF 2;
GN OrderedLocusNames=DVU_0535;
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. ORF2 is a
CC transmembrane redox protein.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein.
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DR EMBL; L16784; AAA71995.1; -; Genomic_DNA.
DR EMBL; AE017285; AAS95017.1; -; Genomic_DNA.
DR PIR; B40605; B40605.
DR RefSeq; WP_010937841.1; NZ_CABHLV010000001.1.
DR RefSeq; YP_009758.1; NC_002937.3.
DR AlphaFoldDB; P33389; -.
DR SMR; P33389; -.
DR STRING; 882.DVU_0535; -.
DR PaxDb; P33389; -.
DR EnsemblBacteria; AAS95017; AAS95017; DVU_0535.
DR KEGG; dvu:DVU_0535; -.
DR PATRIC; fig|882.5.peg.511; -.
DR eggNOG; COG0437; Bacteria.
DR eggNOG; COG3064; Bacteria.
DR HOGENOM; CLU_043374_0_0_7; -.
DR OMA; PKYDYDN; -.
DR PhylomeDB; P33389; -.
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:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR006311; TAT_signal.
DR Pfam; PF13247; Fer4_11; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 3.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW 4Fe-4S; Cell membrane; Electron transport; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..370
FT /note="Protein DVU_0535"
FT /id="PRO_0000159255"
FT TOPO_DOM 1..258
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 285..370
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 40..70
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 101..132
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 133..162
FT /note="4Fe-4S ferredoxin-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT REGION 345..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 49
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 55
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 148
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 187
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT CONFLICT 46
FT /note="T -> S (in Ref. 1; AAA71995)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 370 AA; 40072 MW; C63140DA1A472615 CRC64;
MDRRRFLTLL GSAGLTATVA TAGTAKAAST GTFPGYKDSY GVLHDTTRCI GCRKCEQACN
EVNKLPAPKA KFDDLTVLEK TRRTDADSWT VVNRYNAAGL DHPVFRKQQC NHCLEPACAS
ACFVKAFTKN PDGSVTYDGS LCVGCRYCMV ACPFNVPAFQ YAEAFDPLIQ KCTMCHPRLA
EGKLPGCVEI CPKEALTFGR RKDLVRIAHD RIRQNPGRYI DHVYGEQEMG GTAWMYLSGV
PFSATGMNEE LGTKSAPEYT AGALGAVPMV VGIWPILLTG AYAITKRKEK IAAEEQAEAV
KQAVAASRAE ADDKLKAALA KADKDKEAAV TREVKKAVDE ARKTFEEELA AKEQPEAPEG
DDAGKPGEDA