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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
 
 
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