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Database: UniProt
Entry: A0A0M1J8G7_9GAMM
LinkDB: A0A0M1J8G7_9GAMM
Original site: A0A0M1J8G7_9GAMM 
ID   A0A0M1J8G7_9GAMM        Unreviewed;       287 AA.
AC   A0A0M1J8G7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Ion-translocating oxidoreductase complex subunit B {ECO:0000256|HAMAP-Rule:MF_00463};
DE            EC=7.-.-.- {ECO:0000256|HAMAP-Rule:MF_00463};
DE   AltName: Full=Rnf electron transport complex subunit B {ECO:0000256|HAMAP-Rule:MF_00463};
GN   Name=rnfB {ECO:0000256|HAMAP-Rule:MF_00463};
GN   ORFNames=TI03_03055 {ECO:0000313|EMBL:KOR29147.1};
OS   Achromatium sp. WMS1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Thiotrichaceae; Achromatium.
OX   NCBI_TaxID=1604834 {ECO:0000313|EMBL:KOR29147.1, ECO:0000313|Proteomes:UP000036736};
RN   [1] {ECO:0000313|EMBL:KOR29147.1, ECO:0000313|Proteomes:UP000036736}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WMS1 {ECO:0000313|EMBL:KOR29147.1};
RX   PubMed=26322031; DOI=10.3389/fmicb.2015.00822;
RA   Mansor M., Hamilton T.L., Fantle M.S., Macalady J.L.;
RT   "Metabolic diversity and ecological niches of Achromatium populations
RT   revealed with single-cell genomic sequencing.";
RL   Front. Microbiol. 6:822-822(2015).
CC   -!- FUNCTION: Part of a membrane-bound complex that couples electron
CC       transfer with translocation of ions across the membrane.
CC       {ECO:0000256|HAMAP-Rule:MF_00463}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00463};
CC       Note=Binds 3 [4Fe-4S] clusters. {ECO:0000256|HAMAP-Rule:MF_00463};
CC   -!- SUBUNIT: The complex is composed of six subunits: RnfA, RnfB, RnfC,
CC       RnfD, RnfE and RnfG. {ECO:0000256|HAMAP-Rule:MF_00463}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00463}.
CC   -!- SIMILARITY: Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfB
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00463}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00463}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KOR29147.1}.
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DR   EMBL; JXSM01000120; KOR29147.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M1J8G7; -.
DR   PATRIC; fig|1604834.3.peg.177; -.
DR   Proteomes; UP000036736; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.20; -; 1.
DR   Gene3D; 1.10.15.40; Electron transport complex subunit B, putative Fe-S cluster; 1.
DR   HAMAP; MF_00463; RsxB_RnfB; 1.
DR   InterPro; IPR007202; 4Fe-4S_dom.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR010207; Elect_transpt_cplx_RnfB/RsxB.
DR   PANTHER; PTHR43560; ION-TRANSLOCATING OXIDOREDUCTASE COMPLEX SUBUNIT B; 1.
DR   PANTHER; PTHR43560:SF1; ION-TRANSLOCATING OXIDOREDUCTASE COMPLEX SUBUNIT B; 1.
DR   Pfam; PF12837; Fer4_6; 1.
DR   Pfam; PF04060; FeS; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 2.
DR   PROSITE; PS51656; 4FE4S; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_00463};
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00463};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00463};
KW   Electron transport {ECO:0000256|HAMAP-Rule:MF_00463};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00463};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW   Rule:MF_00463};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00463, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00463}; Reference proteome {ECO:0000313|Proteomes:UP000036736};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_00463};
KW   Translocase {ECO:0000256|HAMAP-Rule:MF_00463};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_00463}.
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          32..91
FT                   /note="4Fe-4S"
FT                   /evidence="ECO:0000259|PROSITE:PS51656"
FT   DOMAIN          162..191
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   REGION          1..26
FT                   /note="Hydrophobic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00463"
FT   BINDING         49
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00463"
FT   BINDING         52
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00463"
FT   BINDING         57
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00463"
FT   BINDING         74
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00463"
FT   BINDING         137
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00463"
FT   BINDING         141
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00463"
FT   BINDING         147
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00463"
FT   BINDING         151
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00463"
FT   BINDING         171
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00463"
FT   BINDING         174
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00463"
FT   BINDING         177
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00463"
FT   BINDING         181
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00463"
SQ   SEQUENCE   287 AA;  30522 MW;  F0E66EA5DE084C8D CRC64;
     MYTITTAVAF MAIFGIILSL ILVAANKKLL VYEDPRIDTV EELLPHANCG ACGTAGCRVF
     AELLVKGQKK PAECTVNSKE MGLAIANYLG VSLGSTEKRV ARLACAGGSH VALIHAHYAG
     LTTCRAATLI SGGGKACAWG CLGLGDCETA CEFGAITMNR YNLPQVDASA CTACGDCVTI
     CPKNLFEIHP LSHRLWVACK NQEFGAVAEQ WCEVACTACE RCAMDAPEGL IQIKNNLATI
     DYAKNALASP IAIQRCPTGA IVWQDDQQIQ KGQNAKKVIR KEALPVT
//
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