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Database: UniProt
Entry: A0A133YVR0_9FIRM
LinkDB: A0A133YVR0_9FIRM
Original site: A0A133YVR0_9FIRM 
ID   A0A133YVR0_9FIRM        Unreviewed;       283 AA.
AC   A0A133YVR0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
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=HMPREF3188_00550 {ECO:0000313|EMBL:KXB47282.1};
OS   Tissierellia bacterium KA00581.
OC   Bacteria; Bacillota; Tissierellia.
OX   NCBI_TaxID=1588751 {ECO:0000313|EMBL:KXB47282.1, ECO:0000313|Proteomes:UP000070503};
RN   [1] {ECO:0000313|EMBL:KXB47282.1, ECO:0000313|Proteomes:UP000070503}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KA00581 {ECO:0000313|EMBL:KXB47282.1,
RC   ECO:0000313|Proteomes:UP000070503};
RA   Oliw E.H.;
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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 membrane {ECO:0000256|HAMAP-Rule:MF_00463}.
CC   -!- SIMILARITY: Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfB
CC       subfamily. {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:KXB47282.1}.
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DR   EMBL; LSCW01000036; KXB47282.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A133YVR0; -.
DR   STRING; 1588751.HMPREF3188_00550; -.
DR   PATRIC; fig|1588751.3.peg.544; -.
DR   Proteomes; UP000070503; 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; -; 2.
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   NCBIfam; TIGR01944; rnfB; 1.
DR   PANTHER; PTHR43560; ION-TRANSLOCATING OXIDOREDUCTASE COMPLEX SUBUNIT B; 1.
DR   PANTHER; PTHR43560:SF1; ION-TRANSLOCATING OXIDOREDUCTASE COMPLEX SUBUNIT B; 1.
DR   Pfam; PF13370; Fer4_13; 1.
DR   Pfam; PF13187; Fer4_9; 1.
DR   Pfam; PF04060; FeS; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 2.
DR   PROSITE; PS51656; 4FE4S; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, 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}; Membrane {ECO:0000256|HAMAP-Rule:MF_00463};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00463}; Reference proteome {ECO:0000313|Proteomes:UP000070503};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_00463};
KW   Translocase {ECO:0000256|HAMAP-Rule:MF_00463};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_00463}.
FT   DOMAIN          38..97
FT                   /note="4Fe-4S"
FT                   /evidence="ECO:0000259|PROSITE:PS51656"
FT   DOMAIN          147..166
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          167..196
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   REGION          1..32
FT                   /note="Hydrophobic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00463"
FT   BINDING         55
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         58
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         63
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         80
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         143
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         150
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         153
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         157
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         176
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         179
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         182
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         186
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   283 AA;  30093 MW;  DDB066DD4A90DFAF CRC64;
     MFRGDIMSSI VVAVLVLSIL GILFALILGL ASKVFFVKVD EKILKVREQM PGANCGACGF
     PGCDGLAKAI AEGKAEVTAC PVGGADLAAR LAKILGLEAG EVEKMVACVM CQGDKDFAKE
     KYIYTGIRDC RVNNSMQGGS KTCAYGCLGC GTCRDVCPFD AIDMVNGIPV VNKDKCTACR
     KCIEICPKDL IDLVPYAQTV MVKCKSFAAG NIVKNACQVG CIGCKMCQRV YPEAFVIENN
     LAKVNYAQGL DEDLLLQAAD KCPTNAIFPG LARKMAEKVN NVA
//
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