ID G8UMS6_TANFA Unreviewed; 301 AA.
AC G8UMS6;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
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 ECO:0000313|EMBL:AEW22120.1};
GN OrderedLocusNames=BFO_2758 {ECO:0000313|EMBL:AEW22120.1};
OS Tannerella forsythia (strain ATCC 43037 / JCM 10827 / CCUG 21028 A / KCTC
OS 5666 / FDC 338) (Bacteroides forsythus).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Tannerella.
OX NCBI_TaxID=203275 {ECO:0000313|EMBL:AEW22120.1, ECO:0000313|Proteomes:UP000005436};
RN [1] {ECO:0000313|Proteomes:UP000005436}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43037 / JCM 10827 / CCUG 33226 / KCTC 5666 / FDC 338
RC {ECO:0000313|Proteomes:UP000005436};
RA Dewhirst F., Tanner A., Izard J., Brinkac L., Durkin A.S., Hostetler J.,
RA Shetty J., Torralba M., Gill S., Nelson K.;
RT "Complete sequence of Tannerella forsythia ATCC 43037.";
RL Submitted (DEC-2011) 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 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003191; AEW22120.1; -; Genomic_DNA.
DR AlphaFoldDB; G8UMS6; -.
DR STRING; 203275.BFO_2758; -.
DR KEGG; tfo:BFO_2758; -.
DR PATRIC; fig|203275.8.peg.2360; -.
DR eggNOG; COG1148; Bacteria.
DR eggNOG; COG2878; Bacteria.
DR HOGENOM; CLU_053470_0_0_10; -.
DR Proteomes; UP000005436; Chromosome.
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 CDD; cd10549; MtMvhB_like; 1.
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 PANTHER; PTHR43560; ION-TRANSLOCATING OXIDOREDUCTASE COMPLEX SUBUNIT B; 1.
DR PANTHER; PTHR43560:SF1; ION-TRANSLOCATING OXIDOREDUCTASE COMPLEX SUBUNIT B; 1.
DR Pfam; PF00037; Fer4; 1.
DR Pfam; PF12838; Fer4_7; 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; 4.
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}; 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:UP000005436};
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 29..89
FT /note="4Fe-4S"
FT /evidence="ECO:0000259|PROSITE:PS51656"
FT DOMAIN 125..159
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 161..190
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 208..237
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 238..268
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT REGION 1..23
FT /note="Hydrophobic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00463"
FT REGION 268..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 46
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 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 54
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 72
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 135
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 139
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 145
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 149
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 170
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 173
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 180
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 301 AA; 31735 MW; 40941AC7C719A66E CRC64;
MYIAIILLGV VGAVAALILF AVSKKFEVHE DPRIGQIQNA LPGANCGGCG FPGCGGFANA
CFKAESLEGL FCPVGGADVM KQVAAIMGKE AGESVPQIAV VRCNGTCEAR PRTNTYDGAR
SCAIAAALYS GETGCSFGCL GLGDCVDACD FDAIHINPET LLPEVVEDKC VACGACVKAC
PKHIIELRKK GPKSRRIFVS CMNKDKGGVA RKACTNACIG CSKCKKECPF EAITVTNNLA
YIDDTKCRLC RKCVAVCPTG AIHELNFPPR KEKEKETAAP EPKPVPQPEV IVPETSLTTN
N
//