ID Q1ZS14_PHOAS Unreviewed; 194 AA.
AC Q1ZS14;
DT 02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 02-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 110.
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=VAS14_05568 {ECO:0000313|EMBL:EAS65163.1};
OS Photobacterium angustum (strain S14 / CCUG 15956) (Vibrio sp. (strain S14 /
OS CCUG 15956)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=314292 {ECO:0000313|EMBL:EAS65163.1, ECO:0000313|Proteomes:UP000001603};
RN [1] {ECO:0000313|EMBL:EAS65163.1, ECO:0000313|Proteomes:UP000001603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S14 {ECO:0000313|EMBL:EAS65163.1,
RC ECO:0000313|Proteomes:UP000001603};
RX PubMed=19805210; DOI=10.1073/pnas.0903507106;
RA Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S.,
RA DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A.,
RA Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V.,
RA Robb F.T., Kjelleberg S., Cavicchioli R.;
RT "The genomic basis of trophic strategy in marine bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(2009).
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 ECO:0000256|PIRSR:PIRSR005784-1};
CC Note=Binds 3 [4Fe-4S] clusters. {ECO:0000256|HAMAP-Rule:MF_00463,
CC ECO:0000256|PIRSR:PIRSR005784-1};
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:EAS65163.1}.
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DR EMBL; AAOJ01000002; EAS65163.1; -; Genomic_DNA.
DR RefSeq; WP_005368843.1; NZ_CH902600.1.
DR AlphaFoldDB; Q1ZS14; -.
DR eggNOG; COG2878; Bacteria.
DR HOGENOM; CLU_063448_2_0_6; -.
DR OrthoDB; 9789936at2; -.
DR Proteomes; UP000001603; 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 InterPro; IPR016463; RnfB/RsxB_Proteobac.
DR NCBIfam; TIGR01944; rnfB; 1.
DR PANTHER; PTHR42859:SF3; ION-TRANSLOCATING OXIDOREDUCTASE COMPLEX SUBUNIT B; 1.
DR PANTHER; PTHR42859; OXIDOREDUCTASE; 1.
DR Pfam; PF14697; Fer4_21; 1.
DR Pfam; PF04060; FeS; 1.
DR PIRSF; PIRSF005784; Elect_transpt_RnfB; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR PROSITE; PS51656; 4FE4S; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
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 inner membrane {ECO:0000256|ARBA:ARBA00022519, ECO:0000256|HAMAP-
KW Rule:MF_00463};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00463}; 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}; 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..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 32..90
FT /note="4Fe-4S"
FT /evidence="ECO:0000259|PROSITE:PS51656"
FT DOMAIN 105..134
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 135..164
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 ECO:0000256|PIRSR:PIRSR005784-1"
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 ECO:0000256|PIRSR:PIRSR005784-1"
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 ECO:0000256|PIRSR:PIRSR005784-1"
FT BINDING 73
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00463,
FT ECO:0000256|PIRSR:PIRSR005784-1"
FT BINDING 114
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00463,
FT ECO:0000256|PIRSR:PIRSR005784-1"
FT BINDING 117
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00463,
FT ECO:0000256|PIRSR:PIRSR005784-1"
FT BINDING 120
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00463,
FT ECO:0000256|PIRSR:PIRSR005784-1"
FT BINDING 124
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00463,
FT ECO:0000256|PIRSR:PIRSR005784-1"
FT BINDING 144
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00463,
FT ECO:0000256|PIRSR:PIRSR005784-1"
FT BINDING 147
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00463,
FT ECO:0000256|PIRSR:PIRSR005784-1"
FT BINDING 150
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00463,
FT ECO:0000256|PIRSR:PIRSR005784-1"
FT BINDING 154
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00463,
FT ECO:0000256|PIRSR:PIRSR005784-1"
SQ SEQUENCE 194 AA; 20676 MW; EB77FC770E69C62D CRC64;
MSGILIAVIA IVILAAIFGL ILGFASVKFK VEADPIVEQI DAILPQTQCG QCGYPGCRPY
AEAIANGDVI NKCPPGGQVT IEKLADLMGV DVPDSTQGEE ENIKKVAFIH EDMCIGCTKC
IQACPVDAIV GGTKSMHTVI KDECTGCDLC VAPCPTDCIE MIPVKETPDN WKWQLNQIPI
VNISDAPSTE KVES
//