GenomeNet

Database: UniProt
Entry: K6Z4V9_9ALTE
LinkDB: K6Z4V9_9ALTE
Original site: K6Z4V9_9ALTE 
ID   K6Z4V9_9ALTE            Unreviewed;       188 AA.
AC   K6Z4V9;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   24-JAN-2024, entry version 56.
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:GAC18450.1};
GN   ORFNames=GARC_1477 {ECO:0000313|EMBL:GAC18450.1};
OS   Paraglaciecola arctica BSs20135.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Paraglaciecola.
OX   NCBI_TaxID=493475 {ECO:0000313|EMBL:GAC18450.1, ECO:0000313|Proteomes:UP000006327};
RN   [1] {ECO:0000313|EMBL:GAC18450.1, ECO:0000313|Proteomes:UP000006327}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BSs20135 {ECO:0000313|EMBL:GAC18450.1,
RC   ECO:0000313|Proteomes:UP000006327};
RX   PubMed=25009843;
RA   Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA   Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT   "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT   high degree of genomic diversity and genomic characteristic for cold
RT   adaptation.";
RL   Environ. Microbiol. 16:1642-1653(2014).
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:GAC18450.1}.
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; BAEO01000017; GAC18450.1; -; Genomic_DNA.
DR   RefSeq; WP_007618293.1; NZ_BAEO01000017.1.
DR   AlphaFoldDB; K6Z4V9; -.
DR   STRING; 493475.GARC_1477; -.
DR   eggNOG; COG2878; Bacteria.
DR   OrthoDB; 9789936at2; -.
DR   Proteomes; UP000006327; 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|HAMAP-Rule:MF_00463};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00463};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|HAMAP-
KW   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|ARBA:ARBA00023136, 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:UP000006327};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_00463};
KW   Translocase {ECO:0000256|HAMAP-Rule:MF_00463};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00463}.
FT   DOMAIN          35..93
FT                   /note="4Fe-4S"
FT                   /evidence="ECO:0000259|PROSITE:PS51656"
FT   DOMAIN          109..138
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          139..168
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   REGION          1..29
FT                   /note="Hydrophobic"
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                   ECO:0000256|PIRSR:PIRSR005784-1"
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                   ECO:0000256|PIRSR:PIRSR005784-1"
FT   BINDING         60
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         76
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         118
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         121
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="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00463,
FT                   ECO:0000256|PIRSR:PIRSR005784-1"
FT   BINDING         128
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         148
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         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                   ECO:0000256|PIRSR:PIRSR005784-1"
FT   BINDING         154
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         158
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   188 AA;  19995 MW;  45571ECDCC67D604 CRC64;
     MSLTFAILTA LLAIGLLALI FGLVLGFAAV KFKVESDPLV EQIDQILPQT QCGQCGYPGC
     KPYAQAIADG DEINKCPPGG DATIKKLADL MGVEAKSLDA AHGQEDIKKV AYIREDECIG
     CTKCIQACPV DAILGAAKQM HTVIVDECTG CDLCVDPCPV DCIDMIPLAN NASSWRWNID
     SIPIKQIG
//
DBGET integrated database retrieval system