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Database: UniProt
Entry: Q2SKU5
LinkDB: Q2SKU5
Original site: Q2SKU5 
ID   RNFB_HAHCH              Reviewed;         197 AA.
AC   Q2SKU5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   16-JAN-2019, entry version 95.
DE   RecName: Full=Ion-translocating oxidoreductase complex subunit B {ECO:0000255|HAMAP-Rule:MF_00463};
DE            EC=7.-.-.- {ECO:0000255|HAMAP-Rule:MF_00463};
DE   AltName: Full=Rnf electron transport complex subunit B {ECO:0000255|HAMAP-Rule:MF_00463};
GN   Name=rnfB {ECO:0000255|HAMAP-Rule:MF_00463};
GN   OrderedLocusNames=HCH_01893;
OS   Hahella chejuensis (strain KCTC 2396).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Hahellaceae; Hahella.
OX   NCBI_TaxID=349521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 2396;
RX   PubMed=16352867; DOI=10.1093/nar/gki1016;
RA   Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H.,
RA   Hur C.-G., Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H.,
RA   Park H.-S., Lee H.K., Oh T.K., Kim J.F.;
RT   "Genomic blueprint of Hahella chejuensis, a marine microbe producing
RT   an algicidal agent.";
RL   Nucleic Acids Res. 33:7066-7073(2005).
CC   -!- FUNCTION: Part of a membrane-bound complex that couples electron
CC       transfer with translocation of ions across the membrane.
CC       {ECO:0000255|HAMAP-Rule:MF_00463}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00463};
CC       Note=Binds 3 [4Fe-4S] clusters. {ECO:0000255|HAMAP-Rule:MF_00463};
CC   -!- SUBUNIT: The complex is composed of six subunits: RnfA, RnfB,
CC       RnfC, RnfD, RnfE and RnfG. {ECO:0000255|HAMAP-Rule:MF_00463}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00463}.
CC   -!- SIMILARITY: Belongs to the 4Fe4S bacterial-type ferredoxin family.
CC       RnfB subfamily. {ECO:0000255|HAMAP-Rule:MF_00463}.
DR   EMBL; CP000155; ABC28729.1; -; Genomic_DNA.
DR   RefSeq; WP_011395800.1; NC_007645.1.
DR   ProteinModelPortal; Q2SKU5; -.
DR   SMR; Q2SKU5; -.
DR   STRING; 349521.HCH_01893; -.
DR   EnsemblBacteria; ABC28729; ABC28729; HCH_01893.
DR   KEGG; hch:HCH_01893; -.
DR   eggNOG; ENOG4108R3D; Bacteria.
DR   eggNOG; COG2878; LUCA.
DR   HOGENOM; HOG000262938; -.
DR   KO; K03616; -.
DR   OMA; CIDMLPV; -.
DR   OrthoDB; 1619561at2; -.
DR   BioCyc; HCHE349521:G1G5E-1721-MONOMER; -.
DR   Proteomes; UP000000238; 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   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   PANTHER; PTHR42859:SF3; PTHR42859:SF3; 1.
DR   Pfam; PF04060; FeS; 1.
DR   PIRSF; PIRSF005784; Elect_transpt_RnfB; 1.
DR   TIGRFAMs; TIGR01944; rnfB; 1.
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; Cell inner membrane; Cell membrane; Complete proteome;
KW   Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding;
KW   Reference proteome; Repeat; Translocase; Transport.
FT   CHAIN         1    197       Ion-translocating oxidoreductase complex
FT                                subunit B.
FT                                /FTId=PRO_1000013648.
FT   DOMAIN       32     90       4Fe-4S. {ECO:0000255|HAMAP-
FT                                Rule:MF_00463}.
FT   DOMAIN      106    135       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   DOMAIN      136    165       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   REGION        1     26       Hydrophobic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00463}.
FT   METAL        49     49       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL        52     52       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL        57     57       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL        73     73       Iron-sulfur 1 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       115    115       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       118    118       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       121    121       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       125    125       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       145    145       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       148    148       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       151    151       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       155    155       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
SQ   SEQUENCE   197 AA;  20447 MW;  C2519F1C6DD732D2 CRC64;
     MSIVIIAVLA LSALALTFGA VLGFASIKFK VEGNPIVDQI DGLLPQTQCG QCGYPGCRPY
     AEAIANGDAI NKCPPGGEAT ITALADLLDV EAVPLDSEHG ESKGKQVAYI REDECIGCTK
     CIQACPVDAI LGAAKQMHTV IVSECTGCDL CVEPCPVDCI DMIPAPSGIR DWAWDMPKPP
     VSSGAIIATD QNNGMAA
//
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