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Database: UniProt
Entry: A7MVC6
LinkDB: A7MVC6
Original site: A7MVC6 
ID   RNFB_VIBCB              Reviewed;         197 AA.
AC   A7MVC6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   10-APR-2019, entry version 81.
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=VIBHAR_02965;
OS   Vibrio campbellii (strain ATCC BAA-1116 / BB120).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=338187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1116 / BB120;
RG   The Vibrio harveyi Genome Sequencing Project;
RA   Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA   Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N.,
RA   Pepin K., Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C.,
RA   Irgon J., Wilson R.K.;
RL   Submitted (AUG-2007) 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: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; CP000789; ABU71916.1; -; Genomic_DNA.
DR   RefSeq; WP_012128497.1; NC_022269.1.
DR   ProteinModelPortal; A7MVC6; -.
DR   SMR; A7MVC6; -.
DR   EnsemblBacteria; ABU71916; ABU71916; VIBHAR_02965.
DR   GeneID; 5554735; -.
DR   KEGG; vca:M892_16150; -.
DR   KEGG; vha:VIBHAR_02965; -.
DR   PATRIC; fig|338187.25.peg.3222; -.
DR   eggNOG; ENOG4108R3D; Bacteria.
DR   eggNOG; COG2878; LUCA.
DR   HOGENOM; HOG000262938; -.
DR   KO; K03616; -.
DR   OMA; CIDMLPV; -.
DR   OrthoDB; 1619561at2; -.
DR   BioCyc; VCAM338187:G1HKJ-3291-MONOMER; -.
DR   Proteomes; UP000008152; Chromosome I.
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   Repeat; Translocase; Transport.
FT   CHAIN         1    197       Ion-translocating oxidoreductase complex
FT                                subunit B.
FT                                /FTId=PRO_1000013665.
FT   DOMAIN       32     90       4Fe-4S. {ECO:0000255|HAMAP-
FT                                Rule:MF_00463}.
FT   DOMAIN      105    134       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   DOMAIN      135    164       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       114    114       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       117    117       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       120    120       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       124    124       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       144    144       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       147    147       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       150    150       Iron-sulfur 3 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
FT   METAL       154    154       Iron-sulfur 2 (4Fe-4S).
FT                                {ECO:0000255|HAMAP-Rule:MF_00463}.
SQ   SEQUENCE   197 AA;  20723 MW;  6BDEB5D1B20D658C CRC64;
     MSTILIAIIA LAALAAVFGA ILGFASIRFK VEADPIVDQI DSILPQTQCG QCGYPGCRPY
     AEAIANGDQI NKCPPGGQAT IEKLADLMGV EAEESAHDLD SKVKTVAFIH EDMCIGCTKC
     IQACPVDAIV GGTKALHTVI KDECTGCDLC VAPCPTDCIE MIPVETTTES WKWKLNAIPV
     VNITDAANAA NVTDSIK
//
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