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Database: UniProt
Entry: A8GE01
LinkDB: A8GE01
Original site: A8GE01 
ID   RNFB_SERP5              Reviewed;         190 AA.
AC   A8GE01;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   16-JAN-2019, entry version 80.
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=Spro_2240;
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=399741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Taghavi S., Newman L., Vangronsveld J., van der Lelie D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL   Submitted (SEP-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; CP000826; ABV41341.1; -; Genomic_DNA.
DR   RefSeq; WP_012144971.1; NC_009832.1.
DR   ProteinModelPortal; A8GE01; -.
DR   STRING; 399741.Spro_2240; -.
DR   EnsemblBacteria; ABV41341; ABV41341; Spro_2240.
DR   KEGG; spe:Spro_2240; -.
DR   eggNOG; ENOG4108R3D; Bacteria.
DR   eggNOG; COG2878; LUCA.
DR   HOGENOM; HOG000262938; -.
DR   KO; K03616; -.
DR   OMA; CIDMLPV; -.
DR   OrthoDB; 1619561at2; -.
DR   BioCyc; SPRO399741:GI55-2295-MONOMER; -.
DR   Proteomes; UP000007074; 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   Repeat; Translocase; Transport.
FT   CHAIN         1    190       Ion-translocating oxidoreductase complex
FT                                subunit B.
FT                                /FTId=PRO_1000060350.
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   190 AA;  20317 MW;  27FBB84FCB7A5C62 CRC64;
     MTALWIAIAA LSALGLLFGL VLGYAARRFE VEEDPVAEQV DEILPQSQCG QCGYPGCRPY
     AEAVANGEMI NKCAPGGEQV MLKLAELLNV EPQPLGSEAA AEPVRQVAYI DEANCIGCTK
     CIQACPVDAI VGATRAMHTV ITDLCTGCDL CVAPCPTDCI EMRPVATTTA NWKWDMKTIP
     VQVIHVEQHA
//
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