ID RNFB_ECOL5 Reviewed; 192 AA.
AC Q0THJ9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 01-MAY-2013, entry version 57.
DE RecName: Full=Electron transport complex protein RnfB;
GN Name=rnfB; OrderedLocusNames=ECP_1573;
OS Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=362663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=536 / UPEC;
RX PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT "Role of pathogenicity island-associated integrases in the genome
RT plasticity of uropathogenic Escherichia coli strain 536.";
RL Mol. Microbiol. 61:584-595(2006).
CC -!- FUNCTION: May be part of a membrane complex involved in electron
CC transport (By similarity).
CC -!- COFACTOR: Binds 1 2Fe-2S cluster (Potential).
CC -!- COFACTOR: Binds 2 4Fe-4S clusters (Potential).
CC -!- SUBUNIT: Composed of at least six subunits; RnfA, RnfB, RnfC,
CC RnfD, RnfE and RnfG (By similarity).
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane
CC protein (By similarity).
CC -!- SIMILARITY: Belongs to the 4Fe4S bacterial-type ferredoxin family.
CC RnfB subfamily.
CC -!- SIMILARITY: Contains 1 4Fe-4S domain.
CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains.
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DR EMBL; CP000247; ABG69580.1; -; Genomic_DNA.
DR RefSeq; YP_669481.1; NC_008253.1.
DR ProteinModelPortal; Q0THJ9; -.
DR SMR; Q0THJ9; 105-169.
DR STRING; 362663.ECP_1573; -.
DR EnsemblBacteria; ABG69580; ABG69580; ECP_1573.
DR GeneID; 4187976; -.
DR KEGG; ecp:ECP_1573; -.
DR PATRIC; 18193870; VBIEscCol77757_1591.
DR eggNOG; COG2878; -.
DR HOGENOM; HOG000262938; -.
DR KO; K03616; -.
DR OMA; NGEMINK; -.
DR PhylomeDB; Q0THJ9; -.
DR ProtClustDB; PRK05113; -.
DR BioCyc; ECOL362663:GIY5-1580-MONOMER; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR GO; GO:0009399; P:nitrogen fixation; IEA:HAMAP.
DR HAMAP; MF_00463; 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.
DR InterPro; IPR016463; RnfB_Proteobac.
DR Pfam; PF13187; Fer4_9; 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 2Fe-2S; 4Fe-4S; Cell inner membrane; Cell membrane; Complete proteome;
KW Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding;
KW Repeat; Transport.
FT CHAIN 1 192 Electron transport complex protein RnfB.
FT /FTId=PRO_1000013641.
FT DOMAIN 32 91 4Fe-4S.
FT DOMAIN 108 137 4Fe-4S ferredoxin-type 1.
FT DOMAIN 138 167 4Fe-4S ferredoxin-type 2.
FT METAL 49 49 Iron-sulfur 1 (2Fe-2S) (Potential).
FT METAL 52 52 Iron-sulfur 1 (2Fe-2S) (Potential).
FT METAL 57 57 Iron-sulfur 1 (2Fe-2S) (Potential).
FT METAL 74 74 Iron-sulfur 1 (2Fe-2S) (Potential).
FT METAL 117 117 Iron-sulfur 2 (4Fe-4S) (By similarity).
FT METAL 120 120 Iron-sulfur 2 (4Fe-4S) (By similarity).
FT METAL 123 123 Iron-sulfur 2 (4Fe-4S) (By similarity).
FT METAL 127 127 Iron-sulfur 3 (4Fe-4S) (By similarity).
FT METAL 147 147 Iron-sulfur 3 (4Fe-4S) (By similarity).
FT METAL 150 150 Iron-sulfur 3 (4Fe-4S) (By similarity).
FT METAL 153 153 Iron-sulfur 3 (4Fe-4S) (By similarity).
FT METAL 157 157 Iron-sulfur 2 (4Fe-4S) (By similarity).
SQ SEQUENCE 192 AA; 20574 MW; 28E570400EF9B2FD CRC64;
MNAIWIAVAA VSLLGLAFGA ILGYASRRFA VEDDPVVEKI DEILPQSQCG QCGYPGCRPY
AETISCNGEK INRCAPGGEA VMLKIAELLN VEPQPLDGEA QELTPARMVA VIDENNCIGC
TKCIQACPVD AIVGATRAMH TVMSDLCTGC NLCVDPCPTH CISLQPVAET PDSWKWDLNT
IPVRIIPVEH HA
//
