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Database: UniProt
Entry: P54932
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ID   RDXB_RHOS4              Reviewed;         477 AA.
AC   P54932; P72341; Q3J016;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2003, sequence version 2.
DT   16-JAN-2019, entry version 110.
DE   RecName: Full=Protein RdxB;
GN   Name=rdxB; OrderedLocusNames=RHOS4_23000; ORFNames=RSP_0692;
OS   Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM
OS   158).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=272943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=9068641; DOI=10.1128/jb.179.6.1951-1961.1997;
RA   O'Gara J.P., Kaplan S.;
RT   "Evidence for the role of redox carriers in photosynthesis gene
RT   expression and carotenoid biosynthesis in Rhodobacter sphaeroides
RT   2.4.1.";
RL   J. Bacteriol. 179:1951-1961(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA   Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J.,
RA   Kaplan S.;
RT   "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-184.
RX   PubMed=7592416; DOI=10.1128/jb.177.22.6422-6431.1995;
RA   Zeilstra-Ryalls J.H., Kaplan S.;
RT   "Aerobic and anaerobic regulation in Rhodobacter sphaeroides 2.4.1:
RT   the role of the fnrL gene.";
RL   J. Bacteriol. 177:6422-6431(1995).
CC   -!- FUNCTION: Involved in a membrane generated redox signal; required
CC       to maintain repression of photosynthesis gene expression in the
CC       presence of oxygen. {ECO:0000269|PubMed:9068641}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC       Note=Binds 1 [4Fe-4S] cluster per subunit.;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
DR   EMBL; AF202779; AAF44623.1; -; Genomic_DNA.
DR   EMBL; CP000143; ABA79868.1; -; Genomic_DNA.
DR   RefSeq; WP_011338421.1; NZ_CP030271.1.
DR   RefSeq; YP_353769.1; NC_007493.2.
DR   ProteinModelPortal; P54932; -.
DR   SMR; P54932; -.
DR   STRING; 272943.RSP_0692; -.
DR   EnsemblBacteria; ABA79868; ABA79868; RSP_0692.
DR   GeneID; 3718342; -.
DR   KEGG; rsp:RSP_0692; -.
DR   PATRIC; fig|272943.9.peg.2644; -.
DR   eggNOG; ENOG4105C58; Bacteria.
DR   eggNOG; COG0348; LUCA.
DR   HOGENOM; HOG000284963; -.
DR   OMA; FRRIEYW; -.
DR   PhylomeDB; P54932; -.
DR   Proteomes; UP000002703; Chromosome 1.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR014116; Cyt_c_oxidase_cbb3_FixG.
DR   InterPro; IPR032879; FixG_C.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF13746; Fer4_18; 1.
DR   Pfam; PF12801; Fer4_5; 1.
DR   Pfam; PF11614; FixG_C; 1.
DR   TIGRFAMs; TIGR02745; ccoG_rdxA_fixG; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   4: Predicted;
KW   4Fe-4S; Cell membrane; Complete proteome; Electron transport; Iron;
KW   Iron-sulfur; Membrane; Metal-binding; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    477       Protein RdxB.
FT                                /FTId=PRO_0000159238.
FT   TOPO_DOM      1     29       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     30     50       Helical. {ECO:0000255}.
FT   TOPO_DOM     51     81       Periplasmic. {ECO:0000255}.
FT   TRANSMEM     82    102       Helical. {ECO:0000255}.
FT   TOPO_DOM    103    154       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    155    175       Helical. {ECO:0000255}.
FT   TOPO_DOM    176    189       Periplasmic. {ECO:0000255}.
FT   TRANSMEM    190    210       Helical. {ECO:0000255}.
FT   TOPO_DOM    211    338       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    339    359       Helical. {ECO:0000255}.
FT   TOPO_DOM    360    477       Periplasmic. {ECO:0000255}.
FT   DOMAIN      253    281       4Fe-4S ferredoxin-type.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL       262    262       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL       265    265       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL       268    268       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL       272    272       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       286    286       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       289    289       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       292    292       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL       296    296       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
SQ   SEQUENCE   477 AA;  53947 MW;  0D2E817FBDD6F5FF CRC64;
     MTSPDTQTSS LYAKREPVFP KRVSGKFRSL KWWIMGVTLG IYYIAPWLRW DRGPNLPDQA
     ILVDLANRRF FFFMIEIWPH EFYFVAGLLI MAGLGLFLFT SAAGRVWCGY ACPQTVWTDL
     FILVERWVEG DRNARIRLLR QRWDLEKTRK YLTKWTLWLL IGLATGGAWV FYFTDAPTLL
     VDLLTGNAHP VAYITMATLT ATTFAFGGFA REQICIYACP WPRIQAAMMD EETITVAYRE
     WRGEPRGKLK KGEPLSPDQG DCIDCMACVN VCPMGIDIRD GQQLACITCA LCIDACDEVM
     DKIGKPRGLI GYLALTDERA EREGRSPRSA WRHVFRLRTL IYTALWSGVG LALIVALFLR
     SPIDINVTPL RNPLYVTLSD GSIRNTYDVR LRNKQGEARD YQISVTSEAD LALSLEGHPA
     TVVTVPANET MTQRVYIIAG KGTPAAEAER TDLRLWVEDL AAGQRVHHDT IFNGRGN
//
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