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FIXP_RHIME
ID   FIXP_RHIME              Reviewed;         289 AA.
AC   Q05577;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Cbb3-type cytochrome c oxidase subunit FixP {ECO:0000250|UniProtKB:D5ARP7, ECO:0000312|EMBL:AAK65320.1};
DE            Short=Cbb3-Cox subunit FixP {ECO:0000250|UniProtKB:D5ARP7};
DE   AltName: Full=C-type cytochrome FixP {ECO:0000250|UniProtKB:Q52689};
DE            Short=Cyt c(FixP) {ECO:0000250|UniProtKB:D5ARP7};
DE   AltName: Full=Cytochrome c oxidase subunit III {ECO:0000250|UniProtKB:D5ARP7};
GN   Name=fixP {ECO:0000312|EMBL:CAA79904.1};
GN   Synonyms=fixP1 {ECO:0000312|EMBL:AAK65320.1}; OrderedLocusNames=RA0662;
GN   ORFNames=SMa1213;
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OG   Plasmid pSymA (megaplasmid 1) {ECO:0000312|EMBL:AAK65320.1}.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834;
RN   [1] {ECO:0000312|EMBL:CAA79904.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=RCR2011 / SU47 {ECO:0000312|EMBL:CAA79904.1};
RX   PubMed=11902723; DOI=10.1046/j.1365-2958.1997.4501814.x;
RA   Foussard M., Garnerone A.-M., Ni F., Soupene E., Boistard P., Batut J.;
RT   "Negative autoregulation of the Rhizobium meliloti fixK gene is indirect
RT   and requires a newly identified regulator, FixT.";
RL   Mol. Microbiol. 25:27-37(1997).
RN   [2] {ECO:0000312|EMBL:AAK65320.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021 {ECO:0000312|EMBL:AAK65320.1}; PLASMID=pSymA (megaplasmid 1);
RX   PubMed=11481432; DOI=10.1073/pnas.161294798;
RA   Barnett M.J., Fisher R.F., Jones T., Komp C., Abola A.P., Barloy-Hubler F.,
RA   Bowser L., Capela D., Galibert F., Gouzy J., Gurjal M., Hong A., Huizar L.,
RA   Hyman R.W., Kahn D., Kahn M.L., Kalman S., Keating D.H., Palm C.,
RA   Peck M.C., Surzycki R., Wells D.H., Yeh K.-C., Davis R.W., Federspiel N.A.,
RA   Long S.R.;
RT   "Nucleotide sequence and predicted functions of the entire Sinorhizobium
RT   meliloti pSymA megaplasmid.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9883-9888(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11474104; DOI=10.1126/science.1060966;
RA   Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA   Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA   Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA   Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA   Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA   Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA   Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA   Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA   Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA   Wong K., Yeh K.-C., Batut J.;
RT   "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL   Science 293:668-672(2001).
CC   -!- FUNCTION: C-type cytochrome. Part of the cbb3-type cytochrome c oxidase
CC       complex. FixP subunit is required for transferring electrons from donor
CC       cytochrome c via its heme groups to FixO subunit. From there, electrons
CC       are shuttled to the catalytic binuclear center of FixN subunit where
CC       oxygen reduction takes place. The complex also functions as a proton
CC       pump (By similarity). {ECO:0000250|UniProtKB:D9IA45,
CC       ECO:0000250|UniProtKB:Q03075, ECO:0000250|UniProtKB:Q8KLH5}.
CC   -!- COFACTOR:
CC       Name=heme c; Xref=ChEBI:CHEBI:61717;
CC         Evidence={ECO:0000250|UniProtKB:D9IA45};
CC       Note=Binds 2 heme C groups per subunit. {ECO:0000250|UniProtKB:D9IA45};
CC   -!- PATHWAY: Energy metabolism; oxidative phosphorylation.
CC       {ECO:0000250|UniProtKB:D5ARP7}.
CC   -!- SUBUNIT: Component of the cbb3-type cytochrome c oxidase at least
CC       composed of FixN, FixO, FixQ and FixP. {ECO:0000250|UniProtKB:D5ARP7}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:Q8KS19, ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000250|UniProtKB:Q8KS19, ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the CcoP / FixP family. {ECO:0000305}.
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DR   EMBL; Z21854; CAA79904.1; -; Genomic_DNA.
DR   EMBL; AE006469; AAK65320.1; -; Genomic_DNA.
DR   PIR; F95344; F95344.
DR   PIR; S39991; S39991.
DR   RefSeq; NP_435908.1; NC_003037.1.
DR   RefSeq; WP_010967641.1; NC_003037.1.
DR   AlphaFoldDB; Q05577; -.
DR   SMR; Q05577; -.
DR   EnsemblBacteria; AAK65320; AAK65320; SMa1213.
DR   GeneID; 61599430; -.
DR   KEGG; sme:SMa1213; -.
DR   PATRIC; fig|266834.11.peg.682; -.
DR   HOGENOM; CLU_047545_2_0_5; -.
DR   OMA; DWLYGGE; -.
DR   UniPathway; UPA00705; -.
DR   Proteomes; UP000001976; Plasmid pSymA.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProt.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.760.10; -; 2.
DR   Gene3D; 6.10.280.130; -; 1.
DR   InterPro; IPR032858; CcoP_N.
DR   InterPro; IPR038414; CcoP_N_sf.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   InterPro; IPR008168; Cyt_C_IC.
DR   InterPro; IPR004678; Cyt_c_oxidase_cbb3_su3.
DR   Pfam; PF13442; Cytochrome_CBB3; 2.
DR   Pfam; PF14715; FixP_N; 1.
DR   PIRSF; PIRSF000006; Cbb3-Cox_fixP; 1.
DR   PRINTS; PR00605; CYTCHROMECIC.
DR   SUPFAM; SSF46626; SSF46626; 2.
DR   TIGRFAMs; TIGR00782; ccoP; 1.
DR   PROSITE; PS51007; CYTC; 2.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Electron transport; Heme;
KW   Hydrogen ion transport; Ion transport; Iron; Membrane; Metal-binding;
KW   Oxidoreductase; Plasmid; Reference proteome; Repeat; Respiratory chain;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..289
FT                   /note="Cbb3-type cytochrome c oxidase subunit FixP"
FT                   /id="PRO_0000412300"
FT   TOPO_DOM        1..33
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q3J015, ECO:0000255"
FT   TRANSMEM        34..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        57..289
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q3J015, ECO:0000255"
FT   DOMAIN          110..198
FT                   /note="Cytochrome c 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   DOMAIN          205..286
FT                   /note="Cytochrome c 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         123
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250|UniProtKB:D9IA45"
FT   BINDING         126
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250|UniProtKB:D9IA45"
FT   BINDING         127
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:D9IA45"
FT   BINDING         175
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:D9IA45"
FT   BINDING         218
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250|UniProtKB:D9IA45"
FT   BINDING         221
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT                   /evidence="ECO:0000250|UniProtKB:D9IA45"
FT   BINDING         222
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:D9IA45"
FT   BINDING         263
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:D9IA45"
SQ   SEQUENCE   289 AA;  31097 MW;  46442B50508B4A9A CRC64;
     MADKHKHVDE VSGVETTGHE WDGIRELNNP MPRWWVYSFY ATIIWAIGYA IAYPSWPMLT
     EATKGMLGYS SRAEVSVELA AAKAAQAGNL EQIASSSVEE IIANPQLQQF AVSAGASAFK
     VNCAQCHGSG AAGGQGFPNL NDDDWLWGGK PQEIYQTIAH GVRHAPDGET RVSEMPPFGD
     MLTPELMQQT AAYVVSLTQA PSQPHLVQQG KQVFADNCAS CHGADAKGNR EMGAPNLADA
     IWLKGEGEQA VITQMKTPKH GVMPAWLPRL GDDTVKQLAV FVHSLGGGE
 
 
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