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