FIXP_RHIEC
ID FIXP_RHIEC Reviewed; 287 AA.
AC Q8KLH5; O69780;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Cbb3-type cytochrome c oxidase subunit FixP {ECO:0000312|EMBL:AAM54763.1};
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:0000312|EMBL:AAM54763.1};
GN Name=fixP {ECO:0000312|EMBL:AAC15890.1}; OrderedLocusNames=RHE_PD00293;
OS Rhizobium etli (strain CFN 42 / ATCC 51251).
OG Plasmid sym p42d.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=347834;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC15890.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=CE3 {ECO:0000312|EMBL:AAC15890.1};
RX PubMed=10223993; DOI=10.1128/aem.65.5.2015-2019.1999;
RA Soberon M., Lopez O., Morera C., Girard M.L., Tabche M.L., Miranda J.;
RT "Enhanced nitrogen fixation in a rhizobium etli ntrC mutant that
RT overproduces the bradyrhizobium japonicum symbiotic terminal oxidase
RT cbb3.";
RL Appl. Environ. Microbiol. 65:2015-2019(1999).
RN [2] {ECO:0000312|EMBL:AAM54763.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFN 42 / ATCC 51251 {ECO:0000312|EMBL:AAM54763.1};
RX PubMed=12801410; DOI=10.1186/gb-2003-4-6-r36;
RA Gonzalez V., Bustos P., Ramirez-Romero M.A., Medrano-Soto A., Salgado H.,
RA Hernandez-Gonzalez I., Hernandez-Celis J.C., Quintero V.,
RA Moreno-Hagelsieb G., Girard L., Rodriguez O., Flores M., Cevallos M.A.,
RA Collado-Vides J., Romero D., Davila G.;
RT "The mosaic structure of the symbiotic plasmid of Rhizobium etli CFN42 and
RT its relation to other symbiotic genome compartments.";
RL Genome Biol. 4:R36.1-R36.13(2003).
RN [3] {ECO:0000312|EMBL:AAM54763.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFN 42 / ATCC 51251 {ECO:0000312|EMBL:AAM54763.1};
RX PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT seven interacting replicons.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
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. {ECO:0000250|UniProtKB:D9IA45, ECO:0000250|UniProtKB:Q03075,
CC ECO:0000269|PubMed:10223993}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U76906; AAC15890.1; -; Genomic_DNA.
DR EMBL; U80928; AAM54763.1; -; Genomic_DNA.
DR RefSeq; WP_004674413.1; NC_004041.2.
DR AlphaFoldDB; Q8KLH5; -.
DR SMR; Q8KLH5; -.
DR EnsemblBacteria; AAM54763; AAM54763; RHE_PD00293.
DR GeneID; 45960636; -.
DR GeneID; 58692275; -.
DR KEGG; ret:RHE_PD00293; -.
DR HOGENOM; CLU_047545_2_0_5; -.
DR OMA; KTTGHEW; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000001936; Plasmid sym p42d.
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..287
FT /note="Cbb3-type cytochrome c oxidase subunit FixP"
FT /id="PRO_0000412298"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q3J015, ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..287
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q3J015, ECO:0000255"
FT DOMAIN 108..196
FT /note="Cytochrome c 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT DOMAIN 203..284
FT /note="Cytochrome c 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 121
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 124
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 125
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 173
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 216
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 219
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 220
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 261
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 VARIANT 11..12
FT /note="GV -> VA (in strain: CE3)"
FT /evidence="ECO:0000269|PubMed:10223993"
FT VARIANT 43
FT /note="W -> C (in strain: CE3)"
FT VARIANT 45..46
FT /note="IG -> DP (in strain: CE3)"
FT /evidence="ECO:0000269|PubMed:10223993"
FT VARIANT 247..248
FT /note="DA -> EP (in strain: CE3)"
FT /evidence="ECO:0000269|PubMed:10223993"
FT VARIANT 278
FT /note="I -> N (in strain: CE3)"
FT /evidence="ECO:0000269|PubMed:10223993"
FT VARIANT 282..283
FT /note="AL -> RF (in strain: CE3)"
FT /evidence="ECO:0000269|PubMed:10223993"
SQ SEQUENCE 287 AA; 30767 MW; 811F3C5E60022AE9 CRC64;
MSQKHIDELS GVETTGHEWD GIQELNNPMP RWWIWTFYVT ILWAIGYAIA YPAIPMITSA
TNGYLGYSTR AELQQDLNLA KSSQTEFHDL IAAKTVEEID ADPALRKFAI AGGASAFKVN
CAPCHGSGAS GGPGFPNLND DDWLWGGDLN AIQATISHGI RFDGDTDSHS SEMPPFAGVL
EPIQMKQVAA FVWGLTNTPS DVGLAAAGKQ VFFDNCAPCH GEDAKGKVEM GAPDLADAIW
LKSRGEDAIL RQVASPKHGV MPAWAARLGD TTVNELTIFV HALGGGT
