FIXP_RHILV
ID FIXP_RHILV Reviewed; 287 AA.
AC P72287;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Cbb3-type cytochrome c oxidase subunit FixPc {ECO:0000250|UniProtKB:D5ARP7, ECO:0000312|EMBL:CAB02452.1};
DE Short=Cbb3-Cox subunit FixPc {ECO:0000250|UniProtKB:D5ARP7};
DE AltName: Full=C-type cytochrome FixPc {ECO:0000250|UniProtKB:Q52689};
DE Short=Cyt c(FixPc) {ECO:0000250|UniProtKB:D5ARP7};
DE AltName: Full=Cytochrome c oxidase subunit III {ECO:0000250|UniProtKB:D5ARP7};
GN Name=fixPc {ECO:0000312|EMBL:CAB02452.1};
OS Rhizobium leguminosarum bv. viciae.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=387;
RN [1] {ECO:0000312|EMBL:CAB02452.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=VF39 {ECO:0000312|EMBL:CAB02452.1};
RX PubMed=9204566; DOI=10.1094/mpmi.1997.10.5.605;
RA Schluter A., Patschkowski T., Quandt J., Selinger L.B., Weidner S.,
RA Kramer M., Zhou L., Hynes M.F., Priefer U.B.;
RT "Functional and regulatory analysis of the two copies of the fixNOQP operon
RT of Rhizobium leguminosarum strain VF39.";
RL Mol. Plant Microbe Interact. 10:605-616(1997).
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; Z80340; CAB02452.1; -; Genomic_DNA.
DR RefSeq; WP_011654241.1; NZ_WIDY01000016.1.
DR AlphaFoldDB; P72287; -.
DR SMR; P72287; -.
DR OMA; DWLYGGE; -.
DR UniPathway; UPA00705; -.
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; Repeat; Respiratory chain; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..287
FT /note="Cbb3-type cytochrome c oxidase subunit FixPc"
FT /id="PRO_0000412299"
FT TOPO_DOM 1..36
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q3J015, ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..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"
SQ SEQUENCE 287 AA; 30688 MW; F8A55D976953E566 CRC64;
MSEKHIDEFS GVETTGHEWD GIRELNNPMP RWWVWTFYAT IVWALGYAIA YPAIPMITDA
TKGMLGFSSR AELQQNLDQA KASQTTLHDL IAAKTVHEID SDSALREFAI AGGASAFKVN
CATCHGSGAS GGPGFPNLND DDWLWGGDLD AIQATIAHGI RFDGDTDTHA SEMPPFAEVL
DPLQTRQVAA YVWGLTNTPS DPGLAEAGKQ VFVDNCAACH GDDAKGKAEM GAPDLADAIW
LKARGEDAII RQVAAPKHGV MPAWAGRLGD TTVKELTIFV HSLGGGT
