FIXP_AZOC5
ID FIXP_AZOC5 Reviewed; 293 AA.
AC A8HZ17; Q43945;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Cbb3-type cytochrome c oxidase subunit FixP {ECO:0000250|UniProtKB:D5ARP7, ECO:0000312|EMBL:BAF90524.1};
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:BAF90524.1}; OrderedLocusNames=AZC_4526;
OS Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / LMG
OS 6465 / NBRC 14845 / NCIMB 13405 / ORS 571).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Azorhizobium.
OX NCBI_TaxID=438753;
RN [1] {ECO:0000312|EMBL:CAA52432.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 / NCIMB
RC 13405 / ORS 571 {ECO:0000312|EMBL:CAA52432.1};
RX PubMed=8282187; DOI=10.1111/j.1574-6968.1993.tb06571.x;
RA Mandon K., Kaminski P.A., Mougel C., Desnoues N., Elmerich C.;
RT "Role of the fixGHI region of Azorhizobium caulinodans in free-living and
RT symbiotic nitrogen fixation.";
RL FEMS Microbiol. Lett. 114:185-189(1993).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAA52432.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND COFACTOR.
RC STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 / NCIMB
RC 13405 / ORS 571 {ECO:0000269|PubMed:8169204};
RX PubMed=8169204; DOI=10.1128/jb.176.9.2560-2568.1994;
RA Mandon K., Kaminski P.A., Elmerich C.;
RT "Functional analysis of the fixNOQP region of Azorhizobium caulinodans.";
RL J. Bacteriol. 176:2560-2568(1994).
RN [3] {ECO:0000312|EMBL:BAF90524.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 / NCIMB
RC 13405 / ORS 571 {ECO:0000312|EMBL:BAF90524.1};
RA Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., Kaneko T.,
RA Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B.,
RA Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., Oyaizu H.;
RT "Complete genome sequence of the nitrogen-fixing bacterium Azorhizobium
RT caulinodans ORS571.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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:D5ARP7,
CC ECO:0000250|UniProtKB:D9IA45, ECO:0000250|UniProtKB:Q03075}.
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000250|UniProtKB:D9IA45, ECO:0000269|PubMed:8169204};
CC Note=Binds 2 heme C groups per subunit. {ECO:0000250|UniProtKB:D9IA45,
CC ECO:0000269|PubMed:8169204};
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; X74410; CAA52432.1; -; Genomic_DNA.
DR EMBL; AP009384; BAF90524.1; -; Genomic_DNA.
DR PIR; D55582; D55582.
DR RefSeq; WP_012173045.1; NC_009937.1.
DR AlphaFoldDB; A8HZ17; -.
DR SMR; A8HZ17; -.
DR STRING; 438753.AZC_4526; -.
DR EnsemblBacteria; BAF90524; BAF90524; AZC_4526.
DR KEGG; azc:AZC_4526; -.
DR eggNOG; COG2010; Bacteria.
DR HOGENOM; CLU_047545_2_0_5; -.
DR OMA; DWLYGGE; -.
DR OrthoDB; 1315115at2; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000000270; Chromosome.
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; Reference proteome; Repeat; Respiratory chain;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..293
FT /note="Cbb3-type cytochrome c oxidase subunit FixP"
FT /id="PRO_0000412295"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 114..201
FT /note="Cytochrome c 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT DOMAIN 209..290
FT /note="Cytochrome c 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 127
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 130
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 131
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 178
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 222
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 225
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 226
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 267
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 293 AA; 30980 MW; 8306973270FDEDEC CRC64;
MSTSHESHHA PVDGAGGPST TGHEWDGIQE LNNPLPRWWL WTFYATIIWA FGYWVAYPAW
PLVSNYTSGV LGWNSRSAVV EQISDLQKLR AASSAKLANV PLEDIEKNPE LLSLARAEGK
VAFADNCAPC HGAGGGGAKG FPNLNDDDWL WGGTLAQIQQ TITHGIRSGD DEGHQGNMLA
FGSILSKADI SNVADYVRSL SGAAPGDTPA AKKGAEIFAA NCATCHGENG KGNQELGSKN
LTDGIWLYGG DKATIVQTIT NGRGGVMPAW GPRLSPTTIK ALTVYVHTLG GGQ
