FIXP_BRADU
ID FIXP_BRADU Reviewed; 290 AA.
AC Q03075; D4AER5; E7FH98; Q79UA4; Q89RK3;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Cbb3-type cytochrome c oxidase subunit FixP {ECO:0000250|UniProtKB:D5ARP7};
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:BAC48031.1};
GN Name=fixP {ECO:0000312|EMBL:AAA26206.1}; OrderedLocusNames=blr2766;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAA26206.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY OF THE CYTOCHROME C
RP OXIDASE COMPLEX, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8386371; DOI=10.1073/pnas.90.8.3309;
RA Preisig O., Anthamatten D., Hennecke H.;
RT "Genes for a microaerobically induced oxidase complex in Bradyrhizobium
RT japonicum are essential for a nitrogen-fixing endosymbiosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:3309-3313(1993).
RN [2] {ECO:0000312|EMBL:CAA06282.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=USDA 110spc4 {ECO:0000312|EMBL:CAA06282.1};
RX PubMed=9748464; DOI=10.1128/jb.180.19.5251-5255.1998;
RA Nellen-Anthamatten D., Rossi P., Preisig O., Kullik I., Babst M.,
RA Fischer H.M., Hennecke H.;
RT "Bradyrhizobium japonicum FixK2, a crucial distributor in the FixLJ-
RT dependent regulatory cascade for control of genes inducible by low oxygen
RT levels.";
RL J. Bacteriol. 180:5251-5255(1998).
RN [3] {ECO:0000312|EMBL:BAC48031.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
RN [4] {ECO:0000305}
RP PROTEIN SEQUENCE OF 1-7, FUNCTION, CATALYTIC ACTIVITY OF THE CYTOCHROME C
RP OXIDASE COMPLEX, COFACTOR, AND SUBUNIT.
RX PubMed=8626278; DOI=10.1128/jb.178.6.1532-1538.1996;
RA Preisig O., Zufferey R., Thony-Meyer L., Appleby C.A., Hennecke H.;
RT "A high-affinity cbb3-type cytochrome oxidase terminates the symbiosis-
RT specific respiratory chain of Bradyrhizobium japonicum.";
RL J. Bacteriol. 178:1532-1538(1996).
RN [5] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY OF THE CYTOCHROME C OXIDASE COMPLEX, SUBUNIT,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=8621562; DOI=10.1074/jbc.271.15.9114;
RA Zufferey R., Preisig O., Hennecke H., Thony-Meyer L.;
RT "Assembly and function of the cytochrome cbb3 oxidase subunits in
RT Bradyrhizobium japonicum.";
RL J. Biol. Chem. 271:9114-9119(1996).
RN [6] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY OF THE CYTOCHROME C OXIDASE COMPLEX, COFACTOR,
RP SUBUNIT, MASS SPECTROMETRY, AND MUTAGENESIS OF CYS-122; CYS-125; CYS-219
RP AND CYS-222.
RX PubMed=9257693; DOI=10.1016/s0014-5793(97)00746-1;
RA Zufferey R., Hennecke H., Thony-Meyer L.;
RT "Heme C incorporation into the c-type cytochromes FixO and FixP is
RT essential for assembly of the Bradyrhizobium japonicum cbb3-type oxidase.";
RL FEBS Lett. 412:75-78(1997).
RN [7] {ECO:0000305}
RP FUNCTION, COFACTOR, AND SUBCELLULAR LOCATION.
RX PubMed=9790980; DOI=10.1006/bbrc.1998.9549;
RA Arslan E., Schulz H., Zufferey R., Kunzler P., Thony-Meyer L.;
RT "Overproduction of the Bradyrhizobium japonicum c-type cytochrome subunits
RT of the cbb3 oxidase in Escherichia coli.";
RL Biochem. Biophys. Res. Commun. 251:744-747(1998).
RN [8] {ECO:0000305}
RP FUNCTION, AND CATALYTIC ACTIVITY OF THE CYTOCHROME C OXIDASE COMPLEX.
RX PubMed=10722835; DOI=10.1016/s0014-5793(00)01277-1;
RA Arslan E., Kannt A., Thony-Meyer L., Hennecke H.;
RT "The symbiotically essential cbb(3)-type oxidase of Bradyrhizobium
RT japonicum is a proton pump.";
RL FEBS Lett. 470:7-10(2000).
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:0000269|PubMed:10722835,
CC ECO:0000269|PubMed:8386371, ECO:0000269|PubMed:8621562,
CC ECO:0000269|PubMed:8626278, ECO:0000269|PubMed:9257693,
CC ECO:0000269|PubMed:9790980}.
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC Evidence={ECO:0000250|UniProtKB:D9IA45, ECO:0000269|PubMed:8626278,
CC ECO:0000269|PubMed:9257693, ECO:0000269|PubMed:9790980};
CC Note=Binds 2 heme C groups per subunit. {ECO:0000250|UniProtKB:D9IA45,
CC ECO:0000269|PubMed:8626278, ECO:0000269|PubMed:9257693,
CC ECO:0000269|PubMed:9790980};
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 ECO:0000269|PubMed:8621562, ECO:0000269|PubMed:8626278,
CC ECO:0000269|PubMed:9257693}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:8386371,
CC ECO:0000269|PubMed:9790980}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q8KS19, ECO:0000255, ECO:0000269|PubMed:8386371,
CC ECO:0000269|PubMed:9790980}.
CC -!- MASS SPECTROMETRY: Mass=32130; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:9257693};
CC -!- DISRUPTION PHENOTYPE: Microaerobically grown cells show 38% decrease in
CC cytochrome c oxadase complex activity. Between 0-5% nitrogen fixing
CC activity of the nitrogenase in root nodules when in symbiosis with
CC soybean. {ECO:0000269|PubMed:8621562}.
CC -!- SIMILARITY: Belongs to the CcoP / FixP family. {ECO:0000305}.
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DR EMBL; L07487; AAA26206.1; -; Genomic_DNA.
DR EMBL; AJ005001; CAA06282.1; -; Genomic_DNA.
DR EMBL; BA000040; BAC48031.1; -; Genomic_DNA.
DR PIR; D47468; D47468.
DR RefSeq; NP_769406.1; NC_004463.1.
DR RefSeq; WP_011085551.1; NZ_CP011360.1.
DR AlphaFoldDB; Q03075; -.
DR SMR; Q03075; -.
DR STRING; 224911.27351023; -.
DR EnsemblBacteria; BAC48031; BAC48031; BAC48031.
DR GeneID; 64022523; -.
DR KEGG; bja:blr2766; -.
DR PATRIC; fig|224911.44.peg.2387; -.
DR eggNOG; COG2010; Bacteria.
DR HOGENOM; CLU_047545_2_0_5; -.
DR InParanoid; Q03075; -.
DR OMA; DWLYGGE; -.
DR PhylomeDB; Q03075; -.
DR UniPathway; UPA00705; -.
DR Proteomes; UP000002526; 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 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Direct protein sequencing;
KW Electron transport; Heme; Hydrogen ion transport; Ion transport; Iron;
KW Membrane; Metal-binding; Oxidoreductase; Reference proteome; Repeat;
KW Respiratory chain; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..290
FT /note="Cbb3-type cytochrome c oxidase subunit FixP"
FT /id="PRO_0000412296"
FT TOPO_DOM 1..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q3J015, ECO:0000255"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..290
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q3J015, ECO:0000255"
FT DOMAIN 109..198
FT /note="Cytochrome c 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT DOMAIN 206..287
FT /note="Cytochrome c 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT BINDING 122
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 /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 /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 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 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 223
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 264
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 MUTAGEN 122
FT /note="C->S: 85% decrease in cytochrome c oxidase complex
FT activity and assembly defects of the complex; when
FT associated with S-125 or with S-125, S-219 and S-222. 85%
FT decrease in cytochrome c oxidase complex activity and
FT assembly defects of the complex."
FT /evidence="ECO:0000269|PubMed:9257693"
FT MUTAGEN 125
FT /note="C->S: 85% decrease in cytochrome c oxidase complex
FT activity and assembly defects of the complex; when
FT associated with S-122 or with S-122, S-219 and S-222. 85%
FT decrease in cytochrome c oxidase complex activity and
FT assembly defects of the complex."
FT /evidence="ECO:0000269|PubMed:9257693"
FT MUTAGEN 219
FT /note="C->S: 85% decrease in cytochrome c oxidase complex
FT activity and assembly defects of the complex; when
FT associated with S-222 or with S-222, S-122 and S-125. 85%
FT decrease in cytochrome c oxidase complex activity and
FT assembly defects of the complex."
FT /evidence="ECO:0000269|PubMed:9257693"
FT MUTAGEN 222
FT /note="C->S: 85% decrease in cytochrome c oxidase complex
FT activity and assembly defects of the complex; when
FT associated with S-219 or with S-219, S-122 and S-125. 85%
FT decrease in cytochrome c oxidase complex activity and
FT assembly defects of the complex."
FT /evidence="ECO:0000269|PubMed:9257693"
SQ SEQUENCE 290 AA; 31024 MW; 983F1B606D507BAC CRC64;
MTDHSEFDSV SGKTTTGHEW DGIKELNTPL PRWWVICFYL TIVWAIGYWI VYPAWPLISS
NTTGLFGYSS RADVAVELAN LEKIRGDKMA ALGAASLADV EKDPALLALA RAKGKTVFGD
NCAPCHGSGG AGAKGFPNLN DDDWLWGGTL DQIMQTIQFG ARSGHAKTHE GQMLAFGKDG
VLKGDEIVTV ANYVRSLSGL PTRKGYDAAK GEKIFVENCV ACHGDGGKGN QEMGAPNLTD
KIWLYGSDEA ALIETISQGR AGVMPAWEGR LDPSTIKAMA VYVHSLGGGK
