COX2_CORGL
ID COX2_CORGL Reviewed; 359 AA.
AC Q8NNK2; Q6M3N8; Q93HZ4;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Cytochrome c oxidase subunit 2;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome aa3 subunit 2;
DE AltName: Full=Cytochrome c oxidase polypeptide II;
DE AltName: Full=Oxidase aa(3) subunit 2;
DE Flags: Precursor;
GN Name=ctaC; OrderedLocusNames=Cgl2195, cg2409;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 29-50, SUBUNIT, HEME
RP CHARACTERIZATION, DIACYLGLYCEROL AT CYS-29, AND MASS SPECTROMETRY.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=11577165; DOI=10.1099/00221287-147-10-2865;
RA Sakamoto J., Shibata T., Mine T., Miyahara R., Torigoe T., Noguchi S.,
RA Matsushita K., Sone N.;
RT "Cytochrome c oxidase contains an extra charged amino acid cluster in a new
RT type of respiratory chain in the amino acid-producing Gram-positive
RT bacterium Corynebacterium glutamicum.";
RL Microbiology 147:2865-2871(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
RN [4]
RP DETECTION IN A SUPERCOMPLEX WITH MENAQUINOL-CYTOCHROME C REDUCTASE
RP (CYTOCHROME BC1).
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12446663; DOI=10.1074/jbc.m210499200;
RA Niebisch A., Bott M.;
RT "Purification of a cytochrome bc1-aa3 supercomplex with quinol oxidase
RT activity from Corynebacterium glutamicum. Identification of a fourth
RT subunity of cytochrome aa3 oxidase and mutational analysis of diheme
RT cytochrome c1.";
RL J. Biol. Chem. 278:4339-4346(2003).
CC -!- FUNCTION: Subunits I and II form the functional core of the enzyme
CC complex. Electrons originating in cytochrome c are transferred via heme
CC a and Cu(A) to the binuclear center formed by heme a3 and Cu(B) (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-
CC [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034; EC=7.1.1.9;
CC -!- COFACTOR:
CC Name=binuclear copper center (CuA); Xref=ChEBI:CHEBI:47357;
CC Evidence={ECO:0000250};
CC Note=Binds a binuclear copper A center per subunit. {ECO:0000250};
CC -!- SUBUNIT: Associates with subunits I, III and IV to form cytochrome c
CC oxidase. The 4 subunit cytochrome c oxidase forms a supercomplex with
CC the menaquinol-cytochrome c reductase complex (cytochrome bc1).
CC {ECO:0000269|PubMed:11577165}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- MASS SPECTROMETRY: Mass=37314.7; Mass_error=83.2; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:11577165};
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC {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; AB052749; BAB64407.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB99588.1; -; Genomic_DNA.
DR EMBL; BX927154; CAF20536.1; -; Genomic_DNA.
DR RefSeq; NP_601399.1; NC_003450.3.
DR RefSeq; WP_011014951.1; NC_006958.1.
DR PDB; 7Q21; EM; 3.00 A; G/g=1-359.
DR PDBsum; 7Q21; -.
DR AlphaFoldDB; Q8NNK2; -.
DR SMR; Q8NNK2; -.
DR STRING; 196627.cg2409; -.
DR TCDB; 3.D.4.4.2; the proton-translocating cytochrome oxidase (cox) superfamily.
DR KEGG; cgb:cg2409; -.
DR KEGG; cgl:Cgl2195; -.
DR PATRIC; fig|196627.13.peg.2131; -.
DR eggNOG; COG1622; Bacteria.
DR HOGENOM; CLU_036876_3_1_11; -.
DR OMA; HAFMPIA; -.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.287.90; -; 1.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR045187; CcO_II.
DR InterPro; IPR002429; CcO_II-like_C.
DR InterPro; IPR001505; Copper_CuA.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom.
DR InterPro; IPR036257; Cyt_c_oxidase_su2_TM_sf.
DR PANTHER; PTHR22888; PTHR22888; 1.
DR Pfam; PF00116; COX2; 1.
DR SUPFAM; SSF49503; SSF49503; 1.
DR SUPFAM; SSF81464; SSF81464; 1.
DR PROSITE; PS00078; COX2; 1.
DR PROSITE; PS50857; COX2_CUA; 1.
DR PROSITE; PS50999; COX2_TM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Copper; Direct protein sequencing;
KW Electron transport; Lipoprotein; Membrane; Metal-binding;
KW Reference proteome; Respiratory chain; Signal; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:11577165"
FT CHAIN 29..359
FT /note="Cytochrome c oxidase subunit 2"
FT /id="PRO_0000006054"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 168..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 244
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250"
FT BINDING 285
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250"
FT BINDING 287
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250"
FT BINDING 289
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250"
FT BINDING 289
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250"
FT BINDING 293
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250"
FT SITE 29
FT /note="Not N-palmitoylated"
FT /evidence="ECO:0000269|PubMed:11577165"
FT LIPID 29
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000269|PubMed:11577165"
FT CONFLICT 69
FT /note="W -> C (in Ref. 1; BAB64407)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="E -> V (in Ref. 1; BAB64407)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 359 AA; 39632 MW; 5BB65F6AB2BE493A CRC64;
MEQQNKRGLK RKALLGGVLG LGGLAMAGCE VAPPGGVLGD FLRMGWPDGI TPEAVAMGNF
WSWVWVAAWI IGIIMWGLFL TAIFAWGAKR AEKRGEGEFP KQLQYNVPLE LVLTIVPIII
VMVLFFFTVQ TQDKVTALDK NPEVTVDVTA YQWNWKFGYS EIDGSLAPGG QDYQGSDPER
QAAAEASKKD PSGDNPIHGN SKSDVSYLEF NRIETLGTTD EIPVMVLPVN TPIEFNLASA
DVAHSFWVPE FLFKRDAYAH PEANKSQRVF QIEEITEEGA FVGRCAEMCG TYHAMMNFEL
RVVDRDSFAE YISFRDSNPD ATNAQALEHI GQAPYATSTS PFVSDRTATR DGENTQSNA
