COX2_MYCLE
ID COX2_MYCLE Reviewed; 353 AA.
AC Q9CCF1;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Probable 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 Flags: Precursor;
GN Name=ctaC; OrderedLocusNames=ML0875;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC Note=Binds a copper A center. {ECO:0000250};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC {ECO:0000305}.
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DR EMBL; AL583920; CAC31256.1; -; Genomic_DNA.
DR PIR; E87018; E87018.
DR RefSeq; NP_301661.1; NC_002677.1.
DR RefSeq; WP_010907985.1; NC_002677.1.
DR AlphaFoldDB; Q9CCF1; -.
DR SMR; Q9CCF1; -.
DR STRING; 272631.ML0875; -.
DR EnsemblBacteria; CAC31256; CAC31256; CAC31256.
DR KEGG; mle:ML0875; -.
DR PATRIC; fig|272631.5.peg.1605; -.
DR Leproma; ML0875; -.
DR eggNOG; COG1622; Bacteria.
DR HOGENOM; CLU_036876_3_1_11; -.
DR OMA; HAFMPIA; -.
DR Proteomes; UP000000806; 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; 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.
PE 3: Inferred from homology;
KW Cell membrane; Copper; Electron transport; Membrane; Metal-binding;
KW Reference proteome; Respiratory chain; Signal; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..42
FT /evidence="ECO:0000255"
FT CHAIN 43..353
FT /note="Probable cytochrome c oxidase subunit 2"
FT /id="PRO_0000006056"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 246
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000255"
FT BINDING 287
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000255"
FT BINDING 291
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000255"
FT BINDING 295
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000255"
SQ SEQUENCE 353 AA; 39521 MW; AA6BFCAB69A27A20 CRC64;
MTARELVCSQ RVGQGLSRRL RPLVLAVTLG VLVVTLSGCS WSDALAIGWP EGITPEAHLN
RQLWIGAVVA SLVVGVIVWG LIFWSTIFHR KKTTDTELPR QFGYNMPLEL VLTVTPFLII
SMLFYFTVIV QDKMLYLAKD PEVVIDVTAF QWNWKFGYQR VDFKDGTLTY DGVDPARKKA
MVSKPEGKDS HGEELVGAVR GLNTEDRAYL NFDKVETLGT TTEIPVLVLP AGKRIEFQLN
SADVVHSFWV PKFLFKRDVM PNPVANNSVN VFQVEEITKT GAFVGHCAEM CGTYHSMMNF
EVRVVAPNDF KAYLQQRIDG KTNAEALQVI AQPPLAVTTH PFDTRRGQLT NSQ
