COX2_THET8
ID COX2_THET8 Reviewed; 168 AA.
AC Q5SJ80;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Cytochrome c oxidase subunit 2;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome c ba(3) subunit II;
DE AltName: Full=Cytochrome c oxidase polypeptide II;
DE AltName: Full=Cytochrome cba3 subunit 2;
GN Name=cbaB; Synonyms=ctaC; OrderedLocusNames=TTHA1134;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-30.
RX PubMed=7657607; DOI=10.1074/jbc.270.35.20345;
RA Keightley J.A., Zimmermann B.H., Mather M.W., Springer P., Pastuszyn A.,
RA Lawrence D.M., Fee J.A.;
RT "Molecular genetic and protein chemical characterization of the cytochrome
RT ba3 from Thermus thermophilus HB8.";
RL J. Biol. Chem. 270:20345-20358(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=10775261; DOI=10.1093/emboj/19.8.1766;
RA Soulimane T., Buse G., Bourenkov G.P., Bartunik H.D., Huber R., Than M.E.;
RT "Structure and mechanism of the aberrant ba3-cytochrome c oxidase from
RT Thermus thermophilus.";
RL EMBO J. 19:1766-1776(2000).
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).
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 -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC {ECO:0000305}.
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DR EMBL; L09121; AAB00369.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD70957.1; -; Genomic_DNA.
DR PIR; T52480; T52480.
DR RefSeq; WP_011173203.1; NC_006461.1.
DR RefSeq; YP_144400.1; NC_006461.1.
DR PDB; 1EHK; X-ray; 2.40 A; B=1-168.
DR PDB; 2QPD; X-ray; 3.25 A; B=1-168.
DR PDB; 2QPE; X-ray; 2.90 A; B=1-168.
DR PDB; 3BVD; X-ray; 3.37 A; B=1-168.
DR PDB; 3EH3; X-ray; 3.10 A; B=3-168.
DR PDB; 3EH4; X-ray; 2.90 A; B=3-168.
DR PDB; 3EH5; X-ray; 2.80 A; B=3-168.
DR PDB; 3QJQ; X-ray; 2.90 A; B=1-168.
DR PDB; 3QJR; X-ray; 3.20 A; B=1-168.
DR PDB; 3QJS; X-ray; 2.80 A; B=1-168.
DR PDB; 3QJT; X-ray; 2.95 A; B=1-168.
DR PDB; 3QJU; X-ray; 2.90 A; B=1-168.
DR PDB; 3QJV; X-ray; 2.80 A; B=1-168.
DR PDB; 3S33; X-ray; 4.45 A; B=3-168.
DR PDB; 3S38; X-ray; 4.20 A; B=3-168.
DR PDB; 3S39; X-ray; 4.80 A; B=3-168.
DR PDB; 3S3A; X-ray; 4.25 A; B=3-168.
DR PDB; 3S3B; X-ray; 3.30 A; B=3-168.
DR PDB; 3S3C; X-ray; 4.00 A; B=3-168.
DR PDB; 3S3D; X-ray; 3.75 A; B=3-168.
DR PDB; 3S8F; X-ray; 1.80 A; B=1-168.
DR PDB; 3S8G; X-ray; 1.80 A; B=1-168.
DR PDB; 4FA7; X-ray; 2.50 A; B=1-168.
DR PDB; 4FAA; X-ray; 2.80 A; B=1-168.
DR PDB; 4G70; X-ray; 2.60 A; B=1-168.
DR PDB; 4G71; X-ray; 2.90 A; B=1-168.
DR PDB; 4G72; X-ray; 3.19 A; B=1-168.
DR PDB; 4G7Q; X-ray; 2.60 A; B=1-168.
DR PDB; 4G7R; X-ray; 3.05 A; B=1-168.
DR PDB; 4G7S; X-ray; 2.00 A; B=1-168.
DR PDB; 4GP4; X-ray; 2.80 A; B=1-168.
DR PDB; 4GP5; X-ray; 2.70 A; B=1-168.
DR PDB; 4GP8; X-ray; 2.80 A; B=1-168.
DR PDB; 4N4Y; X-ray; 2.90 A; B=1-168.
DR PDB; 5NDC; X-ray; 2.30 A; B=1-168.
DR PDB; 5U7N; X-ray; 2.30 A; A/B/C/D/E/F/G/H=44-149, A/B/C/D/E/F/G/H=160-168.
DR PDB; 6PTT; X-ray; 1.84 A; A/B=44-168.
DR PDB; 6PTY; X-ray; 1.98 A; A/B=44-168.
DR PDBsum; 1EHK; -.
DR PDBsum; 2QPD; -.
DR PDBsum; 2QPE; -.
DR PDBsum; 3BVD; -.
DR PDBsum; 3EH3; -.
DR PDBsum; 3EH4; -.
DR PDBsum; 3EH5; -.
DR PDBsum; 3QJQ; -.
DR PDBsum; 3QJR; -.
DR PDBsum; 3QJS; -.
DR PDBsum; 3QJT; -.
DR PDBsum; 3QJU; -.
DR PDBsum; 3QJV; -.
DR PDBsum; 3S33; -.
DR PDBsum; 3S38; -.
DR PDBsum; 3S39; -.
DR PDBsum; 3S3A; -.
DR PDBsum; 3S3B; -.
DR PDBsum; 3S3C; -.
DR PDBsum; 3S3D; -.
DR PDBsum; 3S8F; -.
DR PDBsum; 3S8G; -.
DR PDBsum; 4FA7; -.
DR PDBsum; 4FAA; -.
DR PDBsum; 4G70; -.
DR PDBsum; 4G71; -.
DR PDBsum; 4G72; -.
DR PDBsum; 4G7Q; -.
DR PDBsum; 4G7R; -.
DR PDBsum; 4G7S; -.
DR PDBsum; 4GP4; -.
DR PDBsum; 4GP5; -.
DR PDBsum; 4GP8; -.
DR PDBsum; 4N4Y; -.
DR PDBsum; 5NDC; -.
DR PDBsum; 5U7N; -.
DR PDBsum; 6PTT; -.
DR PDBsum; 6PTY; -.
DR AlphaFoldDB; Q5SJ80; -.
DR BMRB; Q5SJ80; -.
DR SMR; Q5SJ80; -.
DR STRING; 300852.55772516; -.
DR DrugBank; DB02451; B-nonylglucoside.
DR TCDB; 3.D.4.2.1; the proton-translocating cytochrome oxidase (cox) superfamily.
DR EnsemblBacteria; BAD70957; BAD70957; BAD70957.
DR GeneID; 3169672; -.
DR KEGG; ttj:TTHA1134; -.
DR PATRIC; fig|300852.9.peg.1113; -.
DR eggNOG; COG1622; Bacteria.
DR HOGENOM; CLU_120355_0_0_0; -.
DR OMA; FICHEYC; -.
DR PhylomeDB; Q5SJ80; -.
DR BioCyc; MetaCyc:MON-21001; -.
DR BRENDA; 7.1.1.9; 2305.
DR EvolutionaryTrace; Q5SJ80; -.
DR Proteomes; UP000000532; 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 CDD; cd13913; ba3_CcO_II_C; 1.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR034214; Ba3_CcO_II_C.
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 InterPro; IPR015209; Cyt_c_oxidase_su2a_TM_dom.
DR Pfam; PF00116; COX2; 1.
DR Pfam; PF09125; COX2-transmemb; 1.
DR SUPFAM; SSF49503; SSF49503; 1.
DR SUPFAM; SSF81464; SSF81464; 1.
DR PROSITE; PS00078; COX2; 1.
DR PROSITE; PS50857; COX2_CUA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Copper; Direct protein sequencing;
KW Electron transport; Membrane; Metal-binding; Reference proteome;
KW Respiratory chain; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..168
FT /note="Cytochrome c oxidase subunit 2"
FT /id="PRO_0000183722"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT TRANSMEM 4..38
FT /note="Helical"
FT TOPO_DOM 39..168
FT /note="Periplasmic"
FT BINDING 114
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT BINDING 149
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT BINDING 153
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT BINDING 157
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT HELIX 4..36
FT /evidence="ECO:0007829|PDB:3S8F"
FT HELIX 40..44
FT /evidence="ECO:0007829|PDB:3S8F"
FT TURN 55..60
FT /evidence="ECO:0007829|PDB:3S8F"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:3QJT"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:3S8F"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:3S8F"
FT STRAND 78..86
FT /evidence="ECO:0007829|PDB:3S8F"
FT STRAND 89..98
FT /evidence="ECO:0007829|PDB:3S8F"
FT STRAND 101..108
FT /evidence="ECO:0007829|PDB:3S8F"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:3S8F"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:3S8F"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:3S8F"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:3S8F"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:3S8F"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:3S8F"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:3S8F"
SQ SEQUENCE 168 AA; 18563 MW; FE5689FB7672CF05 CRC64;
MVDEHKAHKA ILAYEKGWLA FSLAMLFVFI ALIAYTLATH TAGVIPAGKL ERVDPTTVRQ
EGPWADPAQA VVQTGPNQYT VYVLAFAFGY QPNPIEVPQG AEIVFKITSP DVIHGFHVEG
TNINVEVLPG EVSTVRYTFK RPGEYRIICN QYCGLGHQNM FGTIVVKE
