COX2_BACSU
ID COX2_BACSU Reviewed; 356 AA.
AC P24011; O34404;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Cytochrome c oxidase subunit 2;
DE EC=7.1.1.9;
DE AltName: Full=Caa-3605 subunit 2;
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=BSU14890;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=1847686; DOI=10.1111/j.1432-1033.1991.tb15732.x;
RA Saraste M., Metso T., Nakari T., Jalli T., Lauraeus M., van der Oost J.;
RT "The Bacillus subtilis cytochrome-c oxidase. Variations on a conserved
RT protein theme.";
RL Eur. J. Biochem. 195:517-525(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Bertero M., Presecan E., Glaser P., Richou A., Danchin A.;
RT "Bacillus subtilis chromosomal region downstream nprE.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
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 -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Note=Binds a copper A center.;
CC -!- COFACTOR:
CC Name=heme c; Xref=ChEBI:CHEBI:61717;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC {ECO:0000305}.
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DR EMBL; X54140; CAA38076.1; -; Genomic_DNA.
DR EMBL; Z98682; CAB11342.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13362.1; -; Genomic_DNA.
DR PIR; S14396; S14396.
DR RefSeq; NP_389372.1; NC_000964.3.
DR RefSeq; WP_003232248.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P24011; -.
DR SMR; P24011; -.
DR STRING; 224308.BSU14890; -.
DR TCDB; 3.D.4.4.1; the proton-translocating cytochrome oxidase (cox) superfamily.
DR PaxDb; P24011; -.
DR PRIDE; P24011; -.
DR DNASU; 936789; -.
DR EnsemblBacteria; CAB13362; CAB13362; BSU_14890.
DR GeneID; 936789; -.
DR KEGG; bsu:BSU14890; -.
DR PATRIC; fig|224308.179.peg.1624; -.
DR eggNOG; COG1622; Bacteria.
DR eggNOG; COG2010; Bacteria.
DR InParanoid; P24011; -.
DR OMA; KMTGTYP; -.
DR PhylomeDB; P24011; -.
DR BioCyc; BSUB:BSU14890-MON; -.
DR BioCyc; MetaCyc:BSU14890-MON; -.
DR SABIO-RK; P24011; -.
DR Proteomes; UP000001570; 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 GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IBA:GO_Central.
DR CDD; cd04213; CuRO_CcO_Caa3_II; 1.
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; IPR034236; CuRO_CcO_Caa3_II.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR014222; Cyt_c_oxidase_su2.
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 Pfam; PF02790; COX2_TM; 1.
DR Pfam; PF00034; Cytochrom_C; 1.
DR SUPFAM; SSF46626; SSF46626; 1.
DR SUPFAM; SSF49503; SSF49503; 1.
DR SUPFAM; SSF81464; SSF81464; 1.
DR TIGRFAMs; TIGR02866; CoxB; 1.
DR PROSITE; PS00078; COX2; 1.
DR PROSITE; PS50857; COX2_CUA; 1.
DR PROSITE; PS50999; COX2_TM; 1.
DR PROSITE; PS51007; CYTC; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Cell membrane; Copper; Electron transport; Heme; Iron; Lipoprotein;
KW Membrane; Metal-binding; Palmitate; Reference proteome; Respiratory chain;
KW Signal; Translocase; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 21..356
FT /note="Cytochrome c oxidase subunit 2"
FT /id="PRO_0000006051"
FT TOPO_DOM 21..47
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 107..356
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 258..356
FT /note="Cytochrome c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT REGION 21..257
FT /note="Cytochrome c oxidase subunit II"
FT BINDING 176
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000305"
FT BINDING 217
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000305"
FT BINDING 221
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000305"
FT BINDING 225
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000305"
FT BINDING 271
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000305"
FT BINDING 274
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000305"
FT BINDING 275
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT BINDING 329
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000305"
FT LIPID 21
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 21
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CONFLICT 257
FT /note="D -> H (in Ref. 1; CAA38076)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 356 AA; 40095 MW; DEF74EAF4C8414E9 CRC64;
MVKHWRLILL LALVPLLLSG CGKPFLSTLK PAGEVADKQY DLTVLSTLIM VVVVAVVSVI
FFYVIVRFRR SRVGENTIPK QVEGNKFLEI TWTVIPILLL IILVIPVVLY TLELADTSPM
DKKGRKAEDA LVVNVRANLY WWEFEYPDYG IITSQELIVP TDQRVYFNLK ASDVKHSFWI
PSVGGKLDTN TDNENKFFLT FDSKRSKEAG DMFFGKCAEL CGPSHALMDF KVKTMSAKEF
QGWTKEMKNY KSTAESDLAK QGEELFKEKN CLSCHAVEPN DKRAEAARTA PNLATFGERT
KVAGVKEANK ENVKAWLKDP DSIKPGNKMT GTYPKLSDSE TNALYEYLKG LKAESK
