COX2_ALKPO
ID COX2_ALKPO Reviewed; 342 AA.
AC Q04441; D3FU50;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 154.
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=BpOF4_00915;
OS Alkalihalophilus pseudofirmus (strain ATCC BAA-2126 / JCM 17055 / OF4)
OS (Bacillus pseudofirmus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalophilus.
OX NCBI_TaxID=398511;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 23-48.
RX PubMed=7678007; DOI=10.1016/s0021-9258(18)54205-8;
RA Quirk P.G., Hicks D.B., Krulwich T.A.;
RT "Cloning of the cta operon from alkaliphilic Bacillus firmus OF4 and
RT characterization of the pH-regulated cytochrome caa3 oxidase it encodes.";
RL J. Biol. Chem. 268:678-685(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2126 / JCM 17055 / OF4;
RX PubMed=21951522; DOI=10.1111/j.1462-2920.2011.02591.x;
RA Janto B., Ahmed A., Ito M., Liu J., Hicks D.B., Pagni S., Fackelmayer O.J.,
RA Smith T.A., Earl J., Elbourne L.D., Hassan K., Paulsen I.T., Kolsto A.B.,
RA Tourasse N.J., Ehrlich G.D., Boissy R., Ivey D.M., Li G., Xue Y., Ma Y.,
RA Hu F.Z., Krulwich T.A.;
RT "Genome of alkaliphilic Bacillus pseudofirmus OF4 reveals adaptations that
RT support the ability to grow in an external pH range from 7.5 to 11.4.";
RL Environ. Microbiol. 13:3289-3309(2011).
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; M94110; AAA22364.1; -; Genomic_DNA.
DR EMBL; CP001878; ADC48252.1; -; Genomic_DNA.
DR RefSeq; WP_012959534.1; NC_013791.2.
DR AlphaFoldDB; Q04441; -.
DR SMR; Q04441; -.
DR STRING; 398511.BpOF4_00915; -.
DR EnsemblBacteria; ADC48252; ADC48252; BpOF4_00915.
DR KEGG; bpf:BpOF4_00915; -.
DR eggNOG; COG1622; Bacteria.
DR eggNOG; COG2010; Bacteria.
DR HOGENOM; CLU_036876_1_1_9; -.
DR OMA; KMTGTYP; -.
DR OrthoDB; 1654242at2; -.
DR Proteomes; UP000001544; 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 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 1: Evidence at protein level;
KW Cell membrane; Copper; Direct protein sequencing; Electron transport; Heme;
KW Iron; Lipoprotein; Membrane; Metal-binding; Palmitate; Reference proteome;
KW Respiratory chain; Signal; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303,
FT ECO:0000269|PubMed:7678007"
FT CHAIN 23..342
FT /note="Cytochrome c oxidase subunit 2"
FT /id="PRO_0000006049"
FT TOPO_DOM 23..50
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..342
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 250..342
FT /note="Cytochrome c"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT REGION 23..249
FT /note="Cytochrome c oxidase subunit II"
FT BINDING 175
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000305"
FT BINDING 210
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000305"
FT BINDING 214
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000305"
FT BINDING 218
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000305"
FT BINDING 264
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000305"
FT BINDING 267
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /note="covalent"
FT /evidence="ECO:0000305"
FT BINDING 268
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 317
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 23
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 23
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 342 AA; 38142 MW; F777C7D1FE44A429 CRC64;
MKLWKTASRF LPLSFLTLFL TGCLGEENLT ALDPKGPQAQ WIYDNMILSI IVMALVSIVV
FAIFFIILAK YRRKPGDDEI PKQVHGNTAL EITWTVIPII LLVILAVPTI TGTFMFADKD
PDPEVGDNTV YIKVTGHQFW WQFDYENEGF TAGQDVYIPV GEKVIFELHA QDVLHSFWVP
ALGGKIDTVP GITNHMWLEA DEPGVFKGKC AELCGPSHAL MDFKLIALER DEYDAWVEGM
SAEVEEPTET LANQGRQVFE ENSCIGCHAV GGTGTAAGPA FTNFGEREVI AGYLENNDEN
LEAWIRDPQS LKQGNVMPAY PDMSEEDMEA LIAYLRSLKV ME
