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   27-MAR-2024, entry version 160.
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; Bacillota; 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   KEGG; bpf:BpOF4_00915; -.
DR   eggNOG; COG1622; Bacteria.
DR   eggNOG; COG2010; Bacteria.
DR   HOGENOM; CLU_036876_1_1_9; -.
DR   Proteomes; UP000001544; Chromosome.
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; Cupredoxins - blue copper proteins; 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   NCBIfam; TIGR02866; CoxB; 1.
DR   PANTHER; PTHR22888:SF10; CYTOCHROME C OXIDASE SUBUNIT 2; 1.
DR   PANTHER; PTHR22888; CYTOCHROME C OXIDASE, SUBUNIT II; 1.
DR   Pfam; PF00116; COX2; 1.
DR   Pfam; PF02790; COX2_TM; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR01166; CYCOXIDASEII.
DR   SUPFAM; SSF49503; Cupredoxins; 1.
DR   SUPFAM; SSF46626; Cytochrome c; 1.
DR   SUPFAM; SSF81464; Cytochrome c oxidase subunit II-like, transmembrane region; 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
//