ID C1DA52_LARHH Unreviewed; 371 AA.
AC C1DA52;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 01-MAY-2013, entry version 32.
DE RecName: Full=Cytochrome c oxidase subunit 2;
DE EC=1.9.3.1;
GN Name=coxB; OrderedLocusNames=LHK_00169;
OS Laribacter hongkongensis (strain HLHK9).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC Neisseriaceae; Laribacter.
OX NCBI_TaxID=557598;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLHK9;
RX PubMed=19283063; DOI=10.1371/journal.pgen.1000416;
RA Woo P.C.Y., Lau S.K.P., Tse H., Teng J.L.L., Curreem S.O.,
RA Tsang A.K.L., Fan R.Y.Y., Wong G.K.M., Huang Y., Loman N.J.,
RA Snyder L.A.S., Cai J.J., Huang J.-D., Mak W., Pallen M.J., Lok S.,
RA Yuen K.-Y.;
RT "The complete genome and proteome of Laribacter hongkongensis reveal
RT potential mechanisms for adaptations to different temperatures and
RT habitats.";
RL PLoS Genet. 5:E1000416-E1000416(2009).
CC -!- FUNCTION: Subunits I and II form the functional core of the enzyme
CC complex. Electrons originating in cytochrome c are transferred via
CC heme a and Cu(A) to the binuclear center formed by heme a3 and
CC Cu(B) (By similarity).
CC -!- CATALYTIC ACTIVITY: 4 ferrocytochrome c + O(2) + 4 H(+) = 4
CC ferricytochrome c + 2 H(2)O.
CC -!- COFACTOR: Copper A (By similarity).
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC similarity).
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; CP001154; ACO73165.1; -; Genomic_DNA.
DR RefSeq; YP_002794174.1; NC_012559.1.
DR STRING; 557598.LHK_00169; -.
DR EnsemblBacteria; ACO73165; ACO73165; LHK_00169.
DR GeneID; 7755797; -.
DR KEGG; lhk:LHK_00169; -.
DR PATRIC; 22297463; VBILarHon49832_0167.
DR eggNOG; COG2010; -.
DR HOGENOM; HOG000264987; -.
DR KO; K02275; -.
DR OMA; WGNNTGD; -.
DR ProtClustDB; CLSK2485299; -.
DR BioCyc; LHON557598:GHO5-169-MONOMER; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:EC.
DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR Gene3D; 1.10.287.90; -; 1.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR001505; Copper_CuA.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR009056; Cyt_c_dom.
DR InterPro; IPR014222; Cyt_c_oxidase_su2.
DR InterPro; IPR002429; Cyt_c_oxidase_su2_C.
DR InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom.
DR Pfam; PF00116; COX2; 1.
DR Pfam; PF02790; COX2_TM; 1.
DR SUPFAM; SSF49503; Cupredoxin; 1.
DR SUPFAM; SSF81464; Cyt_c_oxidase_II-like_TM; 1.
DR SUPFAM; SSF46626; Cytochrome_c; 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.
PE 3: Inferred from homology;
KW Complete proteome; Copper; Electron transport; Metal-binding;
KW Oxidoreductase; Respiratory chain; Transmembrane; Transport.
SQ SEQUENCE 371 AA; 40736 MW; 774E0236566E8C21 CRC64;
MHRLSAVPLS LLLLGSRPAM AEWQLNLQPP ATELAGRIFN LHSLLLLICA GIFFGVLGVM
FYAIFRHRKA AGHTARHFHE NPWVEVLWTV IPFLILIGIA VPATRMVLAQ KDASGAELTI
KATGYQWKWG YEYVGEGVQF MSHLATPRAQ LTGQEGKSAH YLLEVDEPLV VPVGQKVRLL
LTANDVIHSW WVPALGVKQD AIPGFVRDAW FKIDRPGIYR GQCTELCGKD HGFMPIVVDA
RTPKDYAAWL TARKQAVADD PGKVWTMPEL RARGEKVFQQ NCMACHQADG RGIPGSFPAL
AGSRIATGDP AAHIEIVLYG SKKNPAMAAF GRQLSDTDIA AVITYERNAF GNQTGQMIEP
ARIAAARQGK G
//
