(data stored in ACNUC7421 zone)

SWISSPROT: A0A0H2ZK39_PSEAB

ID   A0A0H2ZK39_PSEAB        Unreviewed;       374 AA.
AC   A0A0H2ZK39;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   07-JUN-2017, entry version 11.
DE   RecName: Full=Cytochrome c oxidase subunit 2 {ECO:0000256|RuleBase:RU004024};
DE            EC=1.9.3.1 {ECO:0000256|RuleBase:RU004024};
GN   Name=coxB {ECO:0000313|EMBL:ABJ15062.1};
GN   OrderedLocusNames=PA14_01290 {ECO:0000313|EMBL:ABJ15062.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ15062.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ15062.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ15062.1,
RC   ECO:0000313|Proteomes:UP000000653};
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
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). {ECO:0000256|RuleBase:RU004024}.
CC   -!- CATALYTIC ACTIVITY: 4 ferrocytochrome c + O(2) + 4 H(+) = 4
CC       ferricytochrome c + 2 H(2)O. {ECO:0000256|RuleBase:RU004024}.
CC   -!- COFACTOR:
CC       Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC         Evidence={ECO:0000256|RuleBase:RU004024};
CC       Note=Binds a copper A center. {ECO:0000256|RuleBase:RU004024};
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000256|RuleBase:RU000456}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU000456}.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC       {ECO:0000256|RuleBase:RU000456}.
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DR   EMBL; CP000438; ABJ15062.1; -; Genomic_DNA.
DR   RefSeq; WP_003101203.1; NC_008463.1.
DR   ProteinModelPortal; A0A0H2ZK39; -.
DR   SMR; A0A0H2ZK39; -.
DR   EnsemblBacteria; ABJ15062; ABJ15062; PA14_01290.
DR   KEGG; pau:PA14_01290; -.
DR   KO; K02275; -.
DR   OMA; HAFMPIA; -.
DR   Proteomes; UP000000653; 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: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:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:InterPro.
DR   Gene3D; 1.10.760.10; -; 1.
DR   Gene3D; 2.60.40.420; -; 1.
DR   InterPro; IPR002429; CcO_II-like_C.
DR   InterPro; IPR001505; Copper_CuA.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR014222; Cyt_c_oxidase_su2.
DR   InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom.
DR   Pfam; PF00116; COX2; 1.
DR   Pfam; PF02790; COX2_TM; 1.
DR   Pfam; PF13442; Cytochrome_CBB3; 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.
PE   3: Inferred from homology;
DR   PRODOM; A0A0H2ZK39.
DR   SWISS-2DPAGE; A0A0H2ZK39.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000653};
KW   Copper {ECO:0000256|RuleBase:RU004024};
KW   Electron transport {ECO:0000256|RuleBase:RU000456};
KW   Heme {ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Iron {ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00433,
KW   ECO:0000256|RuleBase:RU004024};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000456};
KW   Respiratory chain {ECO:0000256|RuleBase:RU000456};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|RuleBase:RU000456,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|RuleBase:RU000456}.
FT   SIGNAL        1     22       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        23    374       Cytochrome c oxidase subunit 2.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002603441.
FT   TRANSMEM     46     66       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     87    105       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       20    115       COX2_TM. {ECO:0000259|PROSITE:PS50999}.
FT   DOMAIN      116    253       COX2_CUA. {ECO:0000259|PROSITE:PS50857}.
FT   DOMAIN      273    353       Cytochrome c. {ECO:0000259|PROSITE:
FT                                PS51007}.
SQ   SEQUENCE   374 AA;  42205 MW;  D4381A5269E47375 CRC64;
     MLRHPRVWMG FLLLSAISQA NAAWTVNMAP GATEVSRSVF DLHMTIFWIC VVIGVLVFGA
     MFWSMIVHRR STGQQPAHFH ESTTVEILWT VVPFVILVVM AVPATRTLIH IYDTSEPELD
     VQVTGYQWKW QYKYLGQDVE YFSNLATPQD QIHNRQAKDE HYLLEVDEPL VLPVGTKVRF
     LITSSDVIHS WWVPAFAVKR DAIPGFVNEA WTKVDEPGIY RGQCAELCGK DHGFMPIVVD
     VKPKAEFDQW LAKRKEEAAK VKELTSKEWT KEELVARGDK VYHTICAACH QAEGQGMPPM
     FPALKGSKIV TGPKEHHLEV VFNGVPGTAM AAFGKQLNEV DLAAVITYER NAWGNDDGDM
     VTPKDVVAYK QKQQ
//

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