(data stored in ACNUC7421 zone)

SWISSPROT: B4STH2_STRM5

ID   B4STH2_STRM5            Unreviewed;       320 AA.
AC   B4STH2;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 74.
DE   RecName: Full=Cytochrome c oxidase subunit 2 {ECO:0000256|RuleBase:RU004024};
DE            EC=1.9.3.1 {ECO:0000256|RuleBase:RU004024};
DE   Flags: Precursor;
GN   OrderedLocusNames=Smal_0310 {ECO:0000313|EMBL:ACF50015.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF50015.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF50015.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF50015.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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:
CC       Reaction=4 [Fe(II)cytochrome c] + 4 H(+) + O2 = 4
CC         [Fe(III)cytochrome c] + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA-
CC         COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC         ChEBI:CHEBI:29034; EC=1.9.3.1;
CC         Evidence={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; CP001111; ACF50015.1; -; Genomic_DNA.
DR   RefSeq; WP_012509833.1; NC_011071.1.
DR   STRING; 391008.Smal_0310; -.
DR   EnsemblBacteria; ACF50015; ACF50015; Smal_0310.
DR   KEGG; smt:Smal_0310; -.
DR   eggNOG; ENOG4105CV4; Bacteria.
DR   eggNOG; COG1622; LUCA.
DR   HOGENOM; HOG000264988; -.
DR   KO; K02275; -.
DR   OMA; HSEMLFN; -.
DR   OrthoDB; 1654242at2; -.
DR   BioCyc; SMAL391008:SMAL_RS01625-MONOMER; -.
DR   Proteomes; UP000001867; 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   CDD; cd13912; CcO_II_C; 1.
DR   Gene3D; 1.10.287.90; -; 1.
DR   Gene3D; 2.60.40.420; -; 1.
DR   InterPro; IPR002429; CcO_II-like_C.
DR   InterPro; IPR034210; CcO_II_C.
DR   InterPro; IPR001505; Copper_CuA.
DR   InterPro; IPR008972; Cupredoxin.
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   Pfam; PF00116; COX2; 1.
DR   Pfam; PF02790; COX2_TM; 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.
PE   3: Inferred from homology;
DR   PRODOM; B4STH2.
DR   SWISS-2DPAGE; B4STH2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW   Copper {ECO:0000256|RuleBase:RU004024};
KW   Electron transport {ECO:0000256|RuleBase:RU000456};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|RuleBase:RU004024};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000456,
KW   ECO:0000313|EMBL:ACF50015.1};
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     30       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        31    320       Cytochrome c oxidase subunit 2.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002826404.
FT   TRANSMEM     59     80       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    101    119       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       34    129       COX2_TM. {ECO:0000259|PROSITE:PS50999}.
FT   DOMAIN      130    272       COX2_CUA. {ECO:0000259|PROSITE:PS50857}.
SQ   SEQUENCE   320 AA;  34609 MW;  DF3709B182F9D1C1 CRC64;
     MKQSRGWGTK CVAMVATMAA LLSMPGTALA QAADPKPWQL NMGKGVTQTS RLAWESNNLS
     LIVCTVIGVI VFGAMAYAMF KFRKSKGAVA ATFSHNTKAE IIWTVIPVII LVVMAWPATA
     NLIKMYDTRD AEMTVKVTGY QWMWKYEYLG ENVTFTSRLD RESDRVRQSG VVPTRESHPH
     YLLDVDNRLV LPVDTKVRFV ITSDDVIHAW WVPALGWKQD AIPGFINEAW TSIEQPGVYR
     GQCAELCGKD HGFMPIVVEA VSKEEFKQWL AQRKPAPPAG PATPAAPAEP AAPAAPASEA
     PAAPAAAEAG SAPATAASGA
//

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