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Database: UniProt/TrEMBL
Entry: Q0HDL3_SHESM
LinkDB: Q0HDL3_SHESM
Original site: Q0HDL3_SHESM 
ID   Q0HDL3_SHESM            Unreviewed;       513 AA.
AC   Q0HDL3;
DT   03-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2006, sequence version 1.
DT   19-MAR-2014, entry version 68.
DE   RecName: Full=Cytochrome c oxidase subunit 2;
DE            EC=1.9.3.1;
GN   OrderedLocusNames=Shewmr4_3791;
OS   Shewanella sp. (strain MR-4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=60480;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-4;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Nealson K., Konstantinidis K., Klappenbach J.,
RA   Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella sp. MR-4.";
RL   Submitted (AUG-2006) 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) (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.
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DR   EMBL; CP000446; ABI40854.1; -; Genomic_DNA.
DR   RefSeq; YP_735911.1; NC_008321.1.
DR   ProteinModelPortal; Q0HDL3; -.
DR   STRING; 60480.Shewmr4_3791; -.
DR   EnsemblBacteria; ABI40854; ABI40854; Shewmr4_3791.
DR   GeneID; 4254354; -.
DR   KEGG; she:Shewmr4_3791; -.
DR   PATRIC; 23584467; VBISheSp133532_3930.
DR   eggNOG; COG2010; -.
DR   HOGENOM; HOG000264987; -.
DR   KO; K02275; -.
DR   OMA; QWKWHYK; -.
DR   OrthoDB; EOG68SVXT; -.
DR   ProtClustDB; CLSK907729; -.
DR   BioCyc; SSP60480:GI2N-3929-MONOMER; -.
DR   GO; GO:0016021; C:integral component of 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:UniProtKB-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:InterPro.
DR   GO; GO:1902600; P:hydrogen ion transmembrane transport; IEA:GOC.
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-like_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   Pfam; PF13442; Cytochrome_CBB3; 2.
DR   SUPFAM; SSF46626; SSF46626; 2.
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; 2.
PE   3: Inferred from homology;
KW   Complete proteome; Copper; Electron transport; Membrane;
KW   Metal-binding; Oxidoreductase; Respiratory chain; Transmembrane;
KW   Transport.
SQ   SEQUENCE   513 AA;  55262 MW;  9EDF016A69620682 CRC64;
     MKQWLYCLLV VLFAPPLPAA DMRFNMTPGV TEISGKVYHL HMTILYICCA IGLVVFGVMI
     YAMINHRKSK GAVASHFHES TKVEIAWTII PFVILILMAI PATKTLIAME DPSNADLTVK
     VTGSQWKWHY SYFDQDIDFY SILATPRPQI EGSEAKGEHY LLEVDKPLVL PINRKIRFLM
     TSEDVIHSWW MPAFAVKKDA NPGFINEAWT RIDKPGIYRG QCAELCGKDH GFMPIVVQAL
     PEAEFDAWVE EQKQAANAAA QAAQAALSQT LTKEELMAQG EQVYLGHCAA CHQPNGEGLQ
     GVFPHLKGSP IATGPLSGHL EIVLNGKAGT AMQAFGKQLT AQEIAAVVTY ERNAWGNNTG
     DAVQAKDVDA HKSGGTNSEP VATTPPPATT DAPKPATEPA ASVDPASLPT LSHDELMAEG
     EKTYATICAA CHQLTGAGMP PAFPALAGSA IATGPVANHI DIVMHGKPGT AMQAFGTQLT
     PQQLAAIITY ERNAWGNNTG DTVQPADIAR HGQ
//
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