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COPA_PSESM
ID   COPA_PSESM              Reviewed;         589 AA.
AC   P59571;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   11-APR-2003, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Copper resistance protein A homolog;
DE   Flags: Precursor;
GN   Name=copA; OrderedLocusNames=PSPTO_3914;
OS   Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=223283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-871 / DC3000;
RX   PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA   Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA   Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA   Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA   Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA   Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA   Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA   Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA   Collmer A.;
RT   "The complete genome sequence of the Arabidopsis and tomato pathogen
RT   Pseudomonas syringae pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
CC   -!- FUNCTION: Could be involved in copper resistance. May have oxidase
CC       activity (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has not been experimentally proven.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family. CopA subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE016853; AAO57380.1; -; Genomic_DNA.
DR   RefSeq; NP_793685.1; NC_004578.1.
DR   RefSeq; WP_011104780.1; NC_004578.1.
DR   AlphaFoldDB; P59571; -.
DR   SMR; P59571; -.
DR   STRING; 223283.PSPTO_3914; -.
DR   EnsemblBacteria; AAO57380; AAO57380; PSPTO_3914.
DR   GeneID; 1185587; -.
DR   KEGG; pst:PSPTO_3914; -.
DR   PATRIC; fig|223283.9.peg.4013; -.
DR   eggNOG; COG2132; Bacteria.
DR   HOGENOM; CLU_009100_5_2_6; -.
DR   OMA; WNQMRMS; -.
DR   OrthoDB; 971126at2; -.
DR   PhylomeDB; P59571; -.
DR   Proteomes; UP000002515; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd13848; CuRO_1_CopA; 1.
DR   CDD; cd13874; CuRO_2_CopA; 1.
DR   CDD; cd13896; CuRO_3_CopA; 1.
DR   Gene3D; 2.60.40.420; -; 3.
DR   InterPro; IPR001117; Cu-oxidase.
DR   InterPro; IPR011706; Cu-oxidase_C.
DR   InterPro; IPR045087; Cu-oxidase_fam.
DR   InterPro; IPR011707; Cu-oxidase_N.
DR   InterPro; IPR006376; Cu-R_CopA.
DR   InterPro; IPR033138; Cu_oxidase_CS.
DR   InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR034284; CuRO_1_CopA.
DR   InterPro; IPR034282; CuRO_2_CopA.
DR   InterPro; IPR034279; CuRO_3_CopA.
DR   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR019546; TAT_signal_bac_arc.
DR   PANTHER; PTHR11709; PTHR11709; 1.
DR   Pfam; PF00394; Cu-oxidase; 1.
DR   Pfam; PF07731; Cu-oxidase_2; 1.
DR   Pfam; PF07732; Cu-oxidase_3; 1.
DR   SUPFAM; SSF49503; SSF49503; 3.
DR   TIGRFAMs; TIGR01480; copper_res_A; 1.
DR   TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR   PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
DR   PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Copper; Metal-binding; Oxidoreductase; Periplasm; Reference proteome;
KW   Repeat; Signal.
FT   SIGNAL          1..32
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT   CHAIN           33..589
FT                   /note="Copper resistance protein A homolog"
FT                   /id="PRO_0000002948"
FT   REPEAT          367..374
FT                   /note="1"
FT   REPEAT          396..403
FT                   /note="2"
FT   REGION          367..403
FT                   /note="2 X 8 AA tandem repeats of D-H-X-X-M-X-G-M"
FT   BINDING         100
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
FT                   /note="type 2 copper site"
FT                   /evidence="ECO:0000250"
FT   BINDING         102
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="2"
FT                   /note="type 3 copper site"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="2"
FT                   /note="type 3 copper site"
FT                   /evidence="ECO:0000250"
FT   BINDING         144
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="3"
FT                   /note="type 3 copper site"
FT                   /evidence="ECO:0000250"
FT   BINDING         522
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="4"
FT                   /note="type 1 copper site"
FT                   /evidence="ECO:0000255"
FT   BINDING         525
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="1"
FT                   /note="type 2 copper site"
FT                   /evidence="ECO:0000255"
FT   BINDING         527
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="3"
FT                   /note="type 3 copper site"
FT                   /evidence="ECO:0000255"
FT   BINDING         570
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="3"
FT                   /note="type 3 copper site"
FT                   /evidence="ECO:0000255"
FT   BINDING         571
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="4"
FT                   /note="type 1 copper site"
FT                   /evidence="ECO:0000255"
FT   BINDING         572
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="2"
FT                   /note="type 3 copper site"
FT                   /evidence="ECO:0000255"
FT   BINDING         576
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="4"
FT                   /note="type 1 copper site"
FT                   /evidence="ECO:0000255"
FT   BINDING         581
FT                   /ligand="Cu cation"
FT                   /ligand_id="ChEBI:CHEBI:23378"
FT                   /ligand_label="4"
FT                   /note="type 1 copper site"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   589 AA;  66123 MW;  84B88332EAD5D003 CRC64;
     MPTRTSRRTF VKGLAASSIL SGLGLWRSPA WALPNPGQPD GLSGTEFDLT IGETQVNITG
     NARTAMTING GIPGPLLRWR EGDTVTLRVK NRLDETTSIH WHGIILPANM DGVPGLSFDG
     IAPDGMYVYR FKVRQHGTYW YHSHSGFQEQ SGVYGPLVID AKEPEPFTYE REHVVMLTDW
     ADEDPARVMK KLKKQSDYYN NNKRTVGDFI NDVGEKGWSA TTAERWMWAQ MKMNPTDLAD
     VSGATYTYLM NGQAPNMNWT GLFKPGEQIR LRFINGSSMT YFDVRIPGLK MTVVASDGLH
     IKPVVVDELR IAVAETFDVI VEPADGAYTL FAQSMDRTGF ARGTLTSRPG MQAEVPPLDP
     RPLLSMDDMG MAGMDHGSMN HSAKPAMDGM DHSKMDHDSM PGMDHGTMPM QEAPVMQSHP
     DSERNNPLVD MQAMSTSAKL NDPGIGLRDN GRKVLTYADL RSTFEDPDGR EPSRTIELHL
     TGHMEKFAWS FDGVKFSDAK PLMLKYGERV RIVLVNDTMM THPIHLHGMW SDLEDENGQF
     MVRKHTIDMP PGSRRSYRVT ADALGRWAYH CHMLYHMEMG MFREVRVEE
 
 
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