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YPKA_YERPE
ID   YPKA_YERPE              Reviewed;         732 AA.
AC   Q9RI12; O68717;
DT   04-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 144.
DE   RecName: Full=Protein kinase YpkA;
DE            Short=Protein kinase A;
DE            EC=2.7.11.1;
DE   AltName: Full=Targeted effector protein kinase;
DE   Flags: Precursor;
GN   Name=ypkA; OrderedLocusNames=YPCD1.72c, y5008, y0009, YP_pCD13;
OS   Yersinia pestis.
OG   Plasmid pCD1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=632;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=KIM5 / Biovar Mediaevalis;
RX   PubMed=9746557; DOI=10.1128/iai.66.10.4611-4623.1998;
RA   Perry R.D., Straley S.C., Fetherston J.D., Rose D.J., Gregor J.,
RA   Blattner F.R.;
RT   "DNA sequencing and analysis of the low-Ca2+-response plasmid pCD1 of
RT   Yersinia pestis KIM5.";
RL   Infect. Immun. 66:4611-4623(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=KIM5 / Biovar Mediaevalis;
RX   PubMed=9748454; DOI=10.1128/jb.180.19.5192-5202.1998;
RA   Hu P., Elliott J., McCready P., Skowronski E., Garnes J., Kobayashi A.,
RA   Brubaker R.R., Garcia E.;
RT   "Structural organization of virulence-associated plasmids of Yersinia
RT   pestis.";
RL   J. Bacteriol. 180:5192-5202(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CO-92 / Biovar Orientalis;
RX   PubMed=11586360; DOI=10.1038/35097083;
RA   Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA   Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA   Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA   Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA   Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA   Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA   Stevens K., Whitehead S., Barrell B.G.;
RT   "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL   Nature 413:523-527(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=91001 / Biovar Mediaevalis;
RX   PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA   Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA   Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA   Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA   Wang J., Huang P., Yang R.;
RT   "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT   avirulent to humans.";
RL   DNA Res. 11:179-197(2004).
CC   -!- FUNCTION: Acts as a virulence determinant.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1;
CC   -!- INTERACTION:
CC       Q9RI12; Q96FW1: OTUB1; Xeno; NbExp=3; IntAct=EBI-2849107, EBI-1058491;
CC       Q9RI12; P50552: VASP; Xeno; NbExp=4; IntAct=EBI-2849107, EBI-748201;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; AF074612; AAC69765.1; -; Genomic_DNA.
DR   EMBL; AF053946; AAC62602.1; -; Genomic_DNA.
DR   EMBL; AL117189; CAB54949.1; -; Genomic_DNA.
DR   EMBL; AE017043; AAS58532.1; -; Genomic_DNA.
DR   PIR; T43619; T43619.
DR   RefSeq; NP_395206.1; NC_003131.1.
DR   RefSeq; NP_857776.1; NC_004836.1.
DR   RefSeq; NP_857907.1; NC_004839.1.
DR   RefSeq; WP_002213290.1; NZ_VWRZ01000163.1.
DR   RefSeq; WP_011114033.1; NZ_WUCM01000117.1.
DR   AlphaFoldDB; Q9RI12; -.
DR   SMR; Q9RI12; -.
DR   IntAct; Q9RI12; 10.
DR   MINT; Q9RI12; -.
DR   STRING; 214092.5832492; -.
DR   BindingDB; Q9RI12; -.
DR   PRIDE; Q9RI12; -.
DR   DNASU; 1149271; -.
DR   EnsemblBacteria; AAS58532; AAS58532; YP_pCD13.
DR   KEGG; ype:YPCD1.72c; -.
DR   KEGG; ypm:YP_pCD13; -.
DR   PATRIC; fig|214092.21.peg.82; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_402177_0_0_6; -.
DR   OMA; TYSFLNR; -.
DR   Proteomes; UP000000815; Plasmid pCD1.
DR   Proteomes; UP000001019; Plasmid pCD1.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   Gene3D; 1.20.120.1330; -; 1.
DR   Gene3D; 1.20.58.1230; -; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR043119; Rac1-bd_C.
DR   InterPro; IPR019093; Rac1-binding_domain.
DR   InterPro; IPR043120; Rac1-db_N.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR003547; Ser/thr_kinase_yersinia-type.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF09632; Rac1; 1.
DR   PRINTS; PR01373; YERSSTKINASE.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Plasmid; Reference proteome;
KW   Secreted; Serine/threonine-protein kinase; Signal; Transferase; Virulence.
FT   SIGNAL          1..?
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..732
FT                   /note="Protein kinase YpkA"
FT                   /id="PRO_0000024391"
FT   DOMAIN          136..408
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        270
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         142..150
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         163
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   CONFLICT        647
FT                   /note="R -> Q (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   732 AA;  81761 MW;  DEF803AAEE2F5BCD CRC64;
     MKSVKIMGTM PPSISLAKAH ERISQHWQNP VGELNIGGKR YRIIDNQVLR LNPHSGFSLF
     REGVGKIFSG KMFNFSIARN LTDTLHAAQK TTSQELRSDI PNALSNLFGA KPQTELPLGW
     KGEPLSGAPD LEGMRVAETD KFAEGESHIS IIETKDKQRL VAKIERSIAE GHLFAELEAY
     KHIYKTAGKH PNLANVHGMA VVPYGNRKEE ALLMDEVDGW RCSDTLRTLA DSWKQGKINS
     EAYWGTIKFI AHRLLDVTNH LAKAGVVHND IKPGNVVFDR ASGEPVVIDL GLHSRSGEQP
     KGFTESFKAP ELGVGNLGAS EKSDVFLVVS TLLHCIEGFE KNPEIKPNQG LRFITSEPAH
     VMDENGYPIH RPGIAGVETA YTRFITDILG VSADSRPDSN EARLHEFLSD GTIDEESAKQ
     ILKDTLTGEM SPLSTDVRRI TPKKLRELSD LLRTHLSSAA TKQLDMGGVL SDLDTMLVAL
     DKAEREGGVD KDQLKSFNSL ILKTYRVIED YVKGREGDTK NSSTEVSPYH RSNFMLSIVE
     PSLQRIQKHL DQTHSFSDIG SLVRAHKHLE TLLEVLVTLS QQGQPVSSET YGFLNRLTEA
     KITLSQQLNT LQQQQESAKA QLSILINRSG SWADVARQSL QRFDSTRPVV KFGTEQYTAI
     HRQMMAAHAA ITLQEVSEFT DDMRNFTVDS IPLLIQLGRS SLMDEHLVEQ REKLRELTTI
     AERLNRLERE WM
 
 
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