(data stored in ACNUC9435 zone)

SWISSPROT: YPKA_YERPS

ID   YPKA_YERPS              Reviewed;         732 AA.
AC   Q05608; Q663G6;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 2.
DT   11-DEC-2019, entry version 133.
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=pYV0001;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OG   Plasmid pIB1, and Plasmid pYV.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=YPIII / Serotype O:3; PLASMID=pIB1;
RX   PubMed=8441468; DOI=10.1038/361730a0;
RA   Galyov E.E., Haakansson S., Forsberg A., Wolf-Watz H.;
RT   "A secreted protein kinase of Yersinia pseudotuberculosis is an
RT   indispensable virulence determinant.";
RL   Nature 361:730-732(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=YPIII / Serotype O:3; PLASMID=pIB1;
RX   PubMed=8045884; DOI=10.1128/jb.176.15.4543-4548.1994;
RA   Galyov E.E., Haakansson S., Wolf-Watz H.;
RT   "Characterization of the operon encoding the YpkA Ser/Thr protein kinase
RT   and the YopJ protein of Yersinia pseudotuberculosis.";
RL   J. Bacteriol. 176:4543-4548(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953; PLASMID=pYV;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=8736538; DOI=10.1046/j.1365-2958.1996.5251051.x;
RA   Hakansson S., Galyov E.E., Rosqvist R., Wolf-Watz H.;
RT   "The Yersinia YpkA Ser/Thr kinase is translocated and subsequently targeted
RT   to the inner surface of the HeLa cell plasma membrane.";
RL   Mol. Microbiol. 20:593-603(1996).
RN   [5]
RP   FUNCTION.
RX   PubMed=10920208; DOI=10.1073/pnas.170281997;
RA   Juris S.J., Rudolph A.E., Huddler D., Orth K., Dixon J.E.;
RT   "A distinctive role for the Yersinia protein kinase: actin binding, kinase
RT   activation, and cytoskeleton disruption.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:9431-9436(2000).
RN   [6]
RP   FUNCTION.
RX   PubMed=17531806; DOI=10.1016/j.molcel.2007.04.025;
RA   Navarro L., Koller A., Nordfelth R., Wolf-Watz H., Taylor S., Dixon J.E.;
RT   "Identification of a molecular target for the Yersinia protein kinase A.";
RL   Mol. Cell 26:465-477(2007).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 434-732.
RX   PubMed=16959567; DOI=10.1016/j.cell.2006.06.056;
RA   Prehna G., Ivanov M.I., Bliska J.B., Stebbins C.E.;
RT   "Yersinia virulence depends on mimicry of host Rho-family nucleotide
RT   dissociation inhibitors.";
RL   Cell 126:869-880(2006).
CC   -!- FUNCTION: Acts as a virulence determinant.
CC       {ECO:0000269|PubMed:10920208, ECO:0000269|PubMed:17531806}.
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8736538}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
DR   EMBL; X69439; CAA49215.1; -; Genomic_DNA.
DR   EMBL; L33833; AAA68487.1; -; Genomic_DNA.
DR   EMBL; BX936399; CAF25344.1; -; Genomic_DNA.
DR   PIR; S30060; S30060.
DR   RefSeq; WP_011191359.1; NZ_CP009711.1.
DR   PDB; 2H7O; X-ray; 2.00 A; A=434-732.
DR   PDB; 2H7V; X-ray; 2.60 A; C/D=434-732.
DR   PDBsum; 2H7O; -.
DR   PDBsum; 2H7V; -.
DR   SMR; Q05608; -.
DR   IntAct; Q05608; 1.
DR   MINT; Q05608; -.
DR   EnsemblBacteria; CAF25344; CAF25344; pYV0001.
DR   GeneID; 39573293; -.
DR   KEGG; ypo:BZ17_4237; -.
DR   KEGG; yps:pYV0001; -.
DR   PATRIC; fig|273123.14.peg.4471; -.
DR   HOGENOM; HOG000219636; -.
DR   KO; K23472; -.
DR   OMA; MRNFTAD; -.
DR   EvolutionaryTrace; Q05608; -.
DR   Proteomes; UP000001011; Plasmid pYV.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
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;
DR   PRODOM; Q05608.
DR   SWISS-2DPAGE; Q05608.
KW   3D-structure; ATP-binding; Kinase; Nucleotide-binding; Plasmid; Secreted;
KW   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_0000024392"
FT   DOMAIN          136..408
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   NP_BIND         142..150
FT                   /note="ATP"
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         163
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   CONFLICT        566
FT                   /note="H -> N (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
FT   HELIX           442..460
FT                   /evidence="ECO:0000244|PDB:2H7O"
FT   HELIX           466..485
FT                   /evidence="ECO:0000244|PDB:2H7O"
FT   HELIX           491..513
FT                   /evidence="ECO:0000244|PDB:2H7O"
FT   HELIX           534..537
FT                   /evidence="ECO:0000244|PDB:2H7O"
FT   HELIX           539..547
FT                   /evidence="ECO:0000244|PDB:2H7O"
FT   HELIX           548..551
FT                   /evidence="ECO:0000244|PDB:2H7O"
FT   HELIX           556..558
FT                   /evidence="ECO:0000244|PDB:2H7O"
FT   HELIX           559..580
FT                   /evidence="ECO:0000244|PDB:2H7O"
FT   STRAND          583..585
FT                   /evidence="ECO:0000244|PDB:2H7V"
FT   HELIX           588..628
FT                   /evidence="ECO:0000244|PDB:2H7O"
FT   HELIX           629..631
FT                   /evidence="ECO:0000244|PDB:2H7O"
FT   HELIX           633..646
FT                   /evidence="ECO:0000244|PDB:2H7O"
FT   HELIX           656..658
FT                   /evidence="ECO:0000244|PDB:2H7O"
FT   HELIX           659..676
FT                   /evidence="ECO:0000244|PDB:2H7O"
FT   HELIX           677..679
FT                   /evidence="ECO:0000244|PDB:2H7O"
FT   HELIX           680..697
FT                   /evidence="ECO:0000244|PDB:2H7O"
FT   HELIX           705..730
FT                   /evidence="ECO:0000244|PDB:2H7O"
SQ   SEQUENCE   732 AA;  81731 MW;  CEF903AAFE2E57BC 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 YGFLNRLAEA
     KITLSQQLNT LQQQQESAKA QLSILINRSG SWADVARQSL QRFDSTRPVV KFGTEQYTAI
     HRQMMAAHAA ITLQEVSEFT DDMRNFTVDS IPLLIQLGRS SLMDEHLVEQ REKLRELTTI
     AERLNRLERE WM
//

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