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 03-AUG-2022, entry version 143.
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}.
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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 AlphaFoldDB; Q05608; -.
DR SMR; Q05608; -.
DR IntAct; Q05608; 1.
DR MINT; Q05608; -.
DR EnsemblBacteria; CAF25344; CAF25344; pYV0001.
DR GeneID; 66841082; -.
DR KEGG; ypo:BZ17_4237; -.
DR KEGG; yps:pYV0001; -.
DR PATRIC; fig|273123.14.peg.4471; -.
DR OMA; TYSFLNR; -.
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: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 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 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 566
FT /note="H -> N (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT HELIX 442..460
FT /evidence="ECO:0007829|PDB:2H7O"
FT HELIX 466..485
FT /evidence="ECO:0007829|PDB:2H7O"
FT HELIX 491..513
FT /evidence="ECO:0007829|PDB:2H7O"
FT HELIX 534..537
FT /evidence="ECO:0007829|PDB:2H7O"
FT HELIX 539..547
FT /evidence="ECO:0007829|PDB:2H7O"
FT HELIX 548..551
FT /evidence="ECO:0007829|PDB:2H7O"
FT HELIX 556..558
FT /evidence="ECO:0007829|PDB:2H7O"
FT HELIX 559..580
FT /evidence="ECO:0007829|PDB:2H7O"
FT STRAND 583..585
FT /evidence="ECO:0007829|PDB:2H7V"
FT HELIX 588..628
FT /evidence="ECO:0007829|PDB:2H7O"
FT HELIX 629..631
FT /evidence="ECO:0007829|PDB:2H7O"
FT HELIX 633..646
FT /evidence="ECO:0007829|PDB:2H7O"
FT HELIX 656..658
FT /evidence="ECO:0007829|PDB:2H7O"
FT HELIX 659..676
FT /evidence="ECO:0007829|PDB:2H7O"
FT HELIX 677..679
FT /evidence="ECO:0007829|PDB:2H7O"
FT HELIX 680..697
FT /evidence="ECO:0007829|PDB:2H7O"
FT HELIX 705..730
FT /evidence="ECO:0007829|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
