PKN1_CHLPN
ID PKN1_CHLPN Reviewed; 619 AA.
AC Q7AJA5; Q7VQ75; Q9K228; Q9Z935;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Serine/threonine-protein kinase pkn1;
DE EC=2.7.11.1;
GN Name=pkn1; OrderedLocusNames=CPn_0148, CP_0625, CPj0148, CpB0149;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWL029;
RX PubMed=10192388; DOI=10.1038/7716;
RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL Nat. Genet. 21:385-389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR39;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J138;
RX PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT Japan and CWL029 from USA.";
RL Nucleic Acids Res. 28:2311-2314(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW-183;
RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT other Chlamydia strains based on whole genome sequence analysis.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Together with the serine/threonine kinase PknD, may play a
CC role in the specific interactions with host proteins during
CC intracellular growth. {ECO:0000250}.
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 -!- PTM: Autophosphorylated on serine and threonine residues.
CC {ECO:0000250}.
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; AE001363; AAD18301.1; -; Genomic_DNA.
DR EMBL; AE002161; AAF38440.1; -; Genomic_DNA.
DR EMBL; BA000008; BAA98358.1; -; Genomic_DNA.
DR EMBL; AE009440; AAP98082.1; -; Genomic_DNA.
DR PIR; A72114; A72114.
DR PIR; D81556; D81556.
DR PIR; D86509; D86509.
DR RefSeq; NP_224356.1; NC_000922.1.
DR RefSeq; WP_010882798.1; NZ_LN847257.1.
DR AlphaFoldDB; Q7AJA5; -.
DR SMR; Q7AJA5; -.
DR STRING; 115711.CP_0625; -.
DR EnsemblBacteria; AAD18301; AAD18301; CPn_0148.
DR EnsemblBacteria; AAF38440; AAF38440; CP_0625.
DR KEGG; cpa:CP_0625; -.
DR KEGG; cpj:CPj0148; -.
DR KEGG; cpn:CPn_0148; -.
DR KEGG; cpt:CpB0149; -.
DR PATRIC; fig|115713.3.peg.168; -.
DR eggNOG; COG0515; Bacteria.
DR eggNOG; COG1262; Bacteria.
DR HOGENOM; CLU_408763_0_0_0; -.
DR OrthoDB; 1377603at2; -.
DR Proteomes; UP000000583; Chromosome.
DR Proteomes; UP000000801; Chromosome.
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; 3.90.1580.10; -; 1.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR005532; SUMF_dom.
DR InterPro; IPR042095; SUMF_sf.
DR Pfam; PF03781; FGE-sulfatase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..619
FT /note="Serine/threonine-protein kinase pkn1"
FT /id="PRO_0000171188"
FT DOMAIN 15..302
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 141
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 21..29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CONFLICT 309
FT /note="V -> A (in Ref. 2; AAF38440)"
FT /evidence="ECO:0000305"
FT CONFLICT 515
FT /note="I -> V (in Ref. 4; AAP98082)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 619 AA; 70355 MW; CA312E28304D7D80 CRC64;
MESEKDIGAK FLGDYRILYR KGQSLWSEDL LAEHRFIKKR YLIRLLLPDL GSSQPFMEAF
HDVVVKLAKL NHPGILSIEN VSESEGRCFL VTQEQDIPIL SLTQYLKSIP RKLTELEIVD
IVSQLASLLD YVHSEGLAQE EWNLDSVYIH ILNGVPKVIL PDLGFASLIK ERILDGFISD
EENRESKIKE RVLLHTSEGK QGREDTYAFG AITYYLLFGF LPQGIFPMPS KVFSDFIYDW
DFLISSCLSC FMEERAKELF PLIRKKTLGE ELQNVVTNCI ESSLREVPDP LESSQNLPQA
VLKVGETKVS HQQKESAEHL EFVLVEACSI DEAMDTAIES ESSSGVEEEG YSLALQSLLV
REPVVSRYVE AEKEEPKPQP ILTEMVLIEG GEFSRGSVEG QRDELPVHKV ILHSFFLDVH
PVTNEQFIRY LECCGSEQDK YYNELIRLRD SRIQRRSGRL VIEPGYAKHP VVGVTWYGAS
GYAEWIGKRL PTEAEWEIAA SGGVAALRYP CGEEIEKSRA NFFTADTTTV MSYPPNPYGL
YDMAGNVYEW CQDWYGYDFY EISAQEPESP QGPAQGVYRV LRGGCWKSLK DDLRCAHRHR
NNPGAVNSTY GFRCAKNIN
