ID   PKN1_CHLMU              Reviewed;         614 AA.
AC   Q9PKP3;
DT   09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Serine/threonine-protein kinase pkn1;
DE            EC=2.7.11.1;
GN   Name=pkn1; OrderedLocusNames=TC_0422;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
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).
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.
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}.
CC   -!- CAUTION: Gln-136 is present instead of the conserved Asp which is
CC       expected to be an active site residue. {ECO:0000305}.
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DR   EMBL; AE002160; AAF39278.1; -; Genomic_DNA.
DR   PIR; H81703; H81703.
DR   RefSeq; WP_010230419.1; NZ_CP027217.1.
DR   AlphaFoldDB; Q9PKP3; -.
DR   SMR; Q9PKP3; -.
DR   STRING; 243161.TC_0422; -.
DR   EnsemblBacteria; AAF39278; AAF39278; TC_0422.
DR   GeneID; 1245775; -.
DR   KEGG; cmu:TC_0422; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG1262; Bacteria.
DR   HOGENOM; CLU_408763_0_0_0; -.
DR   OMA; TQANFFS; -.
DR   OrthoDB; 1377603at2; -.
DR   Proteomes; UP000000800; 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   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 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..614
FT                   /note="Serine/threonine-protein kinase pkn1"
FT                   /id="PRO_0000171187"
FT   DOMAIN          13..302
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         19..27
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         42
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   614 AA;  69782 MW;  A24D888E70258B75 CRC64;
     MEEQSTVEYW GDYKVIAELE QGLWSRDVLT EHRFIKKRYV LKILPSELSL SEDFMKVFQK
     VIVQLATIRH PSLVAIENVS QEKDRYFIVT EENSGTISLA KYLSGRKLSE EEIVYLIQQL
     CEVLELVHEI GLAHGQINLH SVHVSFINGV ANIYLPEVGF ASLLRERMFS SIMQKASMQE
     SVECIRDLLV FEAPEEKSTN HRATDAYSVG VLAYYLLVGA FPWGAFPKPS SCIPDSIYDW
     DSFILSCLQQ QQQARPKRLR DALKKKTLGE QLQSTIDHCR ESLRAMEVQE EVSEPIAPTS
     LIREGEKLFE GKEEQQAFVL VEAKSIDEAM VTTVDSEEVS ESGEGYVNPL QSLLAREPVV
     SRYVEIEREE VKPQPLSTEM VFIEGGDFSR GSRDGQRDEL PVHNITLPGF LLDIHPVTNE
     HFVRFLEFIG GEQDEHYNEL IRLKDSRIQR RSGRLIIEPG YAKHPVVGVT WYGASSYASW
     IGKRLPSEAE WEVAAAGGKL GMRYPTGEDV DKSKANFFSS DTTPVMSYPA NILGLYDMAG
     NIYEWCQDWY SYDFYENSAL EPDSPQGPPQ GVYRVLRGGC WKSLKEDLRC AHRHRNNPGA
     INSTYGFRCA KDVK