ID   PKN1_CHLTR              Reviewed;         614 AA.
AC   P0DPS7; O84147; Q8GDH8;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2019, sequence version 1.
DT   03-AUG-2022, entry version 12.
DE   RecName: Full=Serine/threonine-protein kinase Pkn1;
DE            EC=2.7.11.1;
GN   Name=pkn1; OrderedLocusNames=CT_145;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
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. Phosphorylates IncG, an inclusion-membrane
CC       protein required for the modification of the nascent chlamydial
CC       inclusion. {ECO:0000250|UniProtKB:A0A0H3MBJ2}.
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         Evidence={ECO:0000250|UniProtKB:A0A0H3MBJ2};
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; Evidence={ECO:0000250|UniProtKB:A0A0H3MBJ2};
CC   -!- SUBUNIT: Interacts with PknD, interacts with and phosphorylates IncG.
CC       {ECO:0000250|UniProtKB:A0A0H3MBJ2}.
CC   -!- PTM: Autophosphorylates on serine and threonine residues.
CC       {ECO:0000250|UniProtKB:A0A0H3MBJ2}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000305}.
CC   -!- CAUTION: Gln-136 is present instead of the conserved Asp which is
CC       expected to be a proton acceptor in the active site. {ECO:0000305}.
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DR   EMBL; AE001273; AAC67736.1; -; Genomic_DNA.
DR   PIR; B71551; B71551.
DR   RefSeq; NP_219648.1; NC_000117.1.
DR   RefSeq; WP_010725091.1; NC_000117.1.
DR   AlphaFoldDB; P0DPS7; -.
DR   SMR; P0DPS7; -.
DR   STRING; 813.O172_00790; -.
DR   EnsemblBacteria; AAC67736; AAC67736; CT_145.
DR   GeneID; 884193; -.
DR   KEGG; ctr:CT_145; -.
DR   OMA; TQANFFS; -.
DR   Proteomes; UP000000431; 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   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..614
FT                   /note="Serine/threonine-protein kinase Pkn1"
FT                   /id="PRO_0000171189"
FT   DOMAIN          13..276
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;  69694 MW;  28BEC559CD694001 CRC64;
     MEERAAVEYW GDYKVIAELG HGLWSRDVLA EHRFIKKRYI LKILPSELSS SENFMRVFQE
     VIVQLAAIRH ASLVAIENVS REGDRYFVVT EENGGTISLA QYLSGRKLSE EEVVHLIQQL
     CDALELVHSI GLAHGQIHLH SVHVSFFNGI ANIYLPEVGF ASLLRERMFS TIMQSGSARE
     SITRIRDLLM FEAPEEQEVF GREADVYSVG VLAYYLLVGS FPWGSFPKPS LCMPDSWYDW
     DGFILSCLQQ QREVRPKCLR EALRRKTSGE QLQVTLDSCR EPLREMEIED TPTELGPPSA
     LIREGERLCE VKEEQHAFVL VEAKSIDEVM VTTVDSEEEL ESSEGYANPL QSLLAREPVV
     SRYVEVEREE IKPQPLLTEM IFIEGGEFSR GSGDGQRDEL PVHNITLPGF FLDIHPVTNE
     QFVRFLECVG SEQDEHYNEL IRLKDSRIQR RSGRLIIEPG YAKHPVVGVT WYGASSYACW
     IGKRLPSEAE WEVAASGGKL GLRYPTGEEI DKSKANFFSS DTTPVMSYPS SILGLYDMAG
     NVYEWCQDWY SYDFYESSAL EPDAPLGPPQ GVYRVLRGGC WKSLKDDLRC AHRHRNNPGA
     INSTYGFRCA KDVK