ID   PKND_CHLTB              Reviewed;         934 AA.
AC   B0BBT2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Serine/threonine-protein kinase PknD {ECO:0000255|HAMAP-Rule:MF_01957};
DE            EC=2.7.11.1 {ECO:0000255|HAMAP-Rule:MF_01957};
GN   Name=pknD {ECO:0000255|HAMAP-Rule:MF_01957}; OrderedLocusNames=CTLon_0549;
OS   Chlamydia trachomatis serovar L2b (strain UCH-1/proctitis).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=471473;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCH-1/proctitis;
RX   PubMed=18032721; DOI=10.1101/gr.7020108;
RA   Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P.,
RA   Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D.,
RA   Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.;
RT   "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
RT   venereum isolates.";
RL   Genome Res. 18:161-171(2008).
CC   -!- FUNCTION: Together with the serine/threonine kinase Pkn1, may play a
CC       role in the specific interactions with host proteins during
CC       intracellular growth. {ECO:0000255|HAMAP-Rule:MF_01957}.
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:0000255|HAMAP-Rule:MF_01957};
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:0000255|HAMAP-Rule:MF_01957};
CC   -!- PTM: Autophosphorylated on serine and threonine residues.
CC       {ECO:0000255|HAMAP-Rule:MF_01957}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|HAMAP-Rule:MF_01957}.
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DR   EMBL; AM884177; CAP06947.1; -; Genomic_DNA.
DR   RefSeq; WP_009873709.1; NC_010280.2.
DR   AlphaFoldDB; B0BBT2; -.
DR   SMR; B0BBT2; -.
DR   KEGG; ctl:CTLon_0549; -.
DR   HOGENOM; CLU_303227_0_0_0; -.
DR   OMA; VVILDWG; -.
DR   Proteomes; UP000000794; 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-UniRule.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   Gene3D; 1.25.40.10; -; 1.
DR   HAMAP; MF_01957; PknD_kinase; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR023507; Ser/Thr_kinase_PknD.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..934
FT                   /note="Serine/threonine-protein kinase PknD"
FT                   /id="PRO_1000188973"
FT   DOMAIN          4..296
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01957"
FT   ACT_SITE        138
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01957"
FT   BINDING         10..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01957"
FT   BINDING         33
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01957"
SQ   SEQUENCE   934 AA;  107754 MW;  B20500268C18D316 CRC64;
     MQRYELIRLI GKGGMGEVYL AHDKACSRRV ALKRIREDLS GNALLRKRFL REAKIAADLI
     HPGIVPVYSI CSDGEAVYYT MPYIEGFSLK SLLKSVWQKE VLSKELEEKT SVKSFLPIFD
     KICATVEYIH SKGVLHRDLK PDNILLGLFG EVVIVDWGAA IFKHAKELKL EQDDEAAVSF
     DERNICYSSM TIPGKIVGTP DYMAPESLLG VEASEKTDIY ALGLILYQML TLAFPYRRKK
     GRKLSYRDVV LPPIEMSPYR EIPPSLSQIA MKAIAINPAD RFSSIQELRQ ALQPYLQGDP
     EWTVKATLMA KEKSCWKYYD PILLSRYFPV LASSPAQWYN FMLSEVEISA STRVEYTVTK
     SAVHEGMGIL FLPSKEAERG EFYCGYGLWF SVQNHELTVS LIKNGIEIQK KSQEMISQQY
     RFAILIEKSD NRIAVFVEQA LFILHIDYLP SLGNRLGVII QDLQGMSNIA ISESIGALRV
     SCLAVPDAFL SEKLYDQAAI FYRKIRDSFP GRKESYEAQF RLGVTLLTQI EEQGGDLTQA
     LSSFDYLHGG AGAPLEYLGK ALVYQRNGSF VEEIRCLLFA LKRYSQHPEI PRLEDHLCFR
     LYDSLHKHRS EALVFMLLIL WIAPEKISVR EEKRFLRIIY HKQQATLFCQ VDKAPLQFRS
     SKMELFLSFW TGFSLFLPEL FRRAGELRDY QALADIFYVA GVSGNREAFM QFSTALANVS
     DEITFPESLH NQKVAELMFF VKGVEALRNK DYQKAKKLLW KTPFTLQLYA LDIFHIQAFL
     DEEIESFIDL LQAIYDPASE EERDHILVYI IQTHLWNRDL ERAYKLLNDR FPLDEELAEY
     SEAFILWGCY LALTGDRVAV KAHFSRCRYK YGKSALIGKC VDGDIFDYLD NLVWWEKKMT
     LFQSYFLLRC LNESPRRYEK YRQAYLSMEN NFFD