ID   PKND_CHLMU              Reviewed;         934 AA.
AC   Q9PK92;
DT   11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 123.
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=TC_0575;
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 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; AE002160; AAF73573.1; -; Genomic_DNA.
DR   RefSeq; WP_010230882.1; NZ_CP027217.1.
DR   AlphaFoldDB; Q9PK92; -.
DR   SMR; Q9PK92; -.
DR   STRING; 243161.TC_0575; -.
DR   PRIDE; Q9PK92; -.
DR   EnsemblBacteria; AAF73573; AAF73573; TC_0575.
DR   GeneID; 1245934; -.
DR   KEGG; cmu:TC_0575; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_303227_0_0_0; -.
DR   OMA; VVILDWG; -.
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-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_0000171191"
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;  107499 MW;  F08AEFD10A47E05C CRC64;
     MQRYELIRLI GRGGMGEVYL AHDKACSRRV ALKKIREDLS DNPLLRKRFL REAKIAADLI
     HPGIVPVYSI CSDGESVYYT MPYIEGFSLK HLLKSVWQKE ILSKELEEKT SVKAFLPIFD
     KICATVEYIH SKGVLHRDLK PDNILLGLFG EVVIVDWGAA IFKHAKELQQ EKDEEGFSSY
     GQKNICYSSM TVPGKIVGTP DYMAPESLLG AEASEKTDIY ALGLILYQML TLSFPYRRKK
     GRKLPYEDSI LSPIEMAPYR EIPPSLSQIA MKAIAVDPVQ RFSSVQELRK ALQPHLQGES
     EWTTRDILST KDRKNWKYYE PILLSRYFPV LASSPAQWYN FMLSDMEVNS SVRVECSVTK
     SSVQEGVGIF FPPSKEADKG EFYCGYGLWF SSQNNELSVS LIKNGIEIQK ESQGIIPQQS
     RFAISIEKSN NKITVFVDQI LFILHIDYLP SLGERIEIII QDLQGISNIT ILESIGALRV
     SCLAVPDAFL AEKLYDQAAR FYRKIRDSFP GRKESYEAQF RLGVTLLTQI EEQGGDLMQA
     LSTFDLLHGS TGAPLEYLGK ALVYQRNGSF VEEIRSLLLA LKRYPQHPEI PRLKDHLCFR
     LYDSLHKHRS EALVFMLLIL WIAPEKIGLR EEERFLEFLH HRQQSTLFCR IDKTPLQFKS
     SKMELFLSFW TGFTLFLPEL FQRARDLRDY QALIDIFYVV CASGNKEVFS QFAEDLAIFV
     DEVVFPKSLH NQRGEELVLF VQGLAALQNR EYRQAKEFIS AVPFALQLYA LDLFSLQAFI
     DEEVKVFSDF LQDIYNSASA EDHKHVLVYM IQVSLWNQDL KQAYELLSKN FPQDKGLIEY
     SEAFVLWGCY LALTGDRSAV KAHFSRCQFK YGRSALIGKC IDDDSLDYLE GLVWWEKKKT
     LFQSYFLLRC LHAPKERYEV YRQAYISMEN SFFG