ID   PKND_CHLTA              Reviewed;         934 AA.
AC   Q3KM61;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=CTA_0323;
OS   Chlamydia trachomatis serovar A (strain ATCC VR-571B / DSM 19440 / HAR-13).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=315277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-571B / DSM 19440 / HAR-13;
RX   PubMed=16177312; DOI=10.1128/iai.73.10.6407-6418.2005;
RA   Carlson J.H., Porcella S.F., McClarty G., Caldwell H.D.;
RT   "Comparative genomic analysis of Chlamydia trachomatis oculotropic and
RT   genitotropic strains.";
RL   Infect. Immun. 73:6407-6418(2005).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000051; AAX50561.1; -; Genomic_DNA.
DR   RefSeq; WP_011324674.1; NC_007429.1.
DR   AlphaFoldDB; Q3KM61; -.
DR   SMR; Q3KM61; -.
DR   PRIDE; Q3KM61; -.
DR   EnsemblBacteria; AAX50561; AAX50561; CTA_0323.
DR   KEGG; cta:CTA_0323; -.
DR   HOGENOM; CLU_303227_0_0_0; -.
DR   OMA; VVILDWG; -.
DR   Proteomes; UP000002532; 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_0000239299"
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;  107668 MW;  7C3E66E729AED843 CRC64;
     MQRYELIRLI GKGGMGEVYL AHDKACSRRV ALKRIREDLS GNALLRQRFL REAKIAADLI
     HPGIVPVYSI CSDGEAVYYT MPYIEGFSLK SLLKSVWQKE VLSKELEEKT SVKSFLPIFD
     KICATVEYIH SKGVLHRDLK PDNILLGLFG EVVIIDWGAA 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 KSQEMISQQS
     RFAILIEKSD NRIAVFVEQA LFILHIDYLP SLGNRLGVII QDLQGMSNIA ISESIGALRV
     SCLAVPDAFL SEKLYDQAAI FYRKIRDSFP GRKESYEAQF RLGVTLLTQI EEQGGDLTQA
     LSSFDYLHGG AGAPLEYLGK ALVYQRNGSF VEEIRCLLFA LKRYSQHPEI PRLEDHLCFR
     LYDSLHKHRS EALVFMLLIL WIAPEKISVR EEERFLRIIY HKQQATLFCQ VDKAPLQFRS
     SKMELFLSFW TGFSLFLPEL FRRAGGLRDY QALADIFYVA GVSGNREAFM QFSTALANVS
     DEITFPESLH NQKVAELMFF VKGVEALRNK DYQKAKKLLW KTPFTLQLYA LDMFHIQAFL
     DEEIESFIDL LQAIYDPTSE EERDHILVYI IQTHLWNRDL ERAYKLLNDR FPLDEELAEY
     SEAFILWGCY LALTGDRVAV KAHFSRCRYK YGKSALIGKC VDGDIFDYLD NLVWWEKKMT
     LFQSYFLLRC LNESPRRYEK YRQAYLSMEN NFFD