ID   PKND_PARUW              Reviewed;         982 AA.
AC   Q6MAN0;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=pc1645;
OS   Protochlamydia amoebophila (strain UWE25).
OC   Bacteria; Chlamydiae; Parachlamydiales; Parachlamydiaceae;
OC   Candidatus Protochlamydia.
OX   NCBI_TaxID=264201;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UWE25;
RX   PubMed=15073324; DOI=10.1126/science.1096330;
RA   Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U.,
RA   Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T.,
RA   Mewes H.-W., Wagner M.;
RT   "Illuminating the evolutionary history of chlamydiae.";
RL   Science 304:728-730(2004).
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; BX908798; CAF24369.1; -; Genomic_DNA.
DR   RefSeq; WP_011176191.1; NC_005861.1.
DR   AlphaFoldDB; Q6MAN0; -.
DR   SMR; Q6MAN0; -.
DR   STRING; 264201.pc1645; -.
DR   PRIDE; Q6MAN0; -.
DR   EnsemblBacteria; CAF24369; CAF24369; PC_RS07875.
DR   KEGG; pcu:PC_RS07875; -.
DR   eggNOG; COG0457; Bacteria.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_303227_0_0_0; -.
DR   OrthoDB; 1377603at2; -.
DR   Proteomes; UP000000529; 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; SSF48452; SSF48452; 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   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..982
FT                   /note="Serine/threonine-protein kinase PknD"
FT                   /id="PRO_0000239302"
FT   DOMAIN          51..342
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01957"
FT   ACT_SITE        186
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01957"
FT   BINDING         57..65
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01957"
FT   BINDING         80
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01957"
SQ   SEQUENCE   982 AA;  113378 MW;  F3AAA39404B80D89 CRC64;
     MPHSFPDYSF TCPFCKNNCK LSFAQCPAFC PFCGKSQKNE STGLPIQSDF YQIIKSIGKG
     GMGEVFLAYD PCYERQIAIK KIRSDLLEHP QIKKRFLKEA HMTSQLTHPA IIPIYTIRSD
     ADTAYYTMPF VEGDTLKQII RKTKLQEKNG ETLDYLGGSI LALMRVFITI CQAVAYAHSK
     GVLHRDLKPE NIIIGKYGEV LILDWGLAKF IDQSPEEELL ASFPESLTKQ KDITKIGKVV
     GTVAYMAPER ALGQPATIQT DIYSLGVILY QLLTLKSPFK RGTLDEFRKN MSREEWQDPV
     TAAPYREVPR MLASFTEKCL SLDLQNRYQS VEELIRDIEN YLEGRSEWFC IANLNTKEKN
     DWEFQENVLI AEHVAITRMT DDAEWVSLMI SKQSFTGNTK IEADVCLGEQ GHGIGFLLSV
     PEASAREHLI EGYCLWLGSD FSKTTKLLRS NVEVVHAPDI FLKRQQTYHV RIEKVDKSIH
     VYINDNLQFS YIAHIPLIGT HVGLLSRDAD FEISPLEIYV GNLNINVNCL AVPDAFLAHR
     DYNQALSEYR RIAYSFPDRT EGREALFRAG LTFLEQAKTA ENKMPLLEEA LNEFEKLHGT
     PSAPLEYLGK ALAYESINDS EEEIKCYELA YRRYPNHPIL PMLQEQIISR LHEVSRMQRI
     TTYRFTLLTV RHLPLNKIDT HTKRLFNSLQ KHWEVLPFIE YKSPSPLTTL STRFATPLAF
     WLAKPFILGE ILDDLIQSPP FPIEEVNNAL LCLVELGSWE YAQEKLNTIQ TYLNLPQNPK
     WLDLKAFIAC HYQTLEDVYK DFFFQIPSTN ADHLHAVLYF MDQCLDQLNT SLIYTLARQF
     EHAELSFEDR LRLNCRRVWA YLLDKNWQDA GNLLYTYSVE TLNKDSSLLH FLYGCWLQVT
     EGAEIANVHF AGVNPVMFPR TWTLGARFLT NNLSKDSYEK AFMWEKRQLC KQLILYYHCV
     GNETKRIHFQ KLYQEQFIHA EL