ID   PKND_CHLFF              Reviewed;         933 AA.
AC   Q255D2;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 2.
DT   03-AUG-2022, entry version 78.
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=CF0334;
OS   Chlamydia felis (strain Fe/C-56) (Chlamydophila felis).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=264202;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fe/C-56;
RX   PubMed=16766509; DOI=10.1093/dnares/dsi027;
RA   Azuma Y., Hirakawa H., Yamashita A., Cai Y., Rahman M.A., Suzuki H.,
RA   Mitaku S., Toh H., Goto S., Murakami T., Sugi K., Hayashi H., Fukushi H.,
RA   Hattori M., Kuhara S., Shirai M.;
RT   "Genome sequence of the cat pathogen, Chlamydophila felis.";
RL   DNA Res. 13:15-23(2006).
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   -!- SEQUENCE CAUTION:
CC       Sequence=BAE81106.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AP006861; BAE81106.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011457886.1; NC_007899.1.
DR   AlphaFoldDB; Q255D2; -.
DR   SMR; Q255D2; -.
DR   STRING; 264202.CF0334; -.
DR   PRIDE; Q255D2; -.
DR   KEGG; cfe:CF0334; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_303227_0_0_0; -.
DR   OrthoDB; 1377603at2; -.
DR   Proteomes; UP000001260; 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..933
FT                   /note="Serine/threonine-protein kinase PknD"
FT                   /id="PRO_0000239301"
FT   DOMAIN          4..291
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   933 AA;  106799 MW;  17E45CDA3148658A CRC64;
     MQRYDIIRMI GKGGMGEVYL AYDPVCSRKV ALKRIREDLS DNELLKKRFL REAKIAADLV
     HPGVVPVFTI CSDSDPVYYT MPYIEGYTLK SLLKSVWQCD SLPKDLAEQT SVGTFLSIFH
     KICSTVEYVH SRGILHRDLK PDNILLGLFS EVVILDWGAA LSKEMQEEVL LDIDIPVTGS
     MFSNMTIPGK IVGTPDYMAP ERLRGTPASE STDIYALGVI LYQMLTLSFP YRNKKGKKIS
     FRHQISSPEE IAPHREIPPF LSQVAMKALA ADPKVRYASV KELKDDIEQH LQGSPEWTPK
     TILHTQKAEC WKLRESILLS KYFPMLGVSP ALWYSLAISK IESFSEVRLE YTLLRKGLED
     GFGILLPPSE GVDHGDFYHG YGFWLHIKNS VFSVSLVKNG LEIRKTSRPI KENKEKFFIA
     LEKQNHRLSL IIDHVVWMIH MDYLPGRGGR IGVIIQDVTD VCGNIVVLES SGSLQVSCLA
     VPDAFLNEKL YDRAITFYRR IAESFPGRKE GYEAQFRIGI ALLEKASESG DSEGFTQALG
     KFEILHNSVA APLEYLGKAL VYQRLGEYNE EVKSLLLALK RYCQCPEISR IRDHIVYRLH
     ETLYSNHRLS LVFMLLALHI APESINATEE EYFVKNLHGK IQDTLFCNLD LSPIDFRSSK
     MELLLSYWSG FTPFLPGLFQ KYWDLKDYRA LADVFYVAAD LGNREFLEMY SDLVRENICS
     TTCTEDIVEF LPHQLEHFFS GVRAISLHEP LEKVFAHIEI LDPVLILYLF DLFAKDALIH
     HRGELILSAI TLIEKYVSSQ QYYEHLLPCE VLAYLWMKDE KKVYNLLCNN YEESLWLDDR
     SPAFVLYGCW LALVEDSSLS YLHLSGCRED ALYPRALIGG FCSPLGICEN QLSYQERRKL
     LLQKFIFFHC LGMNEERDNC TVAYDLLSIE RSL