ID PKND_CHLCV Reviewed; 930 AA. AC Q822K5; DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 116. 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}; GN OrderedLocusNames=CCA_00677; OS Chlamydia caviae (strain ATCC VR-813 / DSM 19441 / 03DC25 / GPIC) OS (Chlamydophila caviae). OC Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae; OC Chlamydia/Chlamydophila group; Chlamydia. OX NCBI_TaxID=227941; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC VR-813 / DSM 19441 / 03DC25 / GPIC; RX PubMed=12682364; DOI=10.1093/nar/gkg321; RA Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T., RA Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A., RA Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O., RA Salzberg S.L., Hsia R.-C., McClarty G., Rank R.G., Bavoil P.M., RA Fraser C.M.; RT "Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC): RT examining the role of niche-specific genes in the evolution of the RT Chlamydiaceae."; RL Nucleic Acids Res. 31:2134-2147(2003). 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; AE015925; AAP05419.1; -; Genomic_DNA. DR RefSeq; WP_011006634.1; NC_003361.3. DR AlphaFoldDB; Q822K5; -. DR SMR; Q822K5; -. DR STRING; 227941.CCA_00677; -. DR KEGG; cca:CCA_00677; -. DR eggNOG; COG0515; Bacteria. DR HOGENOM; CLU_303227_0_0_0; -. DR OrthoDB; 9788659at2; -. DR Proteomes; UP000002193; 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:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd14014; STKc_PknB_like; 1. DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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 PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1. DR PANTHER; PTHR43289:SF37; SERINE_THREONINE-PROTEIN KINASE A; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR SUPFAM; SSF48452; TPR-like; 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..930 FT /note="Serine/threonine-protein kinase PknD" FT /id="PRO_0000171190" 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 930 AA; 106618 MW; 37A2451522D344C1 CRC64; MQRYDIIRMI GKGGMGEVYL AYDPVCSRKV ALKRIREDLS DNELLKKRFL REAKIAADLV HPGVVPVFTI CSDSDPVYYT MPYIEGYTLK SLLKSVWQCD SLPKDLAEQT SVATFLSIFH KICSTVEYVH SRGILHRDLK PDNILLGLFS EVVILDWGAA LSKEMEEDFL SDIDVRIPGS LFSNMTIPGK IVGTPDYMAP ERLRGTPASE STDIYALGVI LYQMLTLSFP YRKKKGQKIS LRHQISFPEE IAPHREIPPF LSQVVMRALA ADPRERYRSV SALKADIEQH LQGSPEWTPK IVLHTQDREC WKFHEPILLS KYFPMLEVSP ALWYSLAISK IESFSEVRLE YTLLRKGLEE GFGILLPPSE GVDHGDFYHG YGFWLHIKEN ILSVSLVKNG LEIQKTSRHI DGNKEKFFIA FEKQNHRLSL IIDNIVWTIH MDYLPARGGR IGVIIQDVAD VCGNIVVLES SGSLQVSCLA VPDAFLNEKL YERAITFYRR IVESFPGRKE GYEAQFRIGI ALLEKASENS DSEGFIQALE EFSTLHNSVA APLEYLGKAL VYQRLGEYNE EVKSLLLALK RYCQRPEISR VRDHVVYRLH EALYSNHRIS LVFMLLALHV APESINASEE EHFLQNLHGK IQDTLFCNLD ISPVDFRSSK MELLLSYWSG FTPFLLGLFQ RSWDLKDYRA LADIFYTAAD LGNKEFIEEY SGILRENIRT TTFSKEIVEI LPDQLLCFLS GLEALTLQES IEKVFDGIEN LDPVLILYLF DLFAKDALIH GRGEEILKAI ALVEKYISPQ QRYRYLLPYE VLSYLWMKDA NKVYDLLSSY DESSWIDDSS HAFVLYGYWL ALAEDSSLAY LHLSGCREDS VFPRALIGVF CSPLGICEEQ LSYQERRQLL LQKFIFFHCL GNSEERDKCR TAYDSKERSL //