PKND_CHLCV
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 03-AUG-2022, entry version 110.
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=CCA_00677;
OS Chlamydia caviae (strain ATCC VR-813 / DSM 19441 / 03DC25 / GPIC)
OS (Chlamydophila caviae).
OC Bacteria; Chlamydiae; 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}.
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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 EnsemblBacteria; AAP05419; AAP05419; CCA_00677.
DR KEGG; cca:CCA_00677; -.
DR eggNOG; COG0515; Bacteria.
DR HOGENOM; CLU_303227_0_0_0; -.
DR OMA; VVILDWG; -.
DR OrthoDB; 1377603at2; -.
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: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 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
