PKND_CHLAB
ID PKND_CHLAB Reviewed; 933 AA.
AC Q5L5J7;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=CAB647;
OS Chlamydia abortus (strain DSM 27085 / S26/3) (Chlamydophila abortus).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=218497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27085 / S26/3;
RX PubMed=15837807; DOI=10.1101/gr.3684805;
RA Thomson N.R., Yeats C., Bell K., Holden M.T.G., Bentley S.D.,
RA Livingstone M., Cerdeno-Tarraga A.-M., Harris B., Doggett J., Ormond D.,
RA Mungall K., Clarke K., Feltwell T., Hance Z., Sanders M., Quail M.A.,
RA Price C., Barrell B.G., Parkhill J., Longbottom D.;
RT "The Chlamydophila abortus genome sequence reveals an array of variable
RT proteins that contribute to interspecies variation.";
RL Genome Res. 15:629-640(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}.
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DR EMBL; CR848038; CAH64094.1; -; Genomic_DNA.
DR RefSeq; WP_011097231.1; NC_004552.2.
DR AlphaFoldDB; Q5L5J7; -.
DR SMR; Q5L5J7; -.
DR EnsemblBacteria; CAH64094; CAH64094; CAB647.
DR KEGG; cab:CAB647; -.
DR eggNOG; COG0515; Bacteria.
DR HOGENOM; CLU_303227_0_0_0; -.
DR OMA; VVILDWG; -.
DR OrthoDB; 1377603at2; -.
DR Proteomes; UP000001012; 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_0000239300"
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; 106836 MW; FF1C265A91BE1A29 CRC64;
MQHYDIIRMI GKGGMGEVYL AYDPICSRKV ALKRIREDLS DNELLKKRFL REAKIAADLV
HPGVVPVFTI CSDSDLVYYT MPYIEGYTLK SLLKSVWQCD SLPKDLAEQT SVGTFLSIFH
KICSTIEYVH SRGILHRDLK PDNILLGLFS EVVILDWGAA LSKEMKEDVL LDLDIPMPGS
MFSNMTVPGK IVGTPDYMAP ERLRGAPASE STDIYALGVI LYQMLTLSFP YRNKKGKKIH
VPNHIISPEE VAPHREIPSF LSQVVMRALA TDPKERYTSV QALKADIEQH LQGSPQWTPK
IALHTQDAEC WKFHESILLS KYFPMLEVSP ALWYSLAISK IESFSEVRLE YTLLRKGLEG
GFGILLPPSE NVDHGDFYRG YGFWLHIKKN VLSVSLVRNG LEIQKTSGNI DVNQEKFFIA
FEKQNHRLSL NIDHTVWMIH MDYLPGRGGR IGVIIQDITD VCGNIVVLES SGALHVSCLA
VPDAFLNEKL YDRAITFYRR IVESFPGRKE GYEAQFRIGI AVLEKAAEEG DQEGFSQALR
EFSVLHDSVA APLEYLGKAL VYQRLEEYNE EVKSLLLALK RYGQRPEISR VRDHVVDRLH
EALYSNHRVS LVFMLLALHV APESINSSEE EHFLKNLQGK IHDTLFCSLD ISPIDFRSSK
MELLLSYWSG FTPFLPGLFQ RSWDLKDYRA LADIFYTAAD LGEREFIDVY GNTLRENIQA
TTFTEDIVEI FPHQLIHFLS ALDAIFLHAP VEKIFSDVDI LDPVLIIYLF DLFAKDVLIH
GKGEQILDAI QVLETYVSPQ QRHTYLLPYE ILAYLWMKEG KKVHELLSAH YDESFWIEDS
HWAFVLYGYW LALTEESSLA YLHLSGCRED HVAPRALIGL FCSPLGICEN QWSYQERRNL
LLQKFIFFHC LGDDVERDNC RVAYDLLVKE RLL
