PKND_CHLTR
ID PKND_CHLTR Reviewed; 934 AA.
AC P0DPS8; B0B7L7; O84303; Q8GDH7;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2019, sequence version 1.
DT 03-AUG-2022, entry version 13.
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=CT_301;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
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 (By similarity). Autophosphorylates and also
CC phosphorylates Pkn1 (By similarity). {ECO:0000250|UniProtKB:B0B7L7,
CC 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 -!- SUBUNIT: Interacts with Pkn1. {ECO:0000250|UniProtKB:B0B7L7}.
CC -!- PTM: Autophosphorylated on serine and threonine residues.
CC {ECO:0000250|UniProtKB:B0B7L7, 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; AE001273; AAC67894.1; -; Genomic_DNA.
DR PIR; G71532; G71532.
DR RefSeq; NP_219806.1; NC_000117.1.
DR RefSeq; WP_009871648.1; NC_000117.1.
DR AlphaFoldDB; P0DPS8; -.
DR SMR; P0DPS8; -.
DR STRING; 813.O172_01615; -.
DR EnsemblBacteria; AAC67894; AAC67894; CT_301.
DR GeneID; 884825; -.
DR KEGG; ctr:CT_301; -.
DR OMA; VVILDWG; -.
DR Proteomes; UP000000431; 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; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
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 Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..934
FT /note="Serine/threonine-protein kinase PknD"
FT /id="PRO_0000171193"
FT DOMAIN 4..296
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 934 AA; 107666 MW; A06EC6F4B025DADB CRC64;
MQRYELIRLI GKGGMGEVYL AHDKACSRRV ALKRIREDLS GNALLRQRFL REAKIAADLI
HPGIVPVYSI CSDGEAVYYT MPYIEGFSLK SLLKSVWQKE VLSKELEEKT SVKSFLPIFD
KICATVEYIH SKGVLHRDLK PDNILLGLFG EVVIIDWGAA IFKHAKELKL EQDDEAAVSF
DERNICYSSM TIPGKIVGTP DYMAPESLLG VEASEKTDIY ALGLILYQML TLAFPYRRKK
GRKLSYRDVV LPPIEMSPYR EIPPSLSQIA MKAIAINPAD RFSSIQELRQ ALQPYLQGDP
EWTVKATLMA KEKSCWKYYD PILLSRYFPV LASSPAQWYN FMLSEVEISA STRVEYTVTK
SAVHEGMGIL FLPSKEAERG EFYCGYGLWF SVQNHELTVS LIKNGIEIQK KSQEMISQQS
RFAILIEKSD NRIAVFVEQA LFILHIDYLP SLGNRLGVII QDLQGMSNIA ISESIGALRV
SCLAVPDAFL SEKLYDQAAI FYRKIRDSFP GRKESYEAQF RLGVTLLTQI EEQGGDLTQA
LSSFDYLHGG AGAPLEYLGK ALVYQRNGSF VEEIRCLLFA LKRYSQHPEI PRLEDHLCFR
LYDSLHKHRS EALVFMLLIL WIAPEKISVR EEERFLRIIY HKQQATLFCQ VDKAPLQFRS
SKMELFLSFW TGFSLFLPEL FRRAGGLRDY QALADIFYVA GVSGNREAFM QFSTALANVS
DEITFPESLH NQKVAELMFF VKGVEALRNK DYQKAKKLLW KTPFTLQLYA LDMFHIQAFL
DEEIESFIDL LQAIYDPASE EERDHILVYI IQTHLWNRDL ERAYKLLNDR FPLDEELAEY
SEAFILWGCY LALTGDRVVV KAHFSRCRYK YGKSALIGKC VDGDIFDYLD NLVWWEKKMT
LFQSYFLLRC LNESPRRYEK YRQAYLSMEN NFFD
