PKND_CHLT2
ID PKND_CHLT2 Reviewed; 934 AA.
AC P0DPS9; 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 15.
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, ECO:0000269|PubMed:14500499};
GN Name=pknD {ECO:0000255|HAMAP-Rule:MF_01957}; OrderedLocusNames=CTL0553;
OS Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=471472;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A KINASE, CATALYTIC
RP ACTIVITY, INTERACTION WITH PKN1, DEVELOPMENTAL STAGE, INDUCTION, AND
RP AUTOPHOSPHORYLATION.
RC STRAIN=L2;
RX PubMed=14500499; DOI=10.1128/iai.71.10.5772-5784.2003;
RA Verma A., Maurelli A.T.;
RT "Identification of two eukaryote-like serine/threonine kinases encoded by
RT Chlamydia trachomatis serovar L2 and characterization of interacting
RT partners of Pkn1.";
RL Infect. Immun. 71:5772-5784(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=434/Bu / ATCC VR-902B;
RX PubMed=18032721; DOI=10.1101/gr.7020108;
RA Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P.,
RA Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D.,
RA Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.;
RT "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
RT venereum isolates.";
RL Genome Res. 18:161-171(2008).
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 (Probable). Autophosphorylates and also
CC phosphorylates Pkn1 (PubMed:14500499). {ECO:0000269|PubMed:14500499,
CC ECO:0000305|PubMed:14500499}.
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 ECO:0000269|PubMed:14500499};
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 ECO:0000269|PubMed:14500499};
CC -!- SUBUNIT: Interacts with Pkn1. {ECO:0000269|PubMed:14500499}.
CC -!- DEVELOPMENTAL STAGE: Detected in isolated elementary bodies 40 hours
CC post-infection (at protein level). {ECO:0000269|PubMed:14500499}.
CC -!- INDUCTION: Transcribed after 6 hours in infected mouse fibroblast
CC cells, that is from the mid-phase of the developmental cycle.
CC {ECO:0000269|PubMed:14500499}.
CC -!- PTM: Autophosphorylated on serine and threonine residues (By
CC similarity) (PubMed:14500499). Present in elementary bodies 40 hours
CC post-infection as 2 bands of approximately 55 to 60 and 45 to 50 kDa,
CC which may be due to differential phosphorylation as well as
CC degradation; an enzymatically active full-length protein can also be
CC detected (PubMed:14500499). {ECO:0000255|HAMAP-Rule:MF_01957,
CC ECO:0000269|PubMed:14500499}.
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; AY148436; AAN71626.1; -; Genomic_DNA.
DR EMBL; AM884176; CAP03993.1; -; Genomic_DNA.
DR RefSeq; WP_009873709.1; NC_010287.1.
DR RefSeq; YP_001654629.1; NC_010287.1.
DR AlphaFoldDB; P0DPS9; -.
DR SMR; P0DPS9; -.
DR EnsemblBacteria; CAP03993; CAP03993; CTL0553.
DR KEGG; ctb:CTL0553; -.
DR OMA; VVILDWG; -.
DR Proteomes; UP000000795; 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 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..934
FT /note="Serine/threonine-protein kinase PknD"
FT /id="PRO_1000188972"
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"
FT CONFLICT 47
FT /note="K -> Q (in Ref. 1; AAN71626)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="V -> I (in Ref. 1; AAN71626)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="A -> G (in Ref. 1; AAN71626)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="M -> I (in Ref. 1; AAN71626)"
FT /evidence="ECO:0000305"
FT CONFLICT 420
FT /note="Y -> S (in Ref. 1; AAN71626)"
FT /evidence="ECO:0000305"
FT CONFLICT 629..633
FT /note="VREEK -> LREEE (in Ref. 1; AAN71626)"
FT /evidence="ECO:0000305"
FT CONFLICT 686
FT /note="E -> G (in Ref. 1; AAN71626)"
FT /evidence="ECO:0000305"
FT CONFLICT 773
FT /note="I -> M (in Ref. 1; AAN71626)"
FT /evidence="ECO:0000305"
FT CONFLICT 859
FT /note="A -> V (in Ref. 1; AAN71626)"
FT /evidence="ECO:0000305"
FT CONFLICT 869
FT /note="Y -> D (in Ref. 1; AAN71626)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 934 AA; 107754 MW; B20500268C18D316 CRC64;
MQRYELIRLI GKGGMGEVYL AHDKACSRRV ALKRIREDLS GNALLRKRFL REAKIAADLI
HPGIVPVYSI CSDGEAVYYT MPYIEGFSLK SLLKSVWQKE VLSKELEEKT SVKSFLPIFD
KICATVEYIH SKGVLHRDLK PDNILLGLFG EVVIVDWGAA 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 KSQEMISQQY
RFAILIEKSD NRIAVFVEQA LFILHIDYLP SLGNRLGVII QDLQGMSNIA ISESIGALRV
SCLAVPDAFL SEKLYDQAAI FYRKIRDSFP GRKESYEAQF RLGVTLLTQI EEQGGDLTQA
LSSFDYLHGG AGAPLEYLGK ALVYQRNGSF VEEIRCLLFA LKRYSQHPEI PRLEDHLCFR
LYDSLHKHRS EALVFMLLIL WIAPEKISVR EEKRFLRIIY HKQQATLFCQ VDKAPLQFRS
SKMELFLSFW TGFSLFLPEL FRRAGELRDY QALADIFYVA GVSGNREAFM QFSTALANVS
DEITFPESLH NQKVAELMFF VKGVEALRNK DYQKAKKLLW KTPFTLQLYA LDIFHIQAFL
DEEIESFIDL LQAIYDPASE EERDHILVYI IQTHLWNRDL ERAYKLLNDR FPLDEELAEY
SEAFILWGCY LALTGDRVAV KAHFSRCRYK YGKSALIGKC VDGDIFDYLD NLVWWEKKMT
LFQSYFLLRC LNESPRRYEK YRQAYLSMEN NFFD
