PKN1_CHLT2
ID PKN1_CHLT2 Reviewed; 614 AA.
AC A0A0H3MBJ2; O84147; Q8GDH8;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=Serine/threonine-protein kinase Pkn1;
DE EC=2.7.11.1 {ECO:0000269|PubMed:14500499};
GN Name=pkn1; OrderedLocusNames=CTL0400;
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 INCG AND PKND, DEVELOPMENTAL STAGE, INDUCTION,
RP AUTOPHOSPHORYLATION, PHOSPHORYLATION OF INCG, AND MUTAGENESIS OF LYS-42.
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 PknD, may play a
CC role in specific interactions with host proteins during host
CC intracellular growth (Probable). Autophosphorylates and phosphorylates
CC IncG, an inclusion-membrane protein required for the modification of
CC the nascent chlamydial inclusion (PubMed:14500499).
CC {ECO:0000269|PubMed:14500499, 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: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:0000269|PubMed:14500499};
CC -!- SUBUNIT: Interacts with PknD, interacts with and phosphorylates IncG.
CC {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: Autophosphorylates on serine and threonine residues
CC (PubMed:14500499). Present in elementary bodies 40 hours post-infection
CC as 2 proteins of approximately 70 and 65 kDa; the smaller one may be
CC due to differential phosphorylation or degradation (PubMed:14500499).
CC {ECO:0000269|PubMed:14500499}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000305|PubMed:14500499}.
CC -!- CAUTION: Gln-136 is present instead of the conserved Asp which is
CC expected to be a proton acceptor in the active site.
CC {ECO:0000305|PubMed:14500499}.
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DR EMBL; AY148435; AAN71625.1; -; Genomic_DNA.
DR EMBL; AM884176; CAP03840.1; -; Genomic_DNA.
DR RefSeq; WP_009873593.1; NC_010287.1.
DR RefSeq; YP_001654484.1; NC_010287.1.
DR AlphaFoldDB; A0A0H3MBJ2; -.
DR SMR; A0A0H3MBJ2; -.
DR EnsemblBacteria; CAP03840; CAP03840; CTL0400.
DR KEGG; ctb:CTL0400; -.
DR PATRIC; fig|471472.4.peg.431; -.
DR HOGENOM; CLU_408763_0_0_0; -.
DR OMA; TQANFFS; -.
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-EC.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 3.90.1580.10; -; 1.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR005532; SUMF_dom.
DR InterPro; IPR042095; SUMF_sf.
DR Pfam; PF03781; FGE-sulfatase; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Transferase.
FT CHAIN 1..614
FT /note="Serine/threonine-protein kinase Pkn1"
FT /id="PRO_0000446192"
FT DOMAIN 13..276
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 19..27
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MUTAGEN 42
FT /note="K->A: No autophosphorylation; protein can be
FT phosphorylated by PknD."
FT /evidence="ECO:0000269|PubMed:14500499"
FT CONFLICT 2
FT /note="E -> D (in Ref. 1; AAN71625)"
FT /evidence="ECO:0000305"
FT CONFLICT 14
FT /note="K -> R (in Ref. 1; AAN71625)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="H -> R (in Ref. 1; AAN71625)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="G -> R (in Ref. 1; AAN71625)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 614 AA; 69638 MW; 3799DB0D21D19618 CRC64;
MEERAAVEYW GDYKVIAELG HGLWSRDVLA EHRFIKKRYI LKILPSELSS SENFMRVFQE
VIVQLAAIRH ASLVAIENVS REGDRYFVVT EENGGTISLA QYLSGRKLSE EEVVHLIQQL
CDALELVHSI GLAHGQIHLH SVHVSFFNGI ANIYLPEVGF ASLLRERMFS TIMQSGSARE
SITRIRDLLM FEAPEEQEVF GREADVYSVG VLAYYLLVGS FPWGSFPKPS LCMPDSWYDW
DGFILSCLQQ QREARPKCLR EALRRKTSGE QLQVTLDSCR EPLREMEIED TPTELGPPSA
LIREGERLCE VKEEQHAFVL VEAKSIDEAM VTTVDSEEEL ESSEGYANPL QSLLAREPVV
SRYVEVEREE IKPQPLLTEM IFIEGGEFSR GSGDGQRDEL PVHNITLPGF FLDIHPVTNE
QFVRFLECVG SEQDEHYNEL IRLKDSRIQR RSGRLIIEPG YAKHPVVGVT WYGASSYACW
IGKRLPSEAE WEVAASGGKL GLRYPTGEEI DKSKANFFSS DTTPVMSYPS SILGLYDMAG
NVYEWCQDWY SYDFYESSAL EPDAPLGPPQ GVYRVLRGGC WKSLKDDLRC AHRHRNNPGA
INSTYGFRCA KDVK
