ID   PKN1_CHLPN              Reviewed;         619 AA.
AC   Q7AJA5; Q7VQ75; Q9K228; Q9Z935;
DT   09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 108.
DE   RecName: Full=Serine/threonine-protein kinase pkn1;
DE            EC=2.7.11.1;
GN   Name=pkn1; OrderedLocusNames=CPn_0148, CP_0625, CPj0148, CpB0149;
OS   Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC   Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=83558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CWL029;
RX   PubMed=10192388; DOI=10.1038/7716;
RA   Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA   Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT   "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL   Nat. Genet. 21:385-389(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AR39;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J138;
RX   PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA   Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA   Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT   "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT   Japan and CWL029 from USA.";
RL   Nucleic Acids Res. 28:2311-2314(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW-183;
RA   Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA   Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT   "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT   other Chlamydia strains based on whole genome sequence analysis.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Together with the serine/threonine kinase PknD, may play a
CC       role in the specific interactions with host proteins during
CC       intracellular growth. {ECO:0000250}.
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   -!- 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;
CC   -!- PTM: Autophosphorylated on serine and threonine residues.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; AE001363; AAD18301.1; -; Genomic_DNA.
DR   EMBL; AE002161; AAF38440.1; -; Genomic_DNA.
DR   EMBL; BA000008; BAA98358.1; -; Genomic_DNA.
DR   EMBL; AE009440; AAP98082.1; -; Genomic_DNA.
DR   PIR; A72114; A72114.
DR   PIR; D81556; D81556.
DR   PIR; D86509; D86509.
DR   RefSeq; NP_224356.1; NC_000922.1.
DR   RefSeq; WP_010882798.1; NZ_LN847257.1.
DR   AlphaFoldDB; Q7AJA5; -.
DR   SMR; Q7AJA5; -.
DR   STRING; 406984.CPK_ORF00662; -.
DR   GeneID; 45050193; -.
DR   KEGG; cpa:CP_0625; -.
DR   KEGG; cpj:CPj0148; -.
DR   KEGG; cpn:CPn_0148; -.
DR   KEGG; cpt:CpB0149; -.
DR   PATRIC; fig|115713.3.peg.168; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG1262; Bacteria.
DR   HOGENOM; CLU_408763_0_0_0; -.
DR   OrthoDB; 9768004at2; -.
DR   Proteomes; UP000000583; Chromosome.
DR   Proteomes; UP000000801; 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-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.1580.10; paralog of FGE (formylglycine-generating enzyme); 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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   PANTHER; PTHR23150:SF19; FORMYLGLYCINE-GENERATING ENZYME; 1.
DR   PANTHER; PTHR23150; SULFATASE MODIFYING FACTOR 1, 2; 1.
DR   Pfam; PF03781; FGE-sulfatase; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..619
FT                   /note="Serine/threonine-protein kinase pkn1"
FT                   /id="PRO_0000171188"
FT   DOMAIN          15..302
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        141
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         21..29
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   CONFLICT        309
FT                   /note="V -> A (in Ref. 2; AAF38440)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        515
FT                   /note="I -> V (in Ref. 4; AAP98082)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   619 AA;  70355 MW;  CA312E28304D7D80 CRC64;
     MESEKDIGAK FLGDYRILYR KGQSLWSEDL LAEHRFIKKR YLIRLLLPDL GSSQPFMEAF
     HDVVVKLAKL NHPGILSIEN VSESEGRCFL VTQEQDIPIL SLTQYLKSIP RKLTELEIVD
     IVSQLASLLD YVHSEGLAQE EWNLDSVYIH ILNGVPKVIL PDLGFASLIK ERILDGFISD
     EENRESKIKE RVLLHTSEGK QGREDTYAFG AITYYLLFGF LPQGIFPMPS KVFSDFIYDW
     DFLISSCLSC FMEERAKELF PLIRKKTLGE ELQNVVTNCI ESSLREVPDP LESSQNLPQA
     VLKVGETKVS HQQKESAEHL EFVLVEACSI DEAMDTAIES ESSSGVEEEG YSLALQSLLV
     REPVVSRYVE AEKEEPKPQP ILTEMVLIEG GEFSRGSVEG QRDELPVHKV ILHSFFLDVH
     PVTNEQFIRY LECCGSEQDK YYNELIRLRD SRIQRRSGRL VIEPGYAKHP VVGVTWYGAS
     GYAEWIGKRL PTEAEWEIAA SGGVAALRYP CGEEIEKSRA NFFTADTTTV MSYPPNPYGL
     YDMAGNVYEW CQDWYGYDFY EISAQEPESP QGPAQGVYRV LRGGCWKSLK DDLRCAHRHR
     NNPGAVNSTY GFRCAKNIN
//