ID   PKN1_CHLCV              Reviewed;         618 AA.
AC   Q822R1;
DT   09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Serine/threonine-protein kinase pkn1;
DE            EC=2.7.11.1;
GN   Name=pkn1; OrderedLocusNames=CCA_00618;
OS   Chlamydia caviae (strain ATCC VR-813 / DSM 19441 / 03DC25 / GPIC)
OS   (Chlamydophila caviae).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=227941;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-813 / DSM 19441 / 03DC25 / GPIC;
RX   PubMed=12682364; DOI=10.1093/nar/gkg321;
RA   Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T.,
RA   Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A.,
RA   Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O.,
RA   Salzberg S.L., Hsia R.-C., McClarty G., Rank R.G., Bavoil P.M.,
RA   Fraser C.M.;
RT   "Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC):
RT   examining the role of niche-specific genes in the evolution of the
RT   Chlamydiaceae.";
RL   Nucleic Acids Res. 31:2134-2147(2003).
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}.
CC   -!- CAUTION: Gly-141 is present instead of the conserved Asp which is
CC       expected to be an active site residue. {ECO:0000305}.
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DR   EMBL; AE015925; AAP05360.1; -; Genomic_DNA.
DR   RefSeq; WP_011006575.1; NC_003361.3.
DR   AlphaFoldDB; Q822R1; -.
DR   SMR; Q822R1; -.
DR   STRING; 227941.CCA_00618; -.
DR   PRIDE; Q822R1; -.
DR   EnsemblBacteria; AAP05360; AAP05360; CCA_00618.
DR   KEGG; cca:CCA_00618; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG1262; Bacteria.
DR   HOGENOM; CLU_408763_0_0_0; -.
DR   OMA; TQANFFS; -.
DR   OrthoDB; 1377603at2; -.
DR   Proteomes; UP000002193; 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: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   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..618
FT                   /note="Serine/threonine-protein kinase pkn1"
FT                   /id="PRO_0000171186"
FT   DOMAIN          15..381
FT                   /note="Protein kinase"
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   BINDING         44
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   618 AA;  70173 MW;  0D0003F43DA35F79 CRC64;
     MEGEQDIGVE FLGDYKILCY LRKGLWCQDI LAEHRFIKKR YILKLLCSEL SSSEAFMTAF
     HEAIIKLATI RHPGIISIEN VSQAEGQYFL VTEEKEVPTL SLAQYLSSCS QGLSELEAKD
     LICQLAEILD YAHANRLIHG GLSLDSVHID LTGQSPKVFL PELGFSFLLK DQYTQSLLRD
     SSEKSSFDKL KQILLFQAPE TALGTVAEDV YAFGVIVYFL LFRQLPQGAF PLPSEAFPEY
     VYDWDRLIQS CLSYAVEKRP KKLAPLLVKK TLGEQFLAAK IQCSEEDLRE IEEEPQVPSV
     ANILQKVEDK IIEETSDHLE FVLVEAKSID EAMNTSVDSK EEVVAEDESY SNALQSLLIR
     EPVVSRYVEE EKEEVKPQPL FTEMVFIEGG KFLRGSREGQ RDEHPVHEIF LHSFFLDIHP
     VTNEQFVRYL ECSGSEQDKY YNELIRLKDS RIQRRSGKLV IEPGYAKHPV VGVTWYGASG
     YASWVGKRLP TEAEWEIASC GGVTQLRYPC GEEIDKSQAN FFSSDTTPVM SYPANPYGLY
     DMAGNVYEWC EDWYGYDFYE ISAQESHAPQ GPAQGVYRVL RGGCWKSLKD DLRCAHRHRN
     NPGAVNSTYG FRCAKGVK