PKND_CHLPN
ID PKND_CHLPN Reviewed; 932 AA.
AC Q9Z986; Q9K216;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 2.
DT 03-AUG-2022, entry version 142.
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};
GN OrderedLocusNames=CPn_0095, CP_0679, CPj0095, CpB0095;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiae; 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 Pkn1, may play a
CC role in the specific interactions with host proteins during
CC intracellular growth. {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 -!- PTM: Autophosphorylated on serine and threonine residues.
CC {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD18248.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA98305.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE001363; AAD18248.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE002161; AAF73695.1; -; Genomic_DNA.
DR EMBL; BA000008; BAA98305.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE009440; AAP98028.1; -; Genomic_DNA.
DR PIR; C72120; C72120.
DR PIR; G86502; G86502.
DR RefSeq; WP_010882745.1; NZ_LN847257.1.
DR AlphaFoldDB; Q9Z986; -.
DR SMR; Q9Z986; -.
DR STRING; 115711.CP_0679; -.
DR EnsemblBacteria; AAD18248; AAD18248; CPn_0095.
DR EnsemblBacteria; AAF73695; AAF73695; CP_0679.
DR GeneID; 45050140; -.
DR KEGG; cpa:CP_0679; -.
DR KEGG; cpj:CPj0095; -.
DR KEGG; cpn:CPn_0095; -.
DR KEGG; cpt:CpB0095; -.
DR eggNOG; COG0515; Bacteria.
DR HOGENOM; CLU_303227_0_0_0; -.
DR OrthoDB; 1377603at2; -.
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-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 3: Inferred from homology;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..932
FT /note="Serine/threonine-protein kinase PknD"
FT /id="PRO_0000171192"
FT DOMAIN 4..291
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 932 AA; 107410 MW; 47AAF87DF6CC5DF7 CRC64;
MERYDIVRII GKGGMGEVYL AYDPVCSRKV ALKKIREDLA ENPLLKRRFL REARIAADLI
HPGVVPVYTI YSEKDPVYYT MPYIEGYTLK TLLKSVWQKE SLSKELAEKT SVGAFLSIFH
KICCTIEYVH SRGILHRDLK PDNILLGLFS EAVILDWGAA VACGEEEDLL DIDVSKEEVL
SSRMTIPGRI VGTPDYMAPE RLLGHPASKS TDIYALGVVL YQMLTLSFPY RRKKGKKIVL
DGQRIPSPQE VAPYREIPPF LSAVVMRMLA VDPQERYSSV TELKEDIESH LKGSPKWTLT
TALPPKKSSS WKLNEPILLS KYFPMLEVSP ASWYSLAISN IESFSEMRLE YTLSKKGLNE
GFGILLPTSE NALGGDFYQG YGFWLHIKER TLSVSLVKNS LEIQRCSQDL ESDKETFLIA
LEQHNHSLSL FVDGTTWLIH MNYLPSRSGR VAIIVRDMED ILEDIGIFES SGSLRVSCLA
VPDAFLAEKL YDRALVLYRR IAESFPGRKE GYEARFRAGI TVLEKASTDN NEQEFALAIE
EFSKLHDGVA APLEYLGKAL VYQRLQEYNE EIKSLLLALK RYSQHPEIFR LKDHVVYRLH
ESFYKRDRLA LVFMILVLEI APQAITPGQE EKILVWLKDK SRATLFCLLD PTVLELRSSK
MELFLSYWSG FIPHLNSLFH RAWDQSDVRA LIEIFYVACD LHKWQFLSSC IDIFKESLED
QKATEEIVEF SFEDLGAFLF AIQSIFNKED AEKIFVSNDQ LSPILLVYIF DLFANRALLE
SQGEAIFQAL DLIRSKVPEN FYHDYLRNHE IRAHLWCRNE KALSTIFENY TEKQLKDEQH
ELFVLYGCYL ALIQGAEAAK QHFDVCREDR IFPASLLARN YNRLGLPKDA LSYQERRLLL
RQKFLYFHCL GNHDERDLCQ TMYHLLTEEF QL
