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PKNS_MYCPN
ID   PKNS_MYCPN              Reviewed;         389 AA.
AC   P75524;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Putative serine/threonine-protein kinase;
DE            EC=2.7.11.1;
GN   OrderedLocusNames=MPN_248; ORFNames=MP584;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; U00089; AAB96232.1; -; Genomic_DNA.
DR   PIR; S73910; S73910.
DR   RefSeq; NP_109936.1; NC_000912.1.
DR   RefSeq; WP_010874605.1; NC_000912.1.
DR   AlphaFoldDB; P75524; -.
DR   SMR; P75524; -.
DR   IntAct; P75524; 1.
DR   STRING; 272634.MPN_248; -.
DR   PRIDE; P75524; -.
DR   EnsemblBacteria; AAB96232; AAB96232; MPN_248.
DR   KEGG; mpn:MPN_248; -.
DR   PATRIC; fig|272634.6.peg.267; -.
DR   HOGENOM; CLU_700090_0_0_14; -.
DR   OMA; LAMEWIQ; -.
DR   BioCyc; MPNE272634:G1GJ3-392-MON; -.
DR   Proteomes; UP000000808; 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   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 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; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..389
FT                   /note="Putative serine/threonine-protein kinase"
FT                   /id="PRO_0000171202"
FT   DOMAIN          15..356
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        164
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
SQ   SEQUENCE   389 AA;  44882 MW;  838E5CDB5AD49B15 CRC64;
     MALNLKIGDI VQNKYRIEKL INRGGMNSYL FLASNLHVQE FGPLQKRQFT RLVLKVVQRT
     DKINDNNWKK FLDGTITTTR VSHKNLVQTF DVVSPRLSVL SENQVIVLED TVMIVMEYVD
     GPSLREMLNQ KGYFSVQEVV YYFTKLVKVI NYLHSFEHQI IHRDLKPENI LFTSNLTDIK
     LLDFGIASAV IRNAEKTEVL TDENSLFGTV SYMTPEVLES TVNKEGKRIR KPPTVQYDIY
     SLGVILFEML VGRVPFNKSI DPKKERETIQ KARNFDVPLM GNLRSDVPVS LENIVFKCTA
     VKRENSKWMY SDTKQLLADL AQWQTEQTLI KPVHERILEG QNEMRELMVS NYLPWYLRKG
     VLIFFSVVLL ALLIAVVSFF IITGVVVHS
 
 
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