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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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