ID   A0PQI2_MYCUA            Unreviewed;       654 AA.
AC   A0PQI2;
DT   09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 85.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   OrderedLocusNames=MUL_2200 {ECO:0000313|EMBL:ABL04601.1};
OS   Mycobacterium ulcerans (strain Agy99).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium ulcerans group.
OX   NCBI_TaxID=362242 {ECO:0000313|EMBL:ABL04601.1, ECO:0000313|Proteomes:UP000000765};
RN   [1] {ECO:0000313|EMBL:ABL04601.1, ECO:0000313|Proteomes:UP000000765}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Agy99 {ECO:0000313|EMBL:ABL04601.1,
RC   ECO:0000313|Proteomes:UP000000765};
RX   PubMed=17210928; DOI=10.1101/gr.5942807;
RA   Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA   Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA   Johnson P.D., Davies J.K., Jenkin G.A., Small P.L., Jones L.M., Tekaia F.,
RA   Laval F., Daffe M., Parkhill J., Cole S.T.;
RT   "Reductive evolution and niche adaptation inferred from the genome of
RT   Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL   Genome Res. 17:192-200(2007).
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:0000256|ARBA:ARBA00001433};
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:0000256|ARBA:ARBA00000775};
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; CP000325; ABL04601.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0PQI2; -.
DR   KEGG; mul:MUL_2200; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG0728; Bacteria.
DR   HOGENOM; CLU_000288_63_44_11; -.
DR   Proteomes; UP000000765; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0080090; P:regulation of primary metabolic process; IEA:UniProt.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF6; SERINE_THREONINE-PROTEIN KINASE NEKL-3; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:ABL04601.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000313|EMBL:ABL04601.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        474..500
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          12..276
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          305..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          444..469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        316..330
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   654 AA;  69725 MW;  5AD0085D6CA893DE CRC64;
     MPLNEGDIFA GYVIQRLLGT GGMGEVYLAQ HPRLPRLDAL KILSLDATDD DEFRARFTRE
     AELAATLWHP HIVGVHDRGE FDGRLWISMD YVDGTDTRHL VEQRYRSGMP LEDVIEIVTA
     VAEALDFAHE RRLLHRDVKP ANILVTEPSE SARRRVLLTD FGIAREIDDK HRLTEAQMAI
     GTVAYAAPEQ LTGRPLDGRA DQYALAATAF HLLAGVPPFD HSNRAVVVGQ HLNMPPPRIS
     KRHPKLAHLD AAFAKALAKD PDDRYPRCID FAKALAAGPG SIAEHQARRG ATSTEPFDVN
     AEMSAEALEP ARPSGTAPSA QAQPHPSEAG VSTASLGAAD QPGAGKARHT KRLERMTVDG
     TAVSVQKRPA GPEQDEEVWL FCVQRYESTG EPHTVIPVEL RGTSITGQLA NGDAVGVSGI
     WDGSTLFADA VVNYTAANRG RRRSSALKVE GGLKEGEASA PARPPGSKSR KGRAFAIVAA
     LLALAAIAVA AVLTHGFGLW STSEPGPVVK AQQATVFSPG GTPDHPGQAG LAIDGDPNSA
     WPTDTYVDAT PFPAFKQGVG LILRLAKPTA LSEVTIDVPS TGTEVQIRAA GSATPASLSD
     TTALTPNVAL HPGHNRIRVD STTKTANVLV WISKLGTTKG ESRNAISDIT LRAR
//