ID   A0PVS6_MYCUA            Unreviewed;       495 AA.
AC   A0PVS6;
DT   09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   Name=pknF {ECO:0000313|EMBL:ABL06445.1};
GN   OrderedLocusNames=MUL_4471 {ECO:0000313|EMBL:ABL06445.1};
OS   Mycobacterium ulcerans (strain Agy99).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium ulcerans group.
OX   NCBI_TaxID=362242 {ECO:0000313|EMBL:ABL06445.1, ECO:0000313|Proteomes:UP000000765};
RN   [1] {ECO:0000313|EMBL:ABL06445.1, ECO:0000313|Proteomes:UP000000765}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Agy99 {ECO:0000313|EMBL:ABL06445.1,
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; ABL06445.1; -; Genomic_DNA.
DR   RefSeq; WP_011742045.1; NC_008611.1.
DR   AlphaFoldDB; A0PVS6; -.
DR   KEGG; mul:MUL_4471; -.
DR   eggNOG; COG0515; 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:ABL06445.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000313|EMBL:ABL06445.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        335..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          12..378
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
SQ   SEQUENCE   495 AA;  52369 MW;  06E42CEACC234277 CRC64;
     MPLPPGSAFA GYTIVGLLGS GAMGEVYLAQ HPRLPRRDAL KVLPPDVSAD TAFRERFQRE
     ADLAATLLHP HIVGVHDRGE FNGQLWISMD YIEGTDAAAL IRSQYPAGMP VAEVVAVVTA
     VAGALDYAHQ RGLLHRDVKP ANILLTGPDN AGGPRIFLAD FGIARQLDDI SGITATNLTV
     GTAAYAAPEQ LTGADVDGRA DQYALAATAF HLLTGAPPYQ HANSVAVISQ HLTAPPPALG
     DRRSELAPLD RVFAAALAKQ PNERYWRCAD FAQALSQVAS PQGAAAAVSP SDPTLPVAIC
     VPPEYAAATQ AAPAPMPWYP TAPAPARPRR QVRTIVVPVV VALLLVSAVA FAVTQVLRPD
     PRQTTAAPAE APQWQPYVDH AKQFAISLTS VNPQTIDADI QRILDGSTGA FHSDFADKSA
     QFKQSIVDAG SATQGKATGA GLESISGTTA HVVVSVTSNI TKSTGVQQEP RQWRLRIQIE
     KIDDAYLASR VEFVT
//