ID   A0PWF4_MYCUA            Unreviewed;       979 AA.
AC   A0PWF4;
DT   09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   SubName: Full=Serine/threonine-protein kinase transcriptional regulatory protein PknK_3 {ECO:0000313|EMBL:ABL06673.1};
GN   Name=pknK_3 {ECO:0000313|EMBL:ABL06673.1};
GN   OrderedLocusNames=MUL_4753 {ECO:0000313|EMBL:ABL06673.1};
OS   Mycobacterium ulcerans (strain Agy99).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium ulcerans group.
OX   NCBI_TaxID=362242 {ECO:0000313|EMBL:ABL06673.1, ECO:0000313|Proteomes:UP000000765};
RN   [1] {ECO:0000313|EMBL:ABL06673.1, ECO:0000313|Proteomes:UP000000765}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Agy99 {ECO:0000313|EMBL:ABL06673.1,
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC       Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}.
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DR   EMBL; CP000325; ABL06673.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0PWF4; -.
DR   KEGG; mul:MUL_4753; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG3903; Bacteria.
DR   HOGENOM; CLU_004665_5_3_11; -.
DR   Proteomes; UP000000765; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0031326; P:regulation of cellular biosynthetic process; IEA:UniProt.
DR   CDD; cd14014; STKc_PknB_like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR47691:SF3; HTH-TYPE TRANSCRIPTIONAL REGULATOR RV0890C-RELATED; 1.
DR   PANTHER; PTHR47691; REGULATOR-RELATED; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:ABL06673.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Transferase {ECO:0000313|EMBL:ABL06673.1}.
FT   DOMAIN          4..261
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         33
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   979 AA;  105193 MW;  C0FCFF73955465B3 CRC64;
     MDGFADAAEV GRGGFGVVYR CRQVDLDRVV AIKVLTIDLD ENRPRFEREQ RAMAKLTGHP
     NIVSVLQIGE TRDGHPYLVM PYCRRGSVQT EISRLGRLSL ADILQLGVAL AAGLESAHRL
     DILHRDIKPA NVLLTDFGEP ALTDFGLAHM AGGFRTATGL FTASPAFTAS ELARGGEPDR
     ASDVYGVGAT LFCALTGHPP FERRKGESVI AQILRVANDP VPDLAEYDVA EDVASVVNRA
     LSRDPAARPT MVELGEAIQS LQAAHGQAVD AMALEGGKRS TSVSSESAWH VSARQTRGNL
     PAKLAGFVGR QAELAELGAL ISTSRPVTLT GVGGVGKTSL AVQAAGEHVS HFHDGVWLVD
     IGELSDGALL AGLAARMLGI RDQGARPLTE VLTDALAERD ALVIFDGCEH VIDHAAQLID
     TLLQGCPQLH ILATSRELLG IGGEAVLALS PLPYPDAASV SSRSSVARYD AVALFVERAR
     TARPGFTLTQ RNAAAVARIC ERLDGLPLAI ELAAARLRAV SVEQIADRLS DRFGLLTRGQ
     RGAPTRQQTL SYCIDWSYDH CTPIQQQLWA RLSVFAGSFD LDAAQYVAPQ DMDADDLLDE
     LCALVDKSIL IRTEDDGAVR FRLLSTMREY GNSRIDAEQY QGLQQSHFDW CERLVTQAHL
     EWFSRKQVDW IHRLRSELPN IEEALQFGLE KAPESVLLMA AKLRNLFVVS GKLQVGRLWV
     ERALSTTTSA QPSGARIAAL AALAMFAVLQ TDWPTAQSCV AQAHEHGAAV PDPIAESLLG
     VARGLGALLQ GQVEQVQTDA EQGLAAGDFE LQVLGMWLMP LRHLAVGDPE PALRWAEKAH
     SVSESRVEVQ MRTYSLSALA VSHLMLGDTG SAERSLREGL KLCQVIDDPW SGASYLEGLA
     WTAGANGNLR RAVVLMAAAA ALSRSSGAGS TVIALVGSMH QQCERAAREE LSDAVFETAR
     VEGESLSFDD AADVALTEP
//