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Database: UniProt
Entry: U5WS34_MYCKA
LinkDB: U5WS34_MYCKA
Original site: U5WS34_MYCKA 
ID   U5WS34_MYCKA            Unreviewed;      1111 AA.
AC   U5WS34;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=Serine/threonine-protein kinase PknK {ECO:0000256|PIRNR:PIRNR000574};
DE            EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR000574};
DE   AltName: Full=Protein kinase K {ECO:0000256|PIRNR:PIRNR000574};
GN   ORFNames=MKAN_16730 {ECO:0000313|EMBL:AGZ51737.1};
OS   Mycobacterium kansasii ATCC 12478.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=557599 {ECO:0000313|EMBL:AGZ51737.1, ECO:0000313|Proteomes:UP000017786};
RN   [1] {ECO:0000313|EMBL:AGZ51737.1, ECO:0000313|Proteomes:UP000017786}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12478 {ECO:0000313|EMBL:AGZ51737.1,
RC   ECO:0000313|Proteomes:UP000017786};
RG   McGill University Mycobacterium genome consortium;
RA   Veyrier F.J., Behr M.A.;
RT   "Genome sequence of Mycobacterium kansasii.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
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         ECO:0000256|PIRNR:PIRNR000574};
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         ECO:0000256|PIRNR:PIRNR000574};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC       Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC       {ECO:0000256|PIRNR:PIRNR000574}.
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DR   EMBL; CP006835; AGZ51737.1; -; Genomic_DNA.
DR   RefSeq; WP_023369774.1; NC_022663.1.
DR   AlphaFoldDB; U5WS34; -.
DR   GeneID; 29698961; -.
DR   KEGG; mkn:MKAN_16730; -.
DR   eggNOG; COG0515; Bacteria.
DR   eggNOG; COG2909; Bacteria.
DR   HOGENOM; CLU_006325_2_0_11; -.
DR   OrthoDB; 136365at2; -.
DR   Proteomes; UP000017786; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0031326; P:regulation of cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:0080090; P:regulation of primary metabolic 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; IPR041664; AAA_16.
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; IPR016236; Ser/Thr_kinase_PknK_prd.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 1.
DR   Pfam; PF13191; AAA_16; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PIRSF; PIRSF000574; Ser/Thr_PK_PknK_prd; 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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000574};
KW   Kinase {ECO:0000256|PIRNR:PIRNR000574, ECO:0000313|EMBL:AGZ51737.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR000574};
KW   Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR000574,
KW   ECO:0000313|EMBL:AGZ51737.1}; Transferase {ECO:0000256|PIRNR:PIRNR000574}.
FT   DOMAIN          26..283
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          310..337
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         55
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1111 AA;  120372 MW;  6B82BF16A8884F8E CRC64;
     MVDVDSHPTQ RGLVPDIPAE LREAGFDEVA EIGCGGFGVV YRCAQPLLDR TVAVKVLTTD
     LDPENLERFL REQHAMGKLS GHPNIVTILQ VGSTVSGRPF IVMPYHAKNS LESLIRRHGP
     LDWVETLRMG VKLAGALEAA HRAGILHRDV KPANILLTEY GEPELTDFGI ARMSGGFQTA
     TGIITGSPAF TAPEVLEGKA PTPASDLYSL GATLFCALTG HAAFERRSGE KVVAQFLRIT
     SQPVPDLREH GLPADVAAVI ERAMARDPAA RPPGAAAFGN ELREVQRISG VAVDEMALPV
     DLGVERRTSP VAPSAVRRDT GATPTPPTPT TKYRPPVPTR SLVVRNRLLD VVRAGGLRRL
     VLIHAPSGFG KSTLAAQWRE ELSRAPVGVG WLTIDDDDNN VVWFLAHLLE SIRQVRPALA
     ASLGQVLDEH GDDAARYVLT ALIDEIHQND DRLVVVIDDW HRVSDTQTIG ALGFLLERGC
     HHLQAVVTSW SRAGLPVSKL RIRDELVEID CEALRFDFDE ARSLLNDVDG LLLPDGDVRA
     LTTSTDGWVA ALQLAALSLR GGADAASLVS RMSGASEMIG DFLAENVLDS LEPELLEFLL
     ATSITERTCG GLASALAAVP RGQAMLEDVE QRGLFLQRID KDPNWFRYHH LFAEFLRHRL
     ERDHPDRVYQ LHRVAADWFA EHDHLNEAVD HALASGDAAR AVDLVEQDET NLLEQSKMTT
     LLEIVKKLPP RMVVSRARLQ LTLAWTNVLL QRLAPAAAAL KSFETALDRA DLSDVTRADL
     RVEADVLRAV GEVFADRVDA IDHLVAEALA RPDSFHPRVG GVAGSLAAFA AVHRFEFDAA
     NRLLAWAEPY QEMMGPFAGV YAHCFGGIAA RYTLDIPGAL KNFREAYELG ATAGPHSYAA
     RLASALLGEL LCQTGDLAEA TRLVDEGYQL ESEGAGVDIM IARYVTGARV KAKQGDRDAA
     IDRLTDGMAA AERLRLPRLA AAVNNERIRL GIAIPQEVAV RLRATRTIRR PPRCDGIATI
     IAELDEDSGI RLLSASDSAD DQEQACRRAA ELLAGIDGAQ RPWAALGAQL LLVETLRATG
     KIDEANSLAP AVVARCREHG LSGLLTDAGL G
//
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