ID   A1UB17_MYCSK            Unreviewed;       623 AA.
AC   A1UB17;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 88.
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=Mkms_0809 {ECO:0000313|EMBL:ABL90025.1};
OS   Mycobacterium sp. (strain KMS).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=189918 {ECO:0000313|EMBL:ABL90025.1};
RN   [1] {ECO:0000313|EMBL:ABL90025.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMS {ECO:0000313|EMBL:ABL90025.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL   Submitted (DEC-2006) 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   -!- 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};
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DR   EMBL; CP000518; ABL90025.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1UB17; -.
DR   STRING; 189918.Mkms_0809; -.
DR   KEGG; mkm:Mkms_0809; -.
DR   HOGENOM; CLU_000288_63_44_11; -.
DR   OrthoDB; 9762169at2; -.
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:ABL90025.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000313|EMBL:ABL90025.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        323..343
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          12..277
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          464..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        466..490
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   623 AA;  66991 MW;  146AB8780570169B CRC64;
     MPLGDGTKIA GYTIRRMLGS GGMGEVYLAQ HPRLPREDAL KVLKSSISAD PDFVERFNRE
     ADLAAKLWHP HIVGIHDRGR YRGRLWISMD FVDGTDVGRL LQQKYPDGMP ADDALEIVEA
     VASALDYAHS RGLLHRDVKP ANILIADVEN DERRILLGDF GVARDLADDA GGGLTQTNMT
     VGTAAYAAPE QLMGLDVDGR TDQYSLAVTA FHMLTGAPPF QNSRPTVVVG QHLNTPPPLL
     ADTHPELAPL DAAMQRALAK NPDERFDTCT EFARALVTPE SPAPAANLDE AETMVRAVAP
     PPVAPPRAAP AAAPVGRRRT GGWLVAAAAV LVAVAAVLGY LVFAPGKQEP APEPFTLAGT
     LRLPDEVVTT GGLPGGYTCA GTKTFGDIGP NTPVTVEDEA GKLLAKGAIR GSASEREGCS
     LAFRVNEVPS GAKFYRVQVA DHPQVNYTEE EAKAGVEFAI AHAQPEPEPS PSPSTVTAAP
     PPPPPPRTVT VTPDADDSSL QQLRAYARND HAYVSRYLTD MWLPQLSAKR VGLEAEGVVW
     DNEQILEEHL AIRDEYPDAR LLWSGDWKTF DGRNFWITIV GLTSPDYTDV LAWCSDQGFD
     RDHCIAKIVS NSRGPSGTTK TNP
//