ID   A1UQJ4_MYCSK            Unreviewed;       576 AA.
AC   A1UQJ4;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 93.
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_5928 {ECO:0000313|EMBL:ABL95102.1};
OS   Mycobacterium sp. (strain KMS).
OG   Plasmid pMKMS02 {ECO:0000313|EMBL:ABL95102.1}.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=189918 {ECO:0000313|EMBL:ABL95102.1};
RN   [1] {ECO:0000313|EMBL:ABL95102.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMS {ECO:0000313|EMBL:ABL95102.1};
RC   PLASMID=pMKMS02 {ECO:0000313|EMBL:ABL95102.1};
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 plasmid pMKMS02 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};
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; CP000520; ABL95102.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1UQJ4; -.
DR   KEGG; mkm:Mkms_5928; -.
DR   HOGENOM; CLU_000288_63_44_11; -.
DR   OrthoDB; 5622056at2; -.
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:SF32; SERINE_THREONINE-PROTEIN KINASE PKAB; 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:ABL95102.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Plasmid {ECO:0000313|EMBL:ABL95102.1};
KW   Transferase {ECO:0000313|EMBL:ABL95102.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        395..416
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          17..282
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          285..380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..326
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        338..365
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   576 AA;  60881 MW;  C38AD9A21D750046 CRC64;
     MWCAGTVLSV GSVVAGYRIE RVLGAGGMGT VYLAKNPTLP RRDALKVLST ELSRDRAFRE
     RFVREADIAS LLDHPGIVSI YGRGETDDGH LWIALQYVEG TDAEAALQSG AMTPLRAVHI
     VTEVAKALDY AHHRNVVHHD VKPANLLLSD EIGDGERVFL TDFGVARPMD DTDRSMDGAF
     TATLAYSAPE VITGEQVDGR SDIYSLGCTL FRLLTGRQPF SQADGVVGTI RAHLAMPQPR
     VSEHVSWATP ELDQVIARAL AKDPAHRFGS AREFAAAAAD AVRQAAPPED AAAPYRVGAA
     PDTPGPRRTA PTPQASPPPA TLKPLPPAPQ QFGDADFRSA VKARRTPVKP PRADKAKREA
     PSTAARREPD FGGAAAPAPV VPRPAQRREV PKHVVWLWAV AIVLMVLAGV LITMVVRRET
     AEPPAPPAAS PSPTVDAAAQ TELERLLPAG YPSGRCEEVA AVPAGARAVL SCGANVDAGG
     PASATYTLVE DAGALQSALD EVISGATTVV CPGNILSPGP WRRNADPTAP AGTLFCGVEG
     GEAVIAWTTD ADLLLNVVRA DRPAMEGLYR WWSGHS
//