ID   A1TE68_MYCVP            Unreviewed;       574 AA.
AC   A1TE68;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 109.
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=Mvan_4693 {ECO:0000313|EMBL:ABM15468.1};
OS   Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS   KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=350058 {ECO:0000313|EMBL:ABM15468.1, ECO:0000313|Proteomes:UP000009159};
RN   [1] {ECO:0000313|EMBL:ABM15468.1, ECO:0000313|Proteomes:UP000009159}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC   PYR-1 {ECO:0000313|Proteomes:UP000009159};
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   Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Anderson I.J., Miller C., Richardson P.;
RT   "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004162};
CC       Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004167}.
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DR   EMBL; CP000511; ABM15468.1; -; Genomic_DNA.
DR   RefSeq; WP_011781843.1; NC_008726.1.
DR   AlphaFoldDB; A1TE68; -.
DR   STRING; 350058.Mvan_4693; -.
DR   KEGG; mva:Mvan_4693; -.
DR   eggNOG; COG0515; Bacteria.
DR   HOGENOM; CLU_000288_63_44_11; -.
DR   Proteomes; UP000009159; 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   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; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR43289; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 20-RELATED; 1.
DR   PANTHER; PTHR43289:SF37; SERINE_THREONINE-PROTEIN KINASE A; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 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:ABM15468.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009159};
KW   Transferase {ECO:0000313|EMBL:ABM15468.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        372..394
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          17..277
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          297..366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          397..436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        298..358
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        400..436
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   574 AA;  60557 MW;  24BEB8E8DAD1B63B CRC64;
     MTDPQRGSRV GSQVGPYRLR RLLGKGGMGE VYEAEDTVKD RVVALKLLPE AVSHDPVFRK
     RLQREAHAAG RLQEPHVVPI HDYGEVDGLL FVDMRLIDGT DLRKLLKEQG PMTPARATAI
     VAQVASALDA AHQNGIMHRD VKPENILINR DDFAYLVDFG IANAVTDEAL TELGTAVGTY
     AYMAPERFTN GEVTHRADVY ALTCVLHECL TGAQPFQGDS VSVVITAHLN DPAPRPSQSR
     PGIPAGLDDV ISRGMAKRPE DRYASAGEMA RAATAALTGA QQDQADSILQ RSQAATMMAP
     LPPPPPPPPP STPGGPLPYG GSPVPPPPPP PGQPTQASGF HTPPPPGGPP PGWPPQPPQS
     SGGGGGSKGP MIALLAGAAV IILVLAGLGI WLVVKPDSTS DPVASRTSTS AAPTTTSRGS
     TTRTRTSTST PPPTESYDQQ LMALLSGGHD SSNCEPVDPP APTILATVDC TQALTPGGPA
     FTRYSLFEDR GALDAAFEEA IRVNSELVQC PGSGVDSPTT WHYTETPDQV VGQIACGTYD
     GNPDLVWTKD DDLLLADAQG PNLEELHNWW LEFG
//