ID   O69568_MYCLR            Unreviewed;       400 AA.
AC   O69568;
DT   01-AUG-1998, integrated into UniProtKB/TrEMBL.
DT   01-AUG-1998, sequence version 1.
DT   27-MAR-2024, entry version 135.
DE   SubName: Full=Putative serine/threonine protein kinase {ECO:0000313|EMBL:CAA18685.1};
GN   Name=MLCB268.19 {ECO:0000313|EMBL:CAA18685.1};
OS   Mycobacterium leprae.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1769 {ECO:0000313|EMBL:CAA18685.1};
RN   [1] {ECO:0000313|EMBL:CAA18685.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=8446027; DOI=10.1111/j.1365-2958.1993.tb01111.x;
RA   Eiglmeier K., Honore N., Woods S.A., Caudron B., Cole S.T.;
RT   "Use of an ordered cosmid library to deduce the genomic organization of
RT   Mycobacterium leprae.";
RL   Mol. Microbiol. 7:197-206(1993).
RN   [2] {ECO:0000313|EMBL:CAA18685.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Parkhill J., Barrell B.G., Rajandream M.A.;
RL   Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:CAA18685.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Brown D., Churcher C.M.;
RL   Submitted (APR-1998) 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}.
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DR   EMBL; AL022602; CAA18685.1; -; Genomic_DNA.
DR   PIR; C87021; C87021.
DR   AlphaFoldDB; O69568; -.
DR   Leproma; ML0897; -.
DR   OMA; EFVWARQ; -.
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-KW.
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; PTHR45832:SF24; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR45832; SERINE/THREONINE-PROTEIN KINASE SAMKA-RELATED-RELATED; 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:CAA18685.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:CAA18685.1};
KW   Transferase {ECO:0000313|EMBL:CAA18685.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        371..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          6..275
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         35
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   400 AA;  43593 MW;  16389D0516EFFD21 CRC64;
     MLDGRYLLKA KIGNGGTATV YRGVDIRLDR PVAVKVMDSR YTGDEQLLTR FQLEARSVAR
     LKDPGLVAVY DQGIDARHPF LVMELIEGGT LRELLAERGP MPPHAVVAVL RPVLGGLAAA
     HRAGLVHRDV KPENILISDD GDVKIADFGL VRAVAAAGIT STSVILGTVA YLSPEQVRDG
     DASPRSDVYS AGIMTYELLT GHTPFTGDSA LSIAYQRLEI DVPRASTVIT GVPQQFDELV
     ARATVRDPSG RYADAIEMAA QVDSIAEELA LPPFRVPAPR NTAQYRSAAL HRGHMVERPV
     EQQVQPVVNA PMPHSTRQFT RRLRDCSAPR RPARPDIDSP EEYEYEPVPD RFAGIAISEF
     IWARQHARRM VLIWVGVVVA IAGLVATVAW TIGSHLSGLL
//