ID   PTKA_MYCTO              Reviewed;         291 AA.
AC   P9WPI8; L0TBP3; P68911; Q10515; Q10516;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=Tyrosine-protein kinase PtkA {ECO:0000250|UniProtKB:P9WPI9};
DE            EC=2.7.10.- {ECO:0000250|UniProtKB:P9WPI9};
DE   AltName: Full=Protein tyrosine kinase A {ECO:0000250|UniProtKB:P9WPI9};
GN   Name=ptkA {ECO:0000250|UniProtKB:P9WPI9}; OrderedLocusNames=MT2292;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Required for growth within macrophages. Catalyzes the
CC       phosphorylation of PtpA on the tyrosine residues at positions 128 and
CC       129, thereby increasing PtpA phosphatase activity and promoting
CC       pathogenicity. {ECO:0000250|UniProtKB:P9WPI9}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000250|UniProtKB:P9WPI9};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10597;
CC         Evidence={ECO:0000250|UniProtKB:P9WPI9};
CC   -!- SUBUNIT: Interacts with PtpA. {ECO:0000250|UniProtKB:P9WPI9}.
CC   -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:P9WPI9}.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC       CbbY/CbbZ/Gph/YieH family. {ECO:0000305}.
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; AE000516; AAK46576.1; -; Genomic_DNA.
DR   PIR; D70777; D70777.
DR   RefSeq; WP_003411507.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WPI8; -.
DR   SMR; P9WPI8; -.
DR   EnsemblBacteria; AAK46576; AAK46576; MT2292.
DR   KEGG; mtc:MT2292; -.
DR   PATRIC; fig|83331.31.peg.2469; -.
DR   HOGENOM; CLU_045011_19_4_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.150.240; -; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR041492; HAD_2.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR023198; PGP-like_dom2.
DR   Pfam; PF13419; HAD_2; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein; Transferase;
KW   Tyrosine-protein kinase; Virulence.
FT   CHAIN           1..291
FT                   /note="Tyrosine-protein kinase PtkA"
FT                   /id="PRO_0000426944"
FT   REGION          1..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         262
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P9WPI9"
SQ   SEQUENCE   291 AA;  30694 MW;  750F090FB154E6E5 CRC64;
     MSSPRERRPA SQAPRLSRRP PAHQTSRSSP DTTAPTGSGL SNRFVNDNGI VTDTTASGTN
     CPPPPRAAAR RASSPGESPQ LVIFDLDGTL TDSARGIVSS FRHALNHIGA PVPEGDLATH
     IVGPPMHETL RAMGLGESAE EAIVAYRADY SARGWAMNSL FDGIGPLLAD LRTAGVRLAV
     ATSKAEPTAR RILRHFGIEQ HFEVIAGAST DGSRGSKVDV LAHALAQLRP LPERLVMVGD
     RSHDVDGAAA HGIDTVVVGW GYGRADFIDK TSTTVVTHAA TIDELREALG V