ID   PHLA_MYCTO              Reviewed;         520 AA.
AC   P9WIB4; L0T9D3; O08223; Q04001; Q50560; Q50771; Q50772; Q53408;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Phospholipase C A {ECO:0000305};
DE            Short=PLC-A {ECO:0000305};
DE            EC=3.1.4.3 {ECO:0000269|PubMed:12100560};
DE   AltName: Full=MTP40 antigen;
DE   Flags: Precursor;
GN   Name=plcA {ECO:0000303|PubMed:12100560}; Synonyms=mpcA, mtp40;
GN   OrderedLocusNames=MT2416;
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).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INDUCTION, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=Mt103;
RX   PubMed=12100560; DOI=10.1046/j.1365-2958.2002.03009.x;
RA   Raynaud C., Guilhot C., Rauzier J., Bordat Y., Pelicic V., Manganelli R.,
RA   Smith I., Gicquel B., Jackson M.;
RT   "Phospholipases C are involved in the virulence of Mycobacterium
RT   tuberculosis.";
RL   Mol. Microbiol. 45:203-217(2002).
CC   -!- FUNCTION: Involved in virulence (PubMed:12100560). Induces cytotoxic
CC       effects on mouse macrophage cell lines, via direct or indirect
CC       enzymatic hydrolysis of cell membrane phospholipids (By similarity).
CC       Hydrolyzes phosphatidylcholine (PubMed:12100560).
CC       {ECO:0000250|UniProtKB:P9WIB5, ECO:0000269|PubMed:12100560}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-
CC         sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:10604,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:295975; EC=3.1.4.3;
CC         Evidence={ECO:0000269|PubMed:12100560};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10605;
CC         Evidence={ECO:0000269|PubMed:12100560};
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC       {ECO:0000269|PubMed:12100560}. Note=Remains associated with the cell.
CC       {ECO:0000269|PubMed:12100560}.
CC   -!- INDUCTION: Expression is induced in vitro in the presence of
CC       phosphatidylcholine. {ECO:0000269|PubMed:12100560}.
CC   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has not been experimentally proven.
CC       {ECO:0000255|PROSITE-ProRule:PRU00648}.
CC   -!- DISRUPTION PHENOTYPE: Disruption of the gene in the clinical strain
CC       Mt103 leads to a reduction of the phospholipase C activity of the
CC       mutant. The plcABCD mutant exhibits a dramatic decrease in
CC       phospholipase C activity. The quadruple mutant is attenuated in the
CC       mouse model of infection, but not in infected THP-1 cells.
CC       {ECO:0000269|PubMed:12100560}.
CC   -!- SIMILARITY: Belongs to the bacterial phospholipase C family.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK46709.1; -; Genomic_DNA.
DR   PIR; H70662; H70662.
DR   AlphaFoldDB; P9WIB4; -.
DR   SMR; P9WIB4; -.
DR   EnsemblBacteria; AAK46709; AAK46709; MT2416.
DR   KEGG; mtc:MT2416; -.
DR   HOGENOM; CLU_008770_2_2_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0034480; F:phosphatidylcholine phospholipase C activity; IEA:UniProtKB-EC.
DR   GO; GO:0044003; P:modulation by symbiont of host process; IEA:UniProt.
DR   Gene3D; 3.40.720.10; -; 2.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR007312; Phosphoesterase.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR31956; PTHR31956; 1.
DR   Pfam; PF04185; Phosphoesterase; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   1: Evidence at protein level;
KW   Cell wall; Hydrolase; Secreted; Signal; Virulence.
FT   SIGNAL          1..38
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT   CHAIN           39..520
FT                   /note="Phospholipase C A"
FT                   /id="PRO_0000428036"
SQ   SEQUENCE   520 AA;  56138 MW;  5844EF0C064288A7 CRC64;
     MSASPLLGMS RREFLTKLTG AGAAAFLMDW AAPVIEKAYG AGPCPGHLTD IEHIVLLMQE
     NRSFDHYFGT LSSTNGFNAA SPAFQQMGWN PMTQALDPAG VTIPFRLDTT RGPFLDGECV
     NDPEHQWVGM HLAWNGGAND NWLPAQATTR AGPYVPLTMG YYTRQDIPIH YLLADTFTIC
     DGYHCSLLTG TLPNRLYWLS ANIDPAGTDG GPQLVEPGFL PLQQFSWRIM PENLEDAGVS
     WKVYQNKGLG RFINTPISNN GLVQAFRQAA DPRSNLARYG IAPTYPGDFA ADVRANRLPK
     VSWLVPNILQ SEHPALPVAL GAVSMVTALR ILLSNPAVWE KTALIVSYDE NGGFFDHVTP
     PTAPPGTPGE FVTVPNIDAV PGSGGIRGPL GLGFRVPCIV ISPYSRGPLM VSDTFDHTSQ
     LKLIRARFGV PVPNMTAWRD GVVGDMTSAF NFATPPNSTR PNLSHPLLGA LPKLPQCIPN
     VVLGTTDGAL PSIPYRVPYP QVMPTQETTP VRGTPSGLCS