ID   PHLC_MYCTO              Reviewed;         517 AA.
AC   P9WIB0; L0TC24; P95245;
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 C {ECO:0000305};
DE            Short=PLC-C {ECO:0000305};
DE            EC=3.1.4.3 {ECO:0000269|PubMed:12100560};
DE   Flags: Precursor;
GN   Name=plcC {ECO:0000303|PubMed:12100560}; OrderedLocusNames=MT2414;
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:P9WIB1, 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK46707.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK46707.1; ALT_INIT; Genomic_DNA.
DR   PIR; F70662; F70662.
DR   AlphaFoldDB; P9WIB0; -.
DR   SMR; P9WIB0; -.
DR   EnsemblBacteria; AAK46707; AAK46707; MT2414.
DR   KEGG; mtc:MT2414; -.
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..39
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT   CHAIN           40..517
FT                   /note="Phospholipase C C"
FT                   /id="PRO_0000428038"
SQ   SEQUENCE   517 AA;  55896 MW;  5B9D4241E09755AE CRC64;
     MVSQGAFAGM SRRAFLAKAA GAGAAAVLTD WAAPVIEKAY GAGPCSGHLT DIEHIVLCLQ
     ENRSFDHYFG TLSAVDGFDT PTPLFQQKGW NPETQALDPT GITLPYRINT TGGPNGVGEC
     VNDPDHQWIA AHLSWNGGAN DGWLPAQART RSVANTPVVM GYYARPDIPI HYLLADTFTI
     CDQYFSSLLG GTMPNRLYWI SATVNPDGDQ GGPQIVEPAI QPKLTFTWRI MPQNLSDAGI
     SWKVYNSKLL GGLNDTSLSR NGYVGSFKQA ADPRSDLARY GIAPAYPWDF IRDVINNTLP
     QVSWVVPLTV ESEHPSFPVA VGAVTIVNLI RVLLRNPAVW EKTALIIAYD EHGGFFDHVT
     PLTAPEGTPG EWIPNSVDID KVDGSGGIRG PIGLGFRVPC FVISPYSRGG LMVHDRFDHT
     SQLQLIGKRF GVPVPNLTPW RASVTGDMTS AFNFAAPPDP SPPNLDHPVR QLPKVAKCVP
     NVVLGFLNEG LPYRVPYPQT TPVQESGPAR PIPSGIC