ID   PHLD_MYCTO              Reviewed;         514 AA.
AC   P9WIA8; L0T7L1; O06792; P0A5R8; Q9XB13;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=Phospholipase C D {ECO:0000305};
DE            Short=PLC-D {ECO:0000305};
DE            EC=3.1.4.3 {ECO:0000269|PubMed:12100560};
DE   Flags: Precursor;
GN   Name=plcD {ECO:0000303|PubMed:12100560}; OrderedLocusNames=MT1799;
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, INDUCTION, AND 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 (By similarity). 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:P9WIA9, 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:0000250|UniProtKB:P9WIA9}. Note=Remains associated with the cell.
CC       {ECO:0000250|UniProtKB:P9WIA9}.
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; AAK46072.1; -; Genomic_DNA.
DR   PIR; D70987; D70987.
DR   RefSeq; WP_003900400.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WIA8; -.
DR   SMR; P9WIA8; -.
DR   EnsemblBacteria; AAK46072; AAK46072; MT1799.
DR   KEGG; mtc:MT1799; -.
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..37
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT   CHAIN           38..514
FT                   /note="Phospholipase C D"
FT                   /id="PRO_0000428039"
FT   REGION          492..514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        497..514
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   514 AA;  55770 MW;  9D99A466D312BA30 CRC64;
     MSQSHIGGVS RREFLAKVAA GGAGALMSFA GPVIEKAYGA GPCSGHLTDI EHFVFFMQEN
     RSFDHYFGTL SGTDGFNTVS PLFQQKGWNP MTQALDATGV TMPYRFDTTR GPFLDGACVN
     DPDHSWVAMH ESWNGGVNDN WLPAQAKTRS AAHTPTVMGY YTRQDIPIHY LLADAFTVCD
     RYFCSVLGPT LPNRLYWLSA TIDPDGQNGG PELQSPTFQP VRRFGWRIMP QNLSDAGVSW
     KVYRNKTLGP ISSVLTYGSL VTSFKQSADP RSDLVRFGVA PSYPASFAAD VLANRLPRVS
     WVIPNVLESE HPAVPAAAGA FAIVNILRIL LANPAVWEKT ALIVSYDENG GFFDHVVPAT
     APAGTPGEYV TVPDIDQVPG SGGIRGPIGL GFRVPCFVIS PYSRGPQMVH DTFDHTSQLR
     LLETRFGVPV PNLTAWRRSV TGDMTSTFNF AVPPNSSWPN LDYPGLHALS TVPQCVPNAA
     LGTINRGIPY RVPDPQIMPT QETTPTRGIP SGPC