ID   PHLB_MYCTO              Reviewed;         521 AA.
AC   P9WIB2; L0TAY7; P95246; Q50561;
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 B {ECO:0000305};
DE            Short=PLC-B {ECO:0000305};
DE            EC=3.1.4.3 {ECO:0000269|PubMed:12100560};
DE   Flags: Precursor;
GN   Name=plcB {ECO:0000303|PubMed:12100560}; Synonyms=mpcB;
GN   OrderedLocusNames=MT2415;
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:P9WIB3, 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=AAK46708.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK46708.1; ALT_INIT; Genomic_DNA.
DR   PIR; G70662; G70662.
DR   AlphaFoldDB; P9WIB2; -.
DR   SMR; P9WIB2; -.
DR   EnsemblBacteria; AAK46708; AAK46708; MT2415.
DR   KEGG; mtc:MT2415; -.
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..521
FT                   /note="Phospholipase C B"
FT                   /id="PRO_0000428037"
FT   REGION          501..521
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   521 AA;  56533 MW;  C45A3EA0D1968870 CRC64;
     MGSEHPVDGM TRRQFFAKAA AATTAGAFMS LAGPIIEKAY GAGPCPGHLT DIEHIVLLMQ
     ENRSFDHYFG TLSDTRGFDD TTPPVVFAQS GWNPMTQAVD PAGVTLPYRF DTTRGPLVAG
     ECVNDPDHSW IGMHNSWNGG ANDNWLPAQV PFSPLQGNVP VTMGFYTRRD LPIHYLLADT
     FTVCDGYFCS LLGGTTPNRL YWMSAWIDPD GTDGGPVLIE PNIQPLQHYS WRIMPENLED
     AGVSWKVYQN KLLGALNNTV VGYNGLVNDF KQAADPRSNL ARFGISPTYP LDFAADVRNN
     RLPKVSWVLP GFLLSEHPAF PVNVGAVAIV DALRILLSNP AVWEKTALIV NYDENGGFFD
     HVVPPTPPPG TPGEFVTVPD IDSVPGSGGI RGPIGLGFRV PCLVISPYSR GPLMVHDTFD
     HTSTLKLIRA RFGVPVPNLT AWRDATVGDM TSTFNFAAPP NPSKPNLDHP RLNALPKLPQ
     CVPNAVLGTV TKTAIPYRVP FPQSMPTQET APTRGIPSGL C