ID   PHLD_MYCBO              Reviewed;         514 AA.
AC   P0A5R9; A0A1R3XZ86; O06792; Q9XB13; X2BID1;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Phospholipase C D {ECO:0000305};
DE            Short=PLC-D {ECO:0000305};
DE            EC=3.1.4.3 {ECO:0000250|UniProtKB:P9WIA8};
DE   Flags: Precursor;
GN   Name=plcD; OrderedLocusNames=BQ2027_MB1784C;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BCG / Pasteur;
RX   PubMed=10320585; DOI=10.1046/j.1365-2958.1999.01383.x;
RA   Gordon S.V., Brosch R., Billault A., Garnier T., Eiglmeier K., Cole S.T.;
RT   "Identification of variable regions in the genomes of tubercle bacilli
RT   using bacterial artificial chromosome arrays.";
RL   Mol. Microbiol. 32:643-655(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
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 (By similarity).
CC       {ECO:0000250|UniProtKB:P9WIA8, ECO:0000250|UniProtKB:P9WIA9}.
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:0000250|UniProtKB:P9WIA8};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10605;
CC         Evidence={ECO:0000250|UniProtKB:P9WIA8};
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC       {ECO:0000250|UniProtKB:P9WIA9}. Note=Remains associated with the cell.
CC       {ECO:0000250|UniProtKB:P9WIA9}.
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   -!- MISCELLANEOUS: Polymorphism was discovered in the phospholipase plcD
CC       region.
CC   -!- SIMILARITY: Belongs to the bacterial phospholipase C family.
CC       {ECO:0000305}.
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DR   EMBL; Y18606; CAB44656.1; -; Genomic_DNA.
DR   EMBL; LT708304; SIU00387.1; -; Genomic_DNA.
DR   RefSeq; NP_855436.1; NC_002945.3.
DR   RefSeq; WP_003900400.1; NC_002945.4.
DR   AlphaFoldDB; P0A5R9; -.
DR   SMR; P0A5R9; -.
DR   EnsemblBacteria; SIU00387; SIU00387; BQ2027_MB1784C.
DR   PATRIC; fig|233413.5.peg.1951; -.
DR   OMA; AYNVVPF; -.
DR   Proteomes; UP000001419; 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   3: Inferred from homology;
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_0000023946"
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