PHLD_MYCTU
ID PHLD_MYCTU Reviewed; 280 AA.
AC P9WIA9; L0T7L1; O06792; P0A5R8; Q9XB13;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 07-OCT-2020, sequence version 2.
DT 25-MAY-2022, entry version 33.
DE RecName: Full=Phospholipase C D {ECO:0000305};
DE Short=PLC-D {ECO:0000303|PubMed:20736081};
DE EC=3.1.4.3 {ECO:0000269|PubMed:20736081};
DE Flags: Fragment;
GN Name=plcD {ECO:0000303|PubMed:12100560}; OrderedLocusNames=Rv1755c;
GN ORFNames=MTCY28.21c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP GENE FAMILY.
RC STRAIN=H37Rv;
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).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND EXPRESSION IN M.SMEGMATIS.
RC STRAIN=H37Rv;
RX PubMed=20736081; DOI=10.1016/j.bbalip.2010.08.007;
RA Bakala N'goma J.C., Schue M., Carriere F., Geerlof A., Canaan S.;
RT "Evidence for the cytotoxic effects of Mycobacterium tuberculosis
RT phospholipase C towards macrophages.";
RL Biochim. Biophys. Acta 1801:1305-1313(2010).
CC -!- FUNCTION: Involved in virulence (PubMed:20736081). Induces cytotoxic
CC effects on mouse macrophage cell lines, via direct or indirect
CC enzymatic hydrolysis of cell membrane phospholipids (PubMed:20736081).
CC Hydrolyzes phosphatidylcholine (PubMed:20736081). Does not have
CC hemolytic activity (PubMed:20736081). {ECO:0000269|PubMed:20736081}.
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:20736081};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10605;
CC Evidence={ECO:0000269|PubMed:20736081};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1,2-
CC dihexadecanoyl-sn-glycerol + H(+) + phosphocholine;
CC Xref=Rhea:RHEA:45304, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:72999, ChEBI:CHEBI:82929, ChEBI:CHEBI:295975;
CC Evidence={ECO:0000269|PubMed:20736081};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45305;
CC Evidence={ECO:0000269|PubMed:20736081};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:20736081};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:20736081};
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:20736081}. Note=Remains associated with the cell.
CC {ECO:0000269|PubMed:20736081}.
CC -!- MISCELLANEOUS: Polymorphism was discovered in the phospholipase plcD
CC region.
CC -!- SIMILARITY: Belongs to the bacterial phospholipase C family.
CC {ECO:0000305}.
CC -!- CAUTION: In strain H37Rv, PLC-D lacks the N-terminal domain. The gene
CC is truncated and interrupted by the insertion of an IS6110 element.
CC However, when expressed in M.smegmatis, recombinant PLC-D is detected
CC in the cell wall fraction and shows phospholipase activity
CC (PubMed:20736081). {ECO:0000269|PubMed:20736081,
CC ECO:0000305|PubMed:12100560, ECO:0000305|PubMed:20736081}.
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DR EMBL; AL123456; CCP44521.1; -; Genomic_DNA.
DR PIR; D70987; D70987.
DR AlphaFoldDB; P9WIA9; -.
DR STRING; 83332.Rv1755c; -.
DR SwissLipids; SLP:000001398; -.
DR PaxDb; P9WIA9; -.
DR TubercuList; Rv1755c; -.
DR eggNOG; COG3511; Bacteria.
DR OMA; MDAGVSW; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0034480; F:phosphatidylcholine phospholipase C activity; IMP:MTBBASE.
DR GO; GO:0052008; P:disruption by symbiont of host cellular component; IDA:MTBBASE.
DR GO; GO:0016042; P:lipid catabolic process; IMP:MTBBASE.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR007312; Phosphoesterase.
DR PANTHER; PTHR31956; PTHR31956; 1.
DR Pfam; PF04185; Phosphoesterase; 1.
PE 1: Evidence at protein level;
KW Cell wall; Hydrolase; Reference proteome; Secreted; Virulence.
FT CHAIN 1..280
FT /note="Phospholipase C D"
FT /id="PRO_0000023945"
FT REGION 258..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000305"
SQ SEQUENCE 280 AA; 29970 MW; 7E8836AF5C00F7F0 CRC64;
DAGVSWKVYR NKTLGPISSV LTYGSLVTSF KQSADPRSDL VRFGVAPSYP ASFAADVLAN
RLPRVSWVIP NVLESEHPAV PAAAGAFAIV NILRILLANP AVWEKTALIV SYDENGGFFD
HVVPATAPAG TPGEYVTVPD IDQVPGSGGI RGPIGLGFRV PCFVISPYSR GPQMVHDTFD
HTSQLRLLET RFGVPVPNLT AWRRSVTGDM TSTFNFAVPP NSSWPNLDYP GLHALSTVPQ
CVPNAALGTI NRGIPYRVPD PQIMPTQETT PTRGIPSGPC
