PHLC_MYCTU
ID PHLC_MYCTU Reviewed; 517 AA.
AC P9WIB1; L0TC24; P95245;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 47.
DE RecName: Full=Phospholipase C C {ECO:0000305};
DE Short=PLC-C {ECO:0000303|PubMed:20736081};
DE EC=3.1.4.3 {ECO:0000269|PubMed:20736081};
DE Flags: Precursor;
GN Name=plcC {ECO:0000303|PubMed:12100560}; OrderedLocusNames=Rv2349c;
GN ORFNames=MTCY98.18c;
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 INDUCTION.
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, AND
RP SUBCELLULAR LOCATION.
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).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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. {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 -!- INDUCTION: Expression is induced in vitro in the presence of
CC phosphatidylcholine. Also induced upon infection of THP-1 macrophages.
CC {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 -!- MISCELLANEOUS: Polymorphism was discovered in the phospholipase
CC plcA/B/C region. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the bacterial phospholipase C family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCP45137.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL123456; CCP45137.1; ALT_INIT; Genomic_DNA.
DR PIR; F70662; F70662.
DR RefSeq; NP_216865.1; NC_000962.3.
DR AlphaFoldDB; P9WIB1; -.
DR SMR; P9WIB1; -.
DR STRING; 83332.Rv2349c; -.
DR SwissLipids; SLP:000001397; -.
DR PaxDb; P9WIB1; -.
DR DNASU; 886000; -.
DR GeneID; 886000; -.
DR KEGG; mtu:Rv2349c; -.
DR TubercuList; Rv2349c; -.
DR eggNOG; COG3511; Bacteria.
DR OMA; GYYCSLH; -.
DR PHI-base; PHI:5290; -.
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 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; Reference proteome; 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_0000023944"
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
