PHLB_MYCTU
ID PHLB_MYCTU Reviewed; 521 AA.
AC P9WIB3; L0TAY7; P95246; Q50561;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 44.
DE RecName: Full=Phospholipase C B {ECO:0000305};
DE Short=PLC-B {ECO:0000303|PubMed:20736081};
DE EC=3.1.4.3 {ECO:0000269|PubMed:20736081, ECO:0000269|PubMed:8757862};
DE AltName: Full=Mycobacterial phospholipase C B {ECO:0000303|PubMed:8757862};
DE Flags: Precursor;
GN Name=plcB {ECO:0000303|PubMed:12100560};
GN Synonyms=mpcB {ECO:0000303|PubMed:8757862}; OrderedLocusNames=Rv2350c;
GN ORFNames=MTCY98.19c;
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 [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=8757862; DOI=10.1128/iai.64.8.3259-3266.1996;
RA Johansen K.A., Gill R.E., Vasil M.L.;
RT "Biochemical and molecular analysis of phospholipase C and phospholipase D
RT activity in mycobacteria.";
RL Infect. Immun. 64:3259-3266(1996).
RN [2]
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 [3]
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 [4]
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 [5]
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 and sphingomyelin (PubMed:8757862,
CC PubMed:20736081). Does not have hemolytic activity (PubMed:20736081).
CC {ECO:0000269|PubMed:20736081, ECO:0000269|PubMed:8757862}.
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, ECO:0000269|PubMed:8757862};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10605;
CC Evidence={ECO:0000269|PubMed:20736081, ECO:0000269|PubMed:8757862};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a sphingomyelin + H2O = an N-acylsphing-4-enine + H(+) +
CC phosphocholine; Xref=Rhea:RHEA:19253, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17636, ChEBI:CHEBI:52639,
CC ChEBI:CHEBI:295975; Evidence={ECO:0000269|PubMed:8757862};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19254;
CC Evidence={ECO:0000269|PubMed:8757862};
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 8. {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, ECO:0000269|PubMed:8757862}.
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=CCP45138.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U49511; AAC18944.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP45138.1; ALT_INIT; Genomic_DNA.
DR PIR; G70662; G70662.
DR RefSeq; NP_216866.1; NC_000962.3.
DR AlphaFoldDB; P9WIB3; -.
DR SMR; P9WIB3; -.
DR STRING; 83332.Rv2350c; -.
DR SwissLipids; SLP:000001396; -.
DR PaxDb; P9WIB3; -.
DR DNASU; 885999; -.
DR GeneID; 885999; -.
DR KEGG; mtu:Rv2350c; -.
DR TubercuList; Rv2350c; -.
DR eggNOG; COG3511; Bacteria.
DR OMA; LPWYLGY; -.
DR PHI-base; PHI:5289; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; IDA:MTBBASE.
DR GO; GO:0034480; F:phosphatidylcholine phospholipase C activity; IMP:MTBBASE.
DR GO; GO:0004629; F:phospholipase C activity; IDA:MTBBASE.
DR GO; GO:0004767; F:sphingomyelin phosphodiesterase activity; IEA:RHEA.
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..521
FT /note="Phospholipase C B"
FT /id="PRO_0000023943"
FT REGION 501..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 303
FT /note="P -> T (in Ref. 1; AAC18944)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="P -> A (in Ref. 1; AAC18944)"
FT /evidence="ECO:0000305"
FT CONFLICT 398
FT /note="F -> P (in Ref. 1; AAC18944)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="V -> F (in Ref. 1; AAC18944)"
FT /evidence="ECO:0000305"
FT CONFLICT 409..410
FT /note="SR -> T (in Ref. 1; AAC18944)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="M -> I (in Ref. 1; AAC18944)"
FT /evidence="ECO:0000305"
FT CONFLICT 472..473
FT /note="LN -> AQC (in Ref. 1; AAC18944)"
FT /evidence="ECO:0000305"
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
