PHLC_LISIV
ID PHLC_LISIV Reviewed; 335 AA.
AC Q9RLV9;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Sphingomyelinase C;
DE Short=SMase;
DE EC=3.1.4.12;
DE AltName: Full=Sphingomyelin phosphodiesterase;
DE Flags: Precursor;
GN Name=smcL;
OS Listeria ivanovii.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=1638;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 19119 / DSM 20750 / BCRC 14844 / JCM 7681 / KCTC 3444 / NCTC
RC 11846 / NRRL B-33017 / SLCC 2379 / WDCM 00018;
RX PubMed=10417642; DOI=10.1046/j.1365-2958.1999.01486.x;
RA Gonzalez-Zorn B., Dominguez-Bernal G., Suarez M., Ripio M.-T., Vega Y.,
RA Novella S., Vazquez-Boland J.-A.;
RT "The smcL gene of Listeria ivanovii encodes a sphingomyelinase C that
RT mediates bacterial escape from the phagocytic vacuole.";
RL Mol. Microbiol. 33:510-523(1999).
CC -!- FUNCTION: Virulence factor that promotes intracellular proliferation by
CC mediating the disruption of the phagocytic vacuole and the release of
CC bacteria into the host cell cytosol. May act in concert with the
CC phospholipases PlcA and PlcB and the hemolysin hly to mediate efficient
CC escape from the vacuole. {ECO:0000269|PubMed:10417642}.
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; EC=3.1.4.12;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DISRUPTION PHENOTYPE: A knockout mutant was shown to be weakly
CC hemolytic on sheep blood agar, does not produce the external halo of
CC incomplete hemolysis characteristic of L.ivanovii and does not give the
CC typical shovel-shaped cooperative hemolytic 'CAMP-like' reaction that
CC happens with Rhodococcus equi. Is also much less virulent for mice
CC infected intravenously. {ECO:0000269|PubMed:10417642}.
CC -!- MISCELLANEOUS: Complementation with SmcL of a mutant lacking the
CC membrane-damaging determinants hly, PlcA and PlcB (thus unable to grow
CC intracellularly) was sufficient to promote bacterial intracellular
CC proliferation.
CC -!- SIMILARITY: Belongs to the neutral sphingomyelinase family.
CC {ECO:0000305}.
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DR EMBL; Y09477; CAA70683.2; -; Genomic_DNA.
DR PDB; 1ZWX; X-ray; 1.90 A; A=36-335.
DR PDBsum; 1ZWX; -.
DR AlphaFoldDB; Q9RLV9; -.
DR SMR; Q9RLV9; -.
DR EvolutionaryTrace; Q9RLV9; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004767; F:sphingomyelin phosphodiesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR CDD; cd09078; nSMase; 1.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR017766; Sphingomyelinase/PLipase_C.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
DR TIGRFAMs; TIGR03395; sphingomy; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytolysis; Hemolysis; Hydrolase; Secreted; Signal; Virulence.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..335
FT /note="Sphingomyelinase C"
FT /id="PRO_0000046031"
FT STRAND 46..54
FT /evidence="ECO:0007829|PDB:1ZWX"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:1ZWX"
FT HELIX 65..73
FT /evidence="ECO:0007829|PDB:1ZWX"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:1ZWX"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:1ZWX"
FT HELIX 92..101
FT /evidence="ECO:0007829|PDB:1ZWX"
FT TURN 102..105
FT /evidence="ECO:0007829|PDB:1ZWX"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:1ZWX"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:1ZWX"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:1ZWX"
FT HELIX 158..162
FT /evidence="ECO:0007829|PDB:1ZWX"
FT STRAND 166..174
FT /evidence="ECO:0007829|PDB:1ZWX"
FT STRAND 177..185
FT /evidence="ECO:0007829|PDB:1ZWX"
FT HELIX 195..216
FT /evidence="ECO:0007829|PDB:1ZWX"
FT STRAND 222..229
FT /evidence="ECO:0007829|PDB:1ZWX"
FT HELIX 237..246
FT /evidence="ECO:0007829|PDB:1ZWX"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:1ZWX"
FT HELIX 267..272
FT /evidence="ECO:0007829|PDB:1ZWX"
FT STRAND 282..287
FT /evidence="ECO:0007829|PDB:1ZWX"
FT STRAND 296..300
FT /evidence="ECO:0007829|PDB:1ZWX"
FT STRAND 308..312
FT /evidence="ECO:0007829|PDB:1ZWX"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:1ZWX"
FT STRAND 322..325
FT /evidence="ECO:0007829|PDB:1ZWX"
FT STRAND 328..332
FT /evidence="ECO:0007829|PDB:1ZWX"
SQ SEQUENCE 335 AA; 38455 MW; 46F398E58A8434D7 CRC64;
MEKFKIIKTI PKICGAFIFL LFFTFLFGHY GELKTQASDE YPGNFKITSH NVYLFSRNIY
PNWGQMHRAD LIAQADYMKN NDVVILNEAF DTSASHRLLN NLREMYPHQT PVIGRSKHGW
DKTEGNYSNF ALEDGGVAVV SQWPIVEKSQ HIFQRGGGAD RLSNKGFAYV KIMKNGKPYH
IIGTHTPADD SLISKDTSRA IRAEQMQEIQ TFIAKKNIPK DEIIFIGGDL NVNYGTDEYH
DMFKLLNVSS PANFNGQMAT WDPTTNSMLK ESYPKAAPEY LDYIFVENGH ARPHSWHNKV
LHTKSPQWSV KSWFKTYTYQ DFSDHYPVVG FTDNN
