SMASE_MYCTO
ID SMASE_MYCTO Reviewed; 490 AA.
AC P9WKQ0; L0T574; P64743; Q10549;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 39.
DE RecName: Full=Sphingomyelinase {ECO:0000250|UniProtKB:P9WKQ1};
DE Short=SMase {ECO:0000250|UniProtKB:P9WKQ1};
DE EC=3.1.4.12 {ECO:0000250|UniProtKB:P9WKQ1};
DE Flags: Precursor;
GN Name=spmT {ECO:0000250|UniProtKB:P9WKQ1}; OrderedLocusNames=MT0911;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Catalyzes the cleavage of sphingomyelin, a major lipid in
CC eukaryotic cells, into ceramide and phosphocholine, which are then
CC utilized by M.tuberculosis as carbon, nitrogen and phosphorus sources,
CC respectively. Thus, enables M.tuberculosis to utilize sphingomyelin as
CC a source of several essential nutrients for intracellular growth during
CC infection. Furthermore, lyses erythrocytes and constitutes the main
CC hemolytic factor of M.tuberculosis. {ECO:0000250|UniProtKB:P9WKQ1}.
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 Evidence={ECO:0000250|UniProtKB:P9WKQ1};
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000250|UniProtKB:P9WKQ1}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P9WKQ1}.
CC -!- DOMAIN: Consists of a surface-exposed C-terminal sphingomyelinase
CC domain and a putative outer membrane-spanning N-terminal channel domain
CC able to mediate glucose and phosphocholine uptake across the outer
CC membrane. {ECO:0000250|UniProtKB:P9WKQ1}.
CC -!- SIMILARITY: Belongs to the SpmT family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK45157.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE000516; AAK45157.1; ALT_INIT; Genomic_DNA.
DR PIR; E70781; E70781.
DR RefSeq; WP_003901038.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WKQ0; -.
DR SMR; P9WKQ0; -.
DR EnsemblBacteria; AAK45157; AAK45157; MT0911.
DR GeneID; 45424852; -.
DR KEGG; mtc:MT0911; -.
DR PATRIC; fig|83331.31.peg.980; -.
DR HOGENOM; CLU_622305_0_0_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR GO; GO:0004767; F:sphingomyelin phosphodiesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
PE 3: Inferred from homology;
KW Cell outer membrane; Cytolysis; Hemolysis; Hydrolase; Ion transport;
KW Lipid degradation; Lipid metabolism; Membrane; Porin; Signal;
KW Transmembrane; Transmembrane beta strand; Transmembrane helix; Transport.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..490
FT /note="Sphingomyelinase"
FT /id="PRO_0000427615"
FT TOPO_DOM 32..136
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P9WKQ1"
FT TRANSMEM 137..145
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P9WKQ1"
FT TOPO_DOM 146..161
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P9WKQ1"
FT TRANSMEM 162..168
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P9WKQ1"
FT TOPO_DOM 169..171
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P9WKQ1"
FT TRANSMEM 172..182
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P9WKQ1"
FT TOPO_DOM 183..187
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P9WKQ1"
FT TRANSMEM 188..196
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P9WKQ1"
FT TOPO_DOM 197..204
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P9WKQ1"
FT TRANSMEM 205..213
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:P9WKQ1"
FT TOPO_DOM 214..490
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P9WKQ1"
FT REGION 30..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 490 AA; 52034 MW; 8A6DEA5E95A3D26E CRC64;
MDYAKRIGQV GALAVVLGVG AAVTTHAIGS AAPTDPSSSS TDSPVDACSP LGGSASSLAA
IPGASVPQVG VRQVDPGSIP DDLLNALIDF LAAVRNGLVP IIENRTPVAN PQQVSVPEGG
TVGPVRFDAC DPDGNRMTFA VRERGAPGGP QHGIVTVDQR TASFIYTADP GFVGTDTFSV
NVSDDTSLHV HGLAGYLGPF HGHDDVATVT VFVGNTPTDT ISGDFSMLTY NIAGLPFPLS
SAILPRFFYT KEIGKRLNAY YVANVQEDFA YHQFLIKKSK MPSQTPPEPP TLLWPIGVPF
SDGLNTLSEF KVQRLDRQTW YECTSDNCLT LKGFTYSQMR LPGGDTVDVY NLHTNTGGGP
TTNANLAQVA NYIQQNSAGR AVIVTGDFNA RYSDDQSALL QFAQVNGLTD AWVQVEHGPT
TPPFAPTCMV GNECELLDKI FYRSGQGVTL QAVSYGNEAP KFFNSKGEPL SDHSPAVVGF
HYVADNVAVR
