UniProtKB - P9WKQ1 (SMASE_MYCTU)
Protein
Sphingomyelinase
Gene
spmT
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Functioni
Catalyzes the cleavage of sphingomyelin, a major lipid in eukaryotic cells, into ceramide and phosphocholine, which are then utilized by M.tuberculosis as carbon, nitrogen and phosphorus sources, respectively. Thus, enables M.tuberculosis to utilize sphingomyelin as a source of several essential nutrients for intracellular growth during infection. Furthermore, lyses erythrocytes and constitutes the main hemolytic factor of M.tuberculosis.1 Publication
Catalytic activityi
- EC:3.1.4.121 Publication
Kineticsi
kcat is 1797 sec(-1).1 Publication
- KM=671 µM for sphingomyelin1 Publication
pH dependencei
Is most active at neutral pH.1 Publication
GO - Molecular functioni
- neutral sphingomyelin phosphodiesterase activity Source: UniProtKB
- porin activity Source: UniProtKB-KW
- transmembrane transporter activity Source: UniProtKB
GO - Biological processi
- cellular response to lipid Source: UniProtKB
- hemolysis in other organism Source: UniProtKB
- ion transport Source: UniProtKB-KW
- organic substance transport Source: UniProtKB
- sphingomyelin catabolic process Source: UniProtKB
Keywordsi
Molecular function | Hydrolase, Porin |
Biological process | Cytolysis, Hemolysis, Ion transport, Lipid degradation, Lipid metabolism, Transport |
Enzyme and pathway databases
BioCyci | MTBH37RV:G185E-5042-MONOMER |
SABIO-RKi | P9WKQ1 |
Protein family/group databases
TCDBi | 1.B.79.1.1 the porin-sphingomyelinase fusion protein, spmt (spmt) family |
Names & Taxonomyi
Protein namesi | Recommended name: Sphingomyelinase1 Publication (EC:3.1.4.121 Publication)Short name: SMase1 Publication |
Gene namesi | Name:spmT1 Publication Ordered Locus Names:Rv0888 ORF Names:MTCY31.16 |
Organismi | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
Taxonomic identifieri | 83332 [NCBI] |
Taxonomic lineagei | Bacteria › Actinobacteria › Corynebacteriales › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › |
Proteomesi |
|
Organism-specific databases
TubercuListi | Rv0888 |
Subcellular locationi
- Cell outer membrane 1 Publication; Multi-pass membrane protein 1 Publication
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 32 – 136 | PeriplasmicCuratedAdd BLAST | 105 | |
Transmembranei | 137 – 145 | Beta strandedSequence analysis1 Publication | 9 | |
Topological domaini | 146 – 161 | ExtracellularCuratedAdd BLAST | 16 | |
Transmembranei | 162 – 168 | Beta strandedSequence analysis1 Publication | 7 | |
Topological domaini | 169 – 171 | PeriplasmicCurated | 3 | |
Transmembranei | 172 – 182 | Beta strandedSequence analysis1 PublicationAdd BLAST | 11 | |
Topological domaini | 183 – 187 | ExtracellularCurated | 5 | |
Transmembranei | 188 – 196 | Beta strandedSequence analysis1 Publication | 9 | |
Topological domaini | 197 – 204 | PeriplasmicCurated | 8 | |
Transmembranei | 205 – 213 | Beta strandedSequence analysis1 Publication | 9 | |
Topological domaini | 214 – 490 | Extracellular1 PublicationAdd BLAST | 277 |
GO - Cellular componenti
- cell outer membrane Source: UniProtKB
- pore complex Source: UniProtKB-KW
Keywords - Cellular componenti
Cell outer membrane, MembranePathology & Biotechi
Disruption phenotypei
Cells lacking this gene do not grow on sphingomyelin as a sole carbon source anymore and replicate poorly in macrophages indicating that M.tuberculosis utilizes sphingomyelin during infection. Moreover, deletion of this gene reduces lysis of erythrocytes by twofold compared with wild-type.1 Publication
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 353 | H → N: Loss of catalytic activity but still able to mediate uptake of glucose and phosphocholine; when associated with N-481. 1 Publication | 1 | |
Mutagenesisi | 481 | H → N: Loss of catalytic activity but still able to mediate uptake of glucose and phosphocholine; when associated with N-353. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 31 | Sequence analysis1 PublicationAdd BLAST | 31 | |
ChainiPRO_0000103731 | 32 – 490 | SphingomyelinaseAdd BLAST | 459 |
Proteomic databases
PaxDbi | P9WKQ1 |
Expressioni
Inductioni
Rv0888 protein levels are increased by 5-fold after contact with erythrocytes for 24 hours, and by 100-fold in the presence of sphingomyelin as the sole carbon source.1 Publication
Family & Domainsi
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 37 – 40 | Poly-SerSequence analysis | 4 |
Domaini
Consists of a surface-exposed C-terminal sphingomyelinase domain and a putative outer membrane-spanning N-terminal channel domain able to mediate glucose and phosphocholine uptake across the outer membrane.1 Publication
Sequence similaritiesi
Belongs to the SpmT family.Curated
Keywords - Domaini
Signal, Transmembrane, Transmembrane beta strandPhylogenomic databases
eggNOGi | ENOG4108PF7 Bacteria ENOG410Z1SH LUCA |
OMAi | PRFLYTK |
Family and domain databases
Gene3Di | 3.60.10.10, 1 hit |
InterProi | View protein in InterPro IPR036691 Endo/exonu/phosph_ase_sf IPR005135 Endo/exonuclease/phosphatase |
Pfami | View protein in Pfam PF03372 Exo_endo_phos, 1 hit |
SUPFAMi | SSF56219 SSF56219, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P9WKQ1-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MDYAKRIGQV GALAVVLGVG AAVTTHAIGS AAPTDPSSSS TDSPVDACSP
60 70 80 90 100
LGGSASSLAA IPGASVPQVG VRQVDPGSIP DDLLNALIDF LAAVRNGLVP
110 120 130 140 150
IIENRTPVAN PQQVSVPEGG TVGPVRFDAC DPDGNRMTFA VRERGAPGGP
160 170 180 190 200
QHGIVTVDQR TASFIYTADP GFVGTDTFSV NVSDDTSLHV HGLAGYLGPF
210 220 230 240 250
HGHDDVATVT VFVGNTPTDT ISGDFSMLTY NIAGLPFPLS SAILPRFFYT
260 270 280 290 300
KEIGKRLNAY YVANVQEDFA YHQFLIKKSK MPSQTPPEPP TLLWPIGVPF
310 320 330 340 350
SDGLNTLSEF KVQRLDRQTW YECTSDNCLT LKGFTYSQMR LPGGDTVDVY
360 370 380 390 400
NLHTNTGGGP TTNANLAQVA NYIQQNSAGR AVIVTGDFNA RYSDDQSALL
410 420 430 440 450
QFAQVNGLTD AWVQVEHGPT TPPFAPTCMV GNECELLDKI FYRSGQGVTL
460 470 480 490
QAVSYGNEAP KFFNSKGEPL SDHSPAVVGF HYVADNVAVR
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP43636.1 |
PIRi | E70781 |
RefSeqi | NP_215403.1, NC_000962.3 WP_003901038.1, NZ_NVQJ01000001.1 |
Genome annotation databases
EnsemblBacteriai | CCP43636; CCP43636; Rv0888 |
GeneIDi | 885210 |
KEGGi | mtu:Rv0888 mtv:RVBD_0888 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AL123456 Genomic DNA Translation: CCP43636.1 |
PIRi | E70781 |
RefSeqi | NP_215403.1, NC_000962.3 WP_003901038.1, NZ_NVQJ01000001.1 |
3D structure databases
ModBasei | Search... |
SWISS-MODEL-Workspacei | Submit a new modelling project... |
Protein-protein interaction databases
STRINGi | 83332.Rv0888 |
Protein family/group databases
TCDBi | 1.B.79.1.1 the porin-sphingomyelinase fusion protein, spmt (spmt) family |
Proteomic databases
PaxDbi | P9WKQ1 |
Genome annotation databases
EnsemblBacteriai | CCP43636; CCP43636; Rv0888 |
GeneIDi | 885210 |
KEGGi | mtu:Rv0888 mtv:RVBD_0888 |
Organism-specific databases
TubercuListi | Rv0888 |
Phylogenomic databases
eggNOGi | ENOG4108PF7 Bacteria ENOG410Z1SH LUCA |
OMAi | PRFLYTK |
Enzyme and pathway databases
BioCyci | MTBH37RV:G185E-5042-MONOMER |
SABIO-RKi | P9WKQ1 |
Family and domain databases
Gene3Di | 3.60.10.10, 1 hit |
InterProi | View protein in InterPro IPR036691 Endo/exonu/phosph_ase_sf IPR005135 Endo/exonuclease/phosphatase |
Pfami | View protein in Pfam PF03372 Exo_endo_phos, 1 hit |
SUPFAMi | SSF56219 SSF56219, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | SMASE_MYCTU | |
Accessioni | P9WKQ1Primary (citable) accession number: P9WKQ1 Secondary accession number(s): L0T574, P64743, Q10549 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 16, 2014 |
Last sequence update: | April 16, 2014 | |
Last modified: | October 16, 2019 | |
This is version 32 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Complete proteome, Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families - Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names