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Protein

MAPK phosphothreonine lyase

Gene

spvC

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Secreted effector that irreversibly inactivates host MAP kinases by catalyzing the dephosphorylation of the phosphothreonine residue in the pT-X-pY motif in MAPK2/ERK2, MAPK3/ERK1, and p38, via a beta-elimination reaction leading to a dehydrobutyrine residue. Is also able to remove the phosphate group from phospho-JNK in vitro, but JNK may not be a substrate in vivo. Could help suppress localized proinflammatory responses at infection foci in the spleen and liver, and thereby facilitate bacterial growth.4 Publications

Kineticsi

kcat is 10.60 sec(-1) with the Erk2 phosphopeptide DHTGFL-pT-E-pY-VATR as substrate.

  1. KM=52.2 µM for the Erk2 phosphopeptide DHTGFL-pT-E-pY-VATR1 Publication
  1. Vmax=22.72 µmol/min/mg enzyme with the Erk2 phosphopeptide DHTGFL-pT-E-pY-VATR as substrate1 Publication

pH dependencei

Optimum pH is 8.5.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei106 – 1061Proton donor
Active sitei136 – 1361Proton acceptor

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Virulence

Names & Taxonomyi

Protein namesi
Recommended name:
MAPK phosphothreonine lyase (EC:4.2.3.-)
Alternative name(s):
27.5 kDa virulence protein
Secreted effector protein SpvC
Gene namesi
Name:spvC
Synonyms:mkaD, vsdD
Ordered Locus Names:PSLT038
Encoded oniPlasmid pSLT3 Publications
Plasmid pEX1022 Publications
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Plasmid pSLT

Subcellular locationi

  • Secreted 1 Publication

  • Note: Can be secreted in vitro by either the SPI-1 or SPI-2 type III secretion systems (T3SS). Translocation of the protein into the cytosol of infected macrophages by intracellular bacteria is dependent on the SPI-2 T3SS. Translocated SpvC proteins appear to be distributed evenly in the cytoplasm of infected cells, and neither colocalize with the SCV membrane nor accumulate in the nucleus of infected cells.

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Disruption phenotypei

Strains lacking this gene are attenuated for systemic virulence in mice.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi86 – 861F → D: Marked decrease in enzymatic activity. 1 Publication
Mutagenesisi90 – 901R → E: Slight decrease in enzymatic activity. 1 Publication
Mutagenesisi100 – 1001F → E: Marked decrease in enzymatic activity. 2 Publications
Mutagenesisi100 – 1001F → L: Loss of enzymatic activity. 2 Publications
Mutagenesisi104 – 1041K → A or R: Loss of enzymatic activity. 2 Publications
Mutagenesisi106 – 1061H → A: Marked decrease in enzymatic activity. 2 Publications
Mutagenesisi106 – 1061H → K: 7-fold decrease in enzymatic activity, but no effect on substrate affinity. 2 Publications
Mutagenesisi106 – 1061H → N: Loss of enzymatic activity. 2 Publications
Mutagenesisi134 – 1341K → A: 2-fold decrease in enzymatic activity. 2 Publications
Mutagenesisi134 – 1341K → E: Slight decrease in enzymatic activity. 2 Publications
Mutagenesisi134 – 1341K → R: No effect on enzymatic activity. 2 Publications
Mutagenesisi136 – 1361K → A or R: Loss of enzymatic activity. 2 Publications
Mutagenesisi148 – 1481R → A: Marked decrease in enzymatic activity. 2 Publications
Mutagenesisi148 – 1481R → Q: Loss of enzymatic activity. 2 Publications
Mutagenesisi149 – 1491V → D: Loss of enzymatic activity. 1 Publication
Mutagenesisi158 – 1581Y → E: Marked decrease in enzymatic activity. 2 Publications
Mutagenesisi158 – 1581Y → F: 20-fold decrease in enzymatic activity, but no effect on substrate affinity. 2 Publications
Mutagenesisi160 – 1601K → A: More than 5-fold decrease in substrate affinity. 2 Publications
Mutagenesisi160 – 1601K → E: Slight decrease in enzymatic activity. 2 Publications
Mutagenesisi160 – 1601K → R: 2-fold decrease in enzymatic activity, but no effect on substrate affinity. 2 Publications
Mutagenesisi201 – 2011D → N: 47-fold decrease in enzymatic activity, but no effect on substrate affinity. 1 Publication
Mutagenesisi213 – 2131R → A or Q: Loss of enzymatic activity. 2 Publications
Mutagenesisi215 – 2151E → A: Nearly no decrease in enzymatic activity. 1 Publication
Mutagenesisi220 – 2201R → A: Marked decrease in enzymatic activity. 2 Publications
Mutagenesisi220 – 2201R → Q: Loss of enzymatic activity. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 241240MAPK phosphothreonine lyasePRO_0000221668Add
BLAST

Proteomic databases

PRIDEiP0A2M9.

Interactioni

Protein-protein interaction databases

DIPiDIP-46403N.

Structurei

Secondary structure

1
241
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi29 – 357Combined sources
Helixi37 – 448Combined sources
Helixi61 – 644Combined sources
Turni66 – 694Combined sources
Beta strandi71 – 733Combined sources
Beta strandi76 – 794Combined sources
Beta strandi82 – 9312Combined sources
Beta strandi102 – 1076Combined sources
Helixi111 – 1133Combined sources
Helixi114 – 12512Combined sources
Beta strandi133 – 1386Combined sources
Turni140 – 1423Combined sources
Helixi147 – 1504Combined sources
Beta strandi155 – 1584Combined sources
Helixi170 – 18920Combined sources
Beta strandi208 – 2147Combined sources
Turni215 – 2173Combined sources
Helixi224 – 2307Combined sources
Helixi234 – 2407Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2P1WX-ray2.30A1-241[»]
2Q8YX-ray2.00A1-241[»]
2Z8MX-ray2.00A/B1-241[»]
2Z8NX-ray1.80A/B1-241[»]
2Z8OX-ray2.40A/B1-241[»]
2Z8PX-ray1.80A1-241[»]
4H43X-ray2.30A/B1-241[»]
4HAHX-ray1.80A/B1-241[»]
ProteinModelPortaliP0A2M9.
SMRiP0A2M9. Positions 27-241.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A2M9.

Family & Domainsi

Sequence similaritiesi

Belongs to the phosphothreonine lyase family.Curated

Phylogenomic databases

HOGENOMiHOG000028458.
KOiK13450.
OMAiFTLYVKP.
OrthoDBiEOG6MM1JV.

Family and domain databases

InterProiIPR003519. OspF/SpvC.
[Graphical view]
PfamiPF03536. VRP3. 1 hit.
[Graphical view]
PRINTSiPR01342. SALVRPPROT.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A2M9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPINRPNLNL NIPPLNIVAA YDGAEIPSTN KHLKNNFNSL HNQMRKMPVS
60 70 80 90 100
HFKEALDVPD YSGMRQSGFF AMSQGFQLNN HGYDVFIHAR RESPQSQGKF
110 120 130 140 150
AGDKFHISVL RDMVPQAFQA LSGLLFSEDS PVDKWKVTDM EKVVQQARVS
160 170 180 190 200
LGAQFTLYIK PDQENSQYSA SFLHKTRQFI ECLESRLSEN GVISGQCPES
210 220 230 240
DVHPENWKYL SYRNELRSGR DGGEMQRQAL REEPFYRLMT E
Length:241
Mass (Da):27,646
Last modified:January 23, 2007 - v2
Checksum:i77625271D78F8814
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34355 Genomic DNA. Translation: AAA27162.1.
AE006471 Genomic DNA. Translation: AAL23529.1.
PIRiJQ0747.
RefSeqiNP_490528.1. NC_003277.1.
WP_001122242.1. NC_003277.1.

Genome annotation databases

EnsemblBacteriaiAAL23529; AAL23529; PSLT038.
GeneIDi1256201.
KEGGistm:PSLT038.
PATRICi32388260. VBISalEnt20916_4889.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34355 Genomic DNA. Translation: AAA27162.1.
AE006471 Genomic DNA. Translation: AAL23529.1.
PIRiJQ0747.
RefSeqiNP_490528.1. NC_003277.1.
WP_001122242.1. NC_003277.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2P1WX-ray2.30A1-241[»]
2Q8YX-ray2.00A1-241[»]
2Z8MX-ray2.00A/B1-241[»]
2Z8NX-ray1.80A/B1-241[»]
2Z8OX-ray2.40A/B1-241[»]
2Z8PX-ray1.80A1-241[»]
4H43X-ray2.30A/B1-241[»]
4HAHX-ray1.80A/B1-241[»]
ProteinModelPortaliP0A2M9.
SMRiP0A2M9. Positions 27-241.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-46403N.

Proteomic databases

PRIDEiP0A2M9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL23529; AAL23529; PSLT038.
GeneIDi1256201.
KEGGistm:PSLT038.
PATRICi32388260. VBISalEnt20916_4889.

Phylogenomic databases

HOGENOMiHOG000028458.
KOiK13450.
OMAiFTLYVKP.
OrthoDBiEOG6MM1JV.

Miscellaneous databases

EvolutionaryTraceiP0A2M9.

Family and domain databases

InterProiIPR003519. OspF/SpvC.
[Graphical view]
PfamiPF03536. VRP3. 1 hit.
[Graphical view]
PRINTSiPR01342. SALVRPPROT.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of mkaD, a virulence-associated gene of Salmonella typhimurium containing variable and constant regions."
    Taira S., Rhen M.
    Gene 93:147-150(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Plasmid: pEX102
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: LT2 / SGSC1412 / ATCC 700720.
    Plasmid: pSLT
  3. "Amino-terminal sequence analysis of four plasmid-encoded virulence-associated proteins of Salmonella typhimurium."
    Taira S., Baumann M., Riikonen P., Sukupolvi S., Rhen M.
    FEMS Microbiol. Lett. 77:319-323(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-10.
    Plasmid: pEX102
  4. "The phosphothreonine lyase activity of a bacterial type III effector family."
    Li H., Xu H., Zhou Y., Zhang J., Long C., Li S., Chen S., Zhou J.-M., Shao F.
    Science 315:1000-1003(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBSTRATES.
    Strain: LT2 / SGSC1412 / ATCC 700720.
    Plasmid: pSLT
  5. "SpvC is a Salmonella effector with phosphothreonine lyase activity on host mitogen-activated protein kinases."
    Mazurkiewicz P., Thomas J., Thompson J.A., Liu M., Arbibe L., Sansonetti P., Holden D.W.
    Mol. Microbiol. 67:1371-1383(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, ROLE IN VIRULENCE, SUBCELLULAR LOCATION, SECRETION VIA TYPE III SECRETION SYSTEM, DISRUPTION PHENOTYPE.
    Strain: ATCC 14028 / SGSC 2980 / CDC 6516-60 / NCTC 12023.
  6. "Structural insights into the enzymatic mechanism of the pathogenic MAPK phosphothreonine lyase."
    Zhu Y., Li H., Long C., Hu L., Xu H., Liu L., Chen S., Wang D.C., Shao F.
    Mol. Cell 28:899-913(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF APOENZYME AND MUTANT ALA-136 IN COMPLEX WITH A PHOSPHOPEPTIDE SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM, ACTIVE SITES, MUTAGENESIS OF PHE-100; LYS-104; HIS-106; LYS-134; LYS-136; ARG-148; TYR-158; LYS-160; ASP-201; ARG-213 AND ARG-220.
    Strain: LT2 / SGSC1412 / ATCC 700720.
    Plasmid: pSLT
  7. "Structural basis for the catalytic mechanism of phosphothreonine lyase."
    Chen L., Wang H., Zhang J., Gu L., Huang N., Zhou J.M., Chai J.
    Nat. Struct. Mol. Biol. 15:101-102(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF APOENZYME AND MUTANT ALA-136 IN COMPLEX WITH A PHOSPHOPEPTIDE SUBSTRATE, FUNCTION, ACTIVE SITES, MUTAGENESIS OF PHE-86; ARG-90; PHE-100; LYS-104; HIS-106; LYS-134; LYS-136; ARG-148; VAL-149; TYR-158; LYS-160; ARG-213; GLU-215 AND ARG-220.

Entry informationi

Entry nameiSPVC_SALTY
AccessioniPrimary (citable) accession number: P0A2M9
Secondary accession number(s): P21456
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: January 23, 2007
Last modified: December 9, 2015
This is version 67 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Plasmid, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.