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Protein

MAPK phosphothreonine lyase

Gene

spvC

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Active sitei106Proton donor1
Active sitei136Proton acceptor1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyase
Biological processVirulence

Enzyme and pathway databases

BioCyciSENT99287:G1FZD-4680-MONOMER

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella
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

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)DescriptionActionsGraphical viewLength
Mutagenesisi86F → D: Marked decrease in enzymatic activity. 1 Publication1
Mutagenesisi90R → E: Slight decrease in enzymatic activity. 1 Publication1
Mutagenesisi100F → E: Marked decrease in enzymatic activity. 2 Publications1
Mutagenesisi100F → L: Loss of enzymatic activity. 2 Publications1
Mutagenesisi104K → A or R: Loss of enzymatic activity. 2 Publications1
Mutagenesisi106H → A: Marked decrease in enzymatic activity. 2 Publications1
Mutagenesisi106H → K: 7-fold decrease in enzymatic activity, but no effect on substrate affinity. 2 Publications1
Mutagenesisi106H → N: Loss of enzymatic activity. 2 Publications1
Mutagenesisi134K → A: 2-fold decrease in enzymatic activity. 2 Publications1
Mutagenesisi134K → E: Slight decrease in enzymatic activity. 2 Publications1
Mutagenesisi134K → R: No effect on enzymatic activity. 2 Publications1
Mutagenesisi136K → A or R: Loss of enzymatic activity. 2 Publications1
Mutagenesisi148R → A: Marked decrease in enzymatic activity. 2 Publications1
Mutagenesisi148R → Q: Loss of enzymatic activity. 2 Publications1
Mutagenesisi149V → D: Loss of enzymatic activity. 1 Publication1
Mutagenesisi158Y → E: Marked decrease in enzymatic activity. 2 Publications1
Mutagenesisi158Y → F: 20-fold decrease in enzymatic activity, but no effect on substrate affinity. 2 Publications1
Mutagenesisi160K → A: More than 5-fold decrease in substrate affinity. 2 Publications1
Mutagenesisi160K → E: Slight decrease in enzymatic activity. 2 Publications1
Mutagenesisi160K → R: 2-fold decrease in enzymatic activity, but no effect on substrate affinity. 2 Publications1
Mutagenesisi201D → N: 47-fold decrease in enzymatic activity, but no effect on substrate affinity. 1 Publication1
Mutagenesisi213R → A or Q: Loss of enzymatic activity. 2 Publications1
Mutagenesisi215E → A: Nearly no decrease in enzymatic activity. 1 Publication1
Mutagenesisi220R → A: Marked decrease in enzymatic activity. 2 Publications1
Mutagenesisi220R → Q: Loss of enzymatic activity. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002216682 – 241MAPK phosphothreonine lyaseAdd BLAST240

Proteomic databases

PRIDEiP0A2M9

Interactioni

Protein-protein interaction databases

DIPiDIP-46403N
IntActiP0A2M9, 1 interactor

Structurei

Secondary structure

1241
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi29 – 35Combined sources7
Helixi37 – 44Combined sources8
Helixi61 – 64Combined sources4
Turni66 – 69Combined sources4
Beta strandi71 – 73Combined sources3
Beta strandi76 – 79Combined sources4
Beta strandi82 – 93Combined sources12
Beta strandi102 – 107Combined sources6
Helixi111 – 113Combined sources3
Helixi114 – 125Combined sources12
Beta strandi133 – 138Combined sources6
Turni140 – 142Combined sources3
Helixi147 – 150Combined sources4
Beta strandi155 – 158Combined sources4
Helixi170 – 189Combined sources20
Beta strandi208 – 214Combined sources7
Turni215 – 217Combined sources3
Helixi224 – 230Combined sources7
Helixi234 – 240Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A2M9

Family & Domainsi

Sequence similaritiesi

Belongs to the phosphothreonine lyase family.Curated

Phylogenomic databases

HOGENOMiHOG000028458
KOiK13450
OMAiFTLYVKP

Family and domain databases

Gene3Di3.30.2430.10, 1 hit
InterProiView protein in InterPro
IPR003519 OspF/SpvC
IPR038498 OspF/SpvC_sf
PfamiView protein in Pfam
PF03536 VRP3, 1 hit
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_003277.2
WP_001122242.1, NC_003277.2

Genome annotation databases

EnsemblBacteriaiAAL23529; AAL23529; PSLT038
GeneIDi1256201
KEGGistm:PSLT038
PATRICifig|99287.12.peg.4889

Similar proteinsi

Entry informationi

Entry nameiSPVC_SALTY
AccessioniPrimary (citable) accession number: P0A2M9
Secondary accession number(s): P21456
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 76 of the entry and version 2 of the sequence. See 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
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Main funding by: National Institutes of Health