P74873 (SPTP_SALTY) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Secreted effector protein sptP

Including the following 2 domains:

1. GTPase-activating protein
   Short name=GAP
2. Tyrosine-protein phosphatase
   EC=3.1.3.48

Gene names

Name:	sptP
Ordered Locus Names:	STM2878

Organism

Salmonella typhimurium

Taxonomic identifier

90371 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

Protein attributes

Sequence length	543 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein includes tyrosine phosphatase and GTPase activating protein (GAP) activities. After bacterial internalization, GAP mediates the reversal of the cytoskeletal changes induced by sopE. This function is independent of its tyrosine phosphatase activity, which remains unclear. Ref.1 Ref.4 Ref.5
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
Enzyme regulation	The tyrosine phosphatase activity is inhibited by sodium vanadate. Ref.1
Subunit structure	Forms a complex with sicP. Binds host RAC1.
Subcellular location	Secreted. Host cytoplasm. Note: Secreted via type III secretion system 1 (SPI-1 TTSS), and delivered into the host cytoplasm. Ref.4
Miscellaneous	Requires sicP as a chaperone for its stability and for secretion. The structure of the sptP-sicP complex contains four molecules of the chaperone sicP, aligned in a linear fashion and arranged in two sets of tightly bound homodimers that bind two sptP molecules. The sicP homodimers do not interact with each other, but are held together by a molecular interface formed between two sptP molecules. The chaperone-binding domain of sptP does not adopt a globular fold for interaction with sicP. Each sptP molecule is wrapped around by three sicP chaperones (two chaperones from one homodimer and a third one from the opposite homodimer pair). SptP interacts with sicP chaperone dimers mainly through four regions of its chaperone-binding domain.
Sequence similarities	In the N-terminal section; belongs to the yopE family. Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
Biological process	Virulence
Cellular component	Host cytoplasm Secreted
Molecular function	GTPase activation Hydrolase Protein phosphatase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular space Inferred from electronic annotation. Source: InterPro host cell cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	GTPase activator activity Inferred from electronic annotation. Source: UniProtKB-KW protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 543

543

Secreted effector protein sptP

PRO_0000094866

Regions

Domain

280 – 543

264

Tyrosine-protein phosphatase

Region

35 – 139

105

Chaperone-binding

Region

167 – 290

124

GAP

Sites

Active site

481

1

Phosphocysteine intermediate

Experimental info

Mutagenesis

209

1

R → A: Loss of GAP activity. Ref.4

Mutagenesis

213

1

T → A: Loss of RAC1 binding and GAP activity. Ref.5

Mutagenesis

246

1

Q → A: Loss of RAC1 binding and GAP activity. Ref.5

Mutagenesis

249

1

T → A: Loss of RAC1 binding and GAP activity. Ref.5

Mutagenesis

481

1

C → S: Loss of phosphatase activity. Ref.1

Secondary structure

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543

Helix Strand Turn

Details...

Beta strand

50 – 54

5

Helix

62 – 71

10

Helix

77 – 89

13

Helix

93 – 105

13

Helix

111 – 113

3

Beta strand

116 – 118

3

Helix

122 – 127

6

Helix

130 – 136

7

Helix

168 – 187

20

Helix

191 – 195

5

Helix

198 – 201

4

Helix

207 – 216

10

Helix

217 – 220

4

Helix

222 – 224

3

Helix

225 – 235

11

Beta strand

237 – 243

7

Helix

244 – 248

5

Beta strand

250 – 252

3

Helix

253 – 260

8

Helix

263 – 279

17

Helix

281 – 291

11

Turn

312 – 314

3

Beta strand

319 – 324

6

Beta strand

330 – 338

9

Beta strand

341 – 347

7

Helix

354 – 367

14

Beta strand

370 – 374

5

Helix

378 – 383

6

Beta strand

391 – 396

6

Beta strand

399 – 405

7

Beta strand

414 – 424

11

Beta strand

427 – 436

10

Helix

448 – 459

12

Beta strand

477 – 480

4

Beta strand

482 – 486

5

Helix

487 – 499

13

Helix

505 – 513

9

Turn

518 – 521

4

Helix

524 – 538

15

Sequences

	Sequence		Length	Mass (Da)
	P74873 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 060D2113EB5B5429	FASTA	543	60,048
	10 20 30 40 50 60 MLKYEERKLN NLTLSSFSKV GVSNDARLYI AKENTDKAYV APEKFSSKVL TWLGKMPLFK 70 80 90 100 110 120 NTEVVQKHTE NIRVQDQKIL QTFLHALTEK YGETAVNDAL LMSRINMNKP LTQRLAVQIT 130 140 150 160 170 180 ECVKAADEGF INLIKSKDNV GVRNAALVIK GGDTKVAEKN NDVGAESKQP LLDIALKGLK 190 200 210 220 230 240 RTLPQLEQMD GNSLRENFQE MASGNGPLRS LMTNLQNLNK IPEAKQLNDY VTTLTNIQVG 250 260 270 280 290 300 VARFSQWGTC GGEVERWVDK ASTHELTQAV KKIHVIAKEL KNVTAELEKI EAGAPMPQTM 310 320 330 340 350 360 SGPTLGLARF AVSSIPINQQ TQVKLSDGMP VPVNTLTFDG KPVALAGSYP KNTPDALEAH 370 380 390 400 410 420 MKMLLEKECS CLVVLTSEDQ MQAKQLPPYF RGSYTFGEVH TNSQKVSSAS QGEAIDQYNM 430 440 450 460 470 480 QLSCGEKRYT IPVLHVKNWP DHQPLPSTDQ LEYLADRVKN SNQNGAPGRS SSDKHLPMIH 490 500 510 520 530 540 CLGGVGRTGT MAAALVLKDN PHSNLEQVRA DFRDSRNNRM LEDASQFVQL KAMQAQLLMT TAS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A secreted protein tyrosine phosphatase with modular effector domains in the bacterial pathogen Salmonella typhimurium." Kaniga K., Uralil J., Bliska J.B., Galan J.E. Mol. Microbiol. 21:633-641(1996) [PubMed: 8866485] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ENZYME REGULATION, FUNCTION, MUTAGENESIS OF CYS-481. Strain: SL1344.
[2]	"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2." McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K. Nature 413:852-856(2001) [PubMed: 11677609] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720.
[3]	"Identification of a specific chaperone for SptP, a substrate of the centisome 63 type III secretion system of Salmonella typhimurium." Fu Y., Galan J.E. J. Bacteriol. 180:3393-3399(1998) [PubMed: 9642193] [Abstract] Cited for: INTERACTION WITH SICP. Strain: SL1344.
[4]	"A Salmonella protein antagonizes Rac-1 and Cdc42 to mediate host-cell recovery after bacterial invasion." Fu Y., Galan J.E. Nature 401:293-297(1999) [PubMed: 10499590] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-209. Strain: SB300.
[5]	"Modulation of host signaling by a bacterial mimic: structure of the Salmonella effector SptP bound to Rac1." Stebbins C.E., Galan J.E. Mol. Cell 6:1449-1460(2000) [PubMed: 11163217] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 161-543 IN COMPLEX WITH RAC1, FUNCTION, MUTAGENESIS OF THR-213; GLN-246 AND THR-249.
[6]	"Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion." Stebbins C.E., Galan J.E. Nature 414:77-81(2001) [PubMed: 11689946] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 35-139 IN COMPLEX WITH SICP.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U63293 Genomic DNA. Translation: AAC44349.1.
AE006468 Genomic DNA. Translation: AAL21758.1.

RefSeq

NP_461799.1. NC_003197.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1G4U	X-ray	2.30	S	161-543	[»]
1G4W	X-ray	2.20	R	161-543	[»]
1JYO	X-ray	1.90	E/F	35-139	[»]

ProteinModelPortal

P74873.

SMR

P74873. Positions 36-139, 167-539.

ModBase

Search...

Protein-protein interaction databases

IntAct

P74873. 2 interactions.

Protein family/group databases

PptaseDB

P3D0410147.

Proteomic databases

PRIDE

P74873.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

1254401.

GenomeReviews

Gene locus STM2878 in contig AE006468_GR.

KEGG

stm:STM2878.

NMPDR

fig|99287.1.peg.2776.

PATRIC

32384444. VBISalEnt20916_3034.

Phylogenomic databases

HOGENOM

HBG671449.

OMA

ALEAHMK.

ProtClustDB

PRK15375.

Enzyme and pathway databases

BioCyc

STYP99287:STM2878-MONOMER.

Family and domain databases

InterPro

IPR011070. Globular_prot_asu/bsu.
IPR015203. SicP-binding.
IPR000387. Tyr/Dual-specificity_Pase.
IPR016130. Tyr_Pase_AS.
IPR003546. Tyr_Pase_modular_bac.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
IPR014773. Uncharacterised_dom_YopE.
[Graphical view]

Gene3D

G3DSA:1.20.120.260. Uncharacterised_dom_YopE. 1 hit.

KO

K13740.

Pfam

PF09119. SicP-binding. 1 hit.
PF00102. Y_phosphatase. 1 hit.
PF03545. YopE. 1 hit.
[Graphical view]

PRINTS

PR01371. BACYPHPHTASE.

SMART

SM00194. PTPc. 1 hit.
[Graphical view]

SUPFAM

SSF56568. AlphaBeta_subunt. 1 hit.
SSF47233. Vir_YopE. 1 hit.

PROSITE

PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

SPTP_SALTY

Accession

Primary (citable) accession number: P74873
Secondary accession number(s): Q7CPX3

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2005
Last sequence update:	February 1, 1997
Last modified:	January 25, 2012
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program