P0CL52 (SIPA_SALTY) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cell invasion protein SipA

Alternative name(s):
Effector protein SipA

Gene names

Name:	sipA
Synonyms:	sspA
Ordered Locus Names:	STM2882

Organism

Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]

Taxonomic identifier

99287 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › Salmonella choleraesuis › Salmonella enterica I › Salmonella typhimurium

Protein attributes

Sequence length	685 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Actin-binding protein that interferes with host cell actin cytoskeleton. It stimulates actin polymerization and counteracts F-actin destabilizing proteins. Potentiates SipC activity; both are required for an efficient bacterial internalization. In vitro, forms a complex with host cell protein T-plastin increasing actin bundling. It inhibits ADF/cofilin-directed depolymerization both by preventing binding of ADF and cofilin and by displacing them from F-actin. Also protects F-actin from gelsolin-directed severing and reanneals gelsolin-severed F-actin fragments. Ref.3 Ref.6
Subcellular location	Secreted. Note: Secreted via the type III secretion system 1 (SPI-1 TTSS). Ref.2
Sequence similarities	Belongs to the SipA/IpaA family.

Ontologies

Keywords
Biological process	Virulence
Cellular component	Secreted
Ligand	Actin-binding
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 685

685

Cell invasion protein SipA

PRO_0000221451

Regions

Region

497 – 669

173

Actin-binding and polymerization

Secondary structure

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685

Helix Strand Turn

Details...

Helix

26 – 29

4

Beta strand

31 – 39

9

Helix

51 – 53

3

Helix

55 – 68

14

Helix

73 – 82

10

Helix

86 – 105

20

Turn

106 – 108

3

Helix

110 – 130

21

Beta strand

137 – 139

3

Helix

146 – 165

20

Helix

168 – 181

14

Helix

183 – 195

13

Helix

201 – 227

27

Helix

245 – 258

14

Turn

522 – 525

4

Helix

526 – 528

3

Helix

532 – 535

4

Helix

542 – 553

12

Helix

562 – 575

14

Helix

580 – 590

11

Helix

591 – 595

5

Helix

597 – 611

15

Helix

616 – 630

15

Turn

632 – 635

4

Helix

636 – 638

3

Helix

641 – 650

10

Helix

655 – 657

3

Sequences

	Sequence		Length	Mass (Da)
	P0CL52 [UniParc]. Last modified March 8, 2011. Version 1. Checksum: 86B1602D4B5DB56F	FASTA	685	73,942
	10 20 30 40 50 60 MVTSVRTQPP VIMPGMQTEI KTQATNLAAN LSAVRESATA TLSGEIKGPQ LEDFPALIKQ 70 80 90 100 110 120 ASLDALFKCG KDAEALKEVF TNSNNVAGKK AIMEFAGLFR SALNATSDSP EAKTLLMKVG 130 140 150 160 170 180 AEYTAQIIKD GLKEKSAFGP WLPETKKAEA KLENLEKQLL DIIKNNTGGE LSKLSTNLVM 190 200 210 220 230 240 QEVMPYIASC IEHNFGCTLD PLTRSNLTHL VDKAAAKAVE ALDMCHQKLT QEQGTSVGRE 250 260 270 280 290 300 ARHLEMQTLI PLLLRNVFAQ IPADKLPDPK IPEPAAGPVP DGGKKAEPTG INININIDSS 310 320 330 340 350 360 NHSVDNSKHI NNSRSHVDNS QRHIDNSNHD NSRKTIDNSR TFIDNSQRNG ESHHSTNSSN 370 380 390 400 410 420 VSHSHSRVDS TTHQTETAHS ASTGAIDHGI AGKIDVTAHA TAEAVTNASS ESKDGKVVTS 430 440 450 460 470 480 EKGTTGETTS FDEVDGVTSK SIIGKPVQAT VHGVDDNKQQ SQTAEIVNVK PLASQLAGVE 490 500 510 520 530 540 NVKTDTLQSD TTVITGNKAG TTDNDNSQTD KTGPFSGLKF KQNSFLSTVP SVTNMHSMHF 550 560 570 580 590 600 DARETFLGVI RKALEPDTST PFPVRRAFDG LRAEILPNDT IKSAALKAQC SDIDKHPELK 610 620 630 640 650 660 AKMETLKEVI THHPQKEKLA EIALQFAREA GLTRLKGETD YVLSNVLDGL IGDGSWRAGP 670 680 AYESYLNKPG VDRVITTVDG LHMQR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LT2 / SGSC1412 / ATCC 700720.
[2]	"Identification of two targets of the type III protein secretion system encoded by the inv and spa loci of Salmonella typhimurium that have homology to the Shigella IpaD and IpaA proteins." Kaniga K., Trollinger D., Galan J.E. J. Bacteriol. 177:7078-7085(1995) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION. Strain: SL1344.
[3]	"Role of the S. typhimurium actin-binding protein SipA in bacterial internalization." Zhou D., Mooseker M.S., Galan J.E. Science 283:2092-2095(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION. Strain: SL1344.
[4]	"An invasion-associated Salmonella protein modulates the actin-bundling activity of plastin." Zhou D., Mooseker M.S., Galan J.E. Proc. Natl. Acad. Sci. U.S.A. 96:10176-10181(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HOST T-PLASTIN. Strain: SL1344.
[5]	"Cooperation between actin-binding proteins of invasive Salmonella: SipA potentiates SipC nucleation and bundling of actin." McGhie E.J., Hayward R.D., Koronakis V. EMBO J. 20:2131-2139(2001) [PubMed] [Europe PMC] [Abstract] Cited for: COOPERATIVE INTERACTION WITH SIPC. Strain: SJW1103.
[6]	"Control of actin turnover by a salmonella invasion protein." McGhie E.J., Hayward R.D., Koronakis V. Mol. Cell 13:497-510(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION. Strain: SJW1103.
[7]	"Salmonella SipA polymerizes actin by stapling filaments with nonglobular protein arms." Lilic M., Galkin V.E., Orlova A., VanLoock M.S., Egelman E.H., Stebbins C.E. Science 301:1918-1921(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 499-668, INTERACTION WITH HOST F-ACTIN.
[8]	"A common structural motif in the binding of virulence factors to bacterial secretion chaperones." Lilic M., Vujanac M., Stebbins C.E. Mol. Cell 21:653-664(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 23-262 ALONE AND IN COMPLEX WITH SPAK.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE006468 Genomic DNA. Translation: AAL21762.1.

RefSeq

NP_461803.1. NC_003197.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Q5Z	X-ray	1.80	A	498-670	[»]
2FM8	X-ray	2.20	C	23-262	[»]
2FM9	X-ray	2.00	A	49-263	[»]

ProteinModelPortal

P0CL52.

SMR

P0CL52. Positions 23-262, 514-658.

ModBase

Search...

Proteomic databases

PRIDE

P0CL52.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAL21762; AAL21762; STM2882.

GeneID

1254405.

KEGG

stm:STM2882.

PATRIC

32384452. VBISalEnt20916_3038.

Phylogenomic databases

HOGENOM

HOG000028234.

KO

K13284.

OMA

ETPSFDE.

Family and domain databases

InterPro

IPR015138. SipA.
IPR023224. SipA_actin-bd_C.
IPR023225. SipA_chaperone-bd.
[Graphical view]

Pfam

PF09052. SipA. 1 hit.
[Graphical view]

SUPFAM

SSF101312. SipA_actin-bd_C. 1 hit.
SSF140746. SSF140746. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P0CL52.

Entry information

Entry name

SIPA_SALTY

Accession

Primary (citable) accession number: P0CL52
Secondary accession number(s): Q56027, Q56034, Q8ZMH9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 8, 2011
Last sequence update:	March 8, 2011
Last modified:	May 1, 2013
This is version 16 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program