SIPA_SALTY
ID SIPA_SALTY Reviewed; 685 AA.
AC P0CL52; Q56027; Q56034; Q8ZMH9;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Cell invasion protein SipA;
DE AltName: Full=Effector protein SipA;
GN Name=sipA; Synonyms=sspA; OrderedLocusNames=STM2882;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP SUBCELLULAR LOCATION.
RC STRAIN=SL1344;
RX PubMed=8522512; DOI=10.1128/jb.177.24.7078-7085.1995;
RA Kaniga K., Trollinger D., Galan J.E.;
RT "Identification of two targets of the type III protein secretion system
RT encoded by the inv and spa loci of Salmonella typhimurium that have
RT homology to the Shigella IpaD and IpaA proteins.";
RL J. Bacteriol. 177:7078-7085(1995).
RN [3]
RP FUNCTION.
RC STRAIN=SL1344;
RX PubMed=10092234; DOI=10.1126/science.283.5410.2092;
RA Zhou D., Mooseker M.S., Galan J.E.;
RT "Role of the S. typhimurium actin-binding protein SipA in bacterial
RT internalization.";
RL Science 283:2092-2095(1999).
RN [4]
RP INTERACTION WITH HOST T-PLASTIN.
RC STRAIN=SL1344;
RX PubMed=10468582; DOI=10.1073/pnas.96.18.10176;
RA Zhou D., Mooseker M.S., Galan J.E.;
RT "An invasion-associated Salmonella protein modulates the actin-bundling
RT activity of plastin.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:10176-10181(1999).
RN [5]
RP COOPERATIVE INTERACTION WITH SIPC.
RC STRAIN=SJW1103;
RX PubMed=11331579; DOI=10.1093/emboj/20.9.2131;
RA McGhie E.J., Hayward R.D., Koronakis V.;
RT "Cooperation between actin-binding proteins of invasive Salmonella: SipA
RT potentiates SipC nucleation and bundling of actin.";
RL EMBO J. 20:2131-2139(2001).
RN [6]
RP FUNCTION.
RC STRAIN=SJW1103;
RX PubMed=14992720; DOI=10.1016/s1097-2765(04)00053-x;
RA McGhie E.J., Hayward R.D., Koronakis V.;
RT "Control of actin turnover by a salmonella invasion protein.";
RL Mol. Cell 13:497-510(2004).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 499-668, AND INTERACTION WITH HOST
RP F-ACTIN.
RX PubMed=14512630; DOI=10.1126/science.1088433;
RA Lilic M., Galkin V.E., Orlova A., VanLoock M.S., Egelman E.H.,
RA Stebbins C.E.;
RT "Salmonella SipA polymerizes actin by stapling filaments with nonglobular
RT protein arms.";
RL Science 301:1918-1921(2003).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 23-262 ALONE AND IN COMPLEX WITH
RP SPAK.
RX PubMed=16507363; DOI=10.1016/j.molcel.2006.01.026;
RA Lilic M., Vujanac M., Stebbins C.E.;
RT "A common structural motif in the binding of virulence factors to bacterial
RT secretion chaperones.";
RL Mol. Cell 21:653-664(2006).
CC -!- FUNCTION: Actin-binding protein that interferes with host cell actin
CC cytoskeleton. It stimulates actin polymerization and counteracts F-
CC actin destabilizing proteins. Potentiates SipC activity; both are
CC required for an efficient bacterial internalization. In vitro, forms a
CC complex with host cell protein T-plastin increasing actin bundling. It
CC inhibits ADF/cofilin-directed depolymerization both by preventing
CC binding of ADF and cofilin and by displacing them from F-actin. Also
CC protects F-actin from gelsolin-directed severing and reanneals
CC gelsolin-severed F-actin fragments. {ECO:0000269|PubMed:10092234,
CC ECO:0000269|PubMed:14992720}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8522512}.
CC Note=Secreted via the type III secretion system 1 (SPI-1 TTSS).
CC -!- SIMILARITY: Belongs to the SipA/IpaA family. {ECO:0000305}.
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DR EMBL; AE006468; AAL21762.1; -; Genomic_DNA.
DR RefSeq; NP_461803.1; NC_003197.2.
DR RefSeq; WP_000258811.1; NC_003197.2.
DR PDB; 1Q5Z; X-ray; 1.80 A; A=498-670.
DR PDB; 2FM8; X-ray; 2.20 A; C=23-262.
DR PDB; 2FM9; X-ray; 2.00 A; A=49-263.
DR PDBsum; 1Q5Z; -.
DR PDBsum; 2FM8; -.
DR PDBsum; 2FM9; -.
DR AlphaFoldDB; P0CL52; -.
DR SMR; P0CL52; -.
DR STRING; 99287.STM2882; -.
DR PaxDb; P0CL52; -.
DR PRIDE; P0CL52; -.
DR EnsemblBacteria; AAL21762; AAL21762; STM2882.
DR GeneID; 1254405; -.
DR KEGG; stm:STM2882; -.
DR PATRIC; fig|99287.12.peg.3038; -.
DR HOGENOM; CLU_410980_0_0_6; -.
DR OMA; DALDMCH; -.
DR BioCyc; SENT99287:STM2882-MON; -.
DR EvolutionaryTrace; P0CL52; -.
DR PHI-base; PHI:7224; -.
DR PHI-base; PHI:7922; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR DisProt; DP00157; -.
DR Gene3D; 1.10.4110.10; -; 1.
DR Gene3D; 1.10.4150.10; -; 1.
DR InterPro; IPR023224; SipA_actin-bd_C_sf.
DR InterPro; IPR023225; SipA_chaperone-bd.
DR InterPro; IPR015138; SipA_N.
DR Pfam; PF09052; SipA; 1.
DR SUPFAM; SSF101312; SSF101312; 1.
DR SUPFAM; SSF140746; SSF140746; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Reference proteome; Secreted; Virulence.
FT CHAIN 1..685
FT /note="Cell invasion protein SipA"
FT /id="PRO_0000221451"
FT REGION 265..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..669
FT /note="Actin-binding and polymerization"
FT COMPBIAS 292..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:2FM8"
FT STRAND 31..39
FT /evidence="ECO:0007829|PDB:2FM8"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:2FM9"
FT HELIX 55..68
FT /evidence="ECO:0007829|PDB:2FM9"
FT HELIX 73..82
FT /evidence="ECO:0007829|PDB:2FM9"
FT HELIX 86..105
FT /evidence="ECO:0007829|PDB:2FM9"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:2FM9"
FT HELIX 110..130
FT /evidence="ECO:0007829|PDB:2FM9"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:2FM9"
FT HELIX 146..165
FT /evidence="ECO:0007829|PDB:2FM9"
FT HELIX 168..181
FT /evidence="ECO:0007829|PDB:2FM9"
FT HELIX 183..195
FT /evidence="ECO:0007829|PDB:2FM9"
FT HELIX 201..227
FT /evidence="ECO:0007829|PDB:2FM9"
FT HELIX 245..258
FT /evidence="ECO:0007829|PDB:2FM9"
FT TURN 522..525
FT /evidence="ECO:0007829|PDB:1Q5Z"
FT HELIX 526..528
FT /evidence="ECO:0007829|PDB:1Q5Z"
FT HELIX 532..535
FT /evidence="ECO:0007829|PDB:1Q5Z"
FT HELIX 542..553
FT /evidence="ECO:0007829|PDB:1Q5Z"
FT HELIX 562..575
FT /evidence="ECO:0007829|PDB:1Q5Z"
FT HELIX 580..590
FT /evidence="ECO:0007829|PDB:1Q5Z"
FT HELIX 591..595
FT /evidence="ECO:0007829|PDB:1Q5Z"
FT HELIX 597..611
FT /evidence="ECO:0007829|PDB:1Q5Z"
FT HELIX 616..630
FT /evidence="ECO:0007829|PDB:1Q5Z"
FT TURN 632..635
FT /evidence="ECO:0007829|PDB:1Q5Z"
FT HELIX 636..638
FT /evidence="ECO:0007829|PDB:1Q5Z"
FT HELIX 641..650
FT /evidence="ECO:0007829|PDB:1Q5Z"
FT HELIX 655..657
FT /evidence="ECO:0007829|PDB:1Q5Z"
SQ SEQUENCE 685 AA; 73942 MW; 86B1602D4B5DB56F CRC64;
MVTSVRTQPP VIMPGMQTEI KTQATNLAAN LSAVRESATA TLSGEIKGPQ LEDFPALIKQ
ASLDALFKCG KDAEALKEVF TNSNNVAGKK AIMEFAGLFR SALNATSDSP EAKTLLMKVG
AEYTAQIIKD GLKEKSAFGP WLPETKKAEA KLENLEKQLL DIIKNNTGGE LSKLSTNLVM
QEVMPYIASC IEHNFGCTLD PLTRSNLTHL VDKAAAKAVE ALDMCHQKLT QEQGTSVGRE
ARHLEMQTLI PLLLRNVFAQ IPADKLPDPK IPEPAAGPVP DGGKKAEPTG INININIDSS
NHSVDNSKHI NNSRSHVDNS QRHIDNSNHD NSRKTIDNSR TFIDNSQRNG ESHHSTNSSN
VSHSHSRVDS TTHQTETAHS ASTGAIDHGI AGKIDVTAHA TAEAVTNASS ESKDGKVVTS
EKGTTGETTS FDEVDGVTSK SIIGKPVQAT VHGVDDNKQQ SQTAEIVNVK PLASQLAGVE
NVKTDTLQSD TTVITGNKAG TTDNDNSQTD KTGPFSGLKF KQNSFLSTVP SVTNMHSMHF
DARETFLGVI RKALEPDTST PFPVRRAFDG LRAEILPNDT IKSAALKAQC SDIDKHPELK
AKMETLKEVI THHPQKEKLA EIALQFAREA GLTRLKGETD YVLSNVLDGL IGDGSWRAGP
AYESYLNKPG VDRVITTVDG LHMQR
