SIPA_SALTI
ID SIPA_SALTI Reviewed; 685 AA.
AC P74849; Q56137; Q7C7N4; Q8Z494;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 2.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Cell invasion protein SipA;
DE AltName: Full=Effector protein SipA;
GN Name=sipA; Synonyms=sspA; OrderedLocusNames=STY3005, t2784;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-235.
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=8801431; DOI=10.1111/j.1365-2958.1995.mmi_17040781.x;
RA Hermant D., Menard R., Arricau N., Parsot C., Popoff M.Y.;
RT "Functional conservation of the Salmonella and Shigella effectors of entry
RT into epithelial cells.";
RL Mol. Microbiol. 17:781-789(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 236-685.
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=9404501; DOI=10.1016/s0923-2508(97)81896-7;
RA Arricau N., Hermant D., Waxin H., Popoff M.Y.;
RT "Molecular characterization of the Salmonella typhi StpA protein that is
RT related to both Yersinia YopE cytotoxin and YopH tyrosine phosphatase.";
RL Res. Microbiol. 148:21-26(1997).
RN [5]
RP SUBCELLULAR LOCATION.
RC STRAIN=GIFU 10007;
RX PubMed=11293481; DOI=10.1111/j.1348-0421.2001.tb01283.x;
RA Zhao L., Ezak T., Li Z.-Y., Kawamura Y., Hirose K., Watanabe H.;
RT "Vi-Suppressed wild strain Salmonella typhi cultured in high osmolarity is
RT hyperinvasive toward epithelial cells and destructive of Peyer's patches.";
RL Microbiol. Immunol. 45:149-158(2001).
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11293481}.
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; AL513382; CAD05989.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO70345.1; -; Genomic_DNA.
DR EMBL; X82670; CAA57991.1; -; Genomic_DNA.
DR EMBL; X92546; CAA63302.1; -; Genomic_DNA.
DR PIR; S70219; S70219.
DR RefSeq; NP_457276.1; NC_003198.1.
DR RefSeq; WP_000258814.1; NZ_WSUR01000005.1.
DR AlphaFoldDB; P74849; -.
DR SMR; P74849; -.
DR STRING; 220341.16503960; -.
DR EnsemblBacteria; AAO70345; AAO70345; t2784.
DR KEGG; stt:t2784; -.
DR KEGG; sty:STY3005; -.
DR PATRIC; fig|220341.7.peg.3059; -.
DR eggNOG; ENOG5032WWN; Bacteria.
DR HOGENOM; CLU_410980_0_0_6; -.
DR OMA; DALDMCH; -.
DR PHI-base; PHI:637; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Actin-binding; Secreted; Virulence.
FT CHAIN 1..685
FT /note="Cell invasion protein SipA"
FT /id="PRO_0000221450"
FT REGION 265..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..432
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 352..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 685 AA; 73940 MW; A9B722FE6751A4AB CRC64;
MVTSVRTQPP VIMPGMQTEI KTQATNLAAN LSAVRESATA TLSGEIKGQQ LEDFPALIKQ
ASLDALFKCG KDAEALKEVF TNSNNVAGKK AIMEFAGLFR SALNATSDSP EAKTLLMKVG
AEYTAQIIKD GLKEKSAFGP WLPETKKAEA KLENLEKQLL DIIKNNTGGE LSKLSTNLVM
QEVMPYIASC IEHNFGCTLD PLTRSSLTQL VDKAAAKAVE ALDMCHQKLT QEQGTSVGRE
ARHLEMQTLI PLLLRNVFAQ IPADKLPDPK IPEPAAGPVP DGGKKAEPTG INININIDSS
NHSVDNSKHI NNSRSHVDNS QRHIDNSNHD NSRKTIDNSR TFIDNSQRHG ESHHSTNSSN
VSHSHSRVDS TTHQTETAHS ASTGTIDHGI AGKIDVTAHA TAEAVTNSSS ESKDGKVVTS
EKGTTGETTS FDEVDGVTSK SIIGKPLQAT VHGVDDNKQQ SQTAEIVNVK PLASQLAGVE
NVKIDTLQSD STVITGNKAG TTDNDNSQTD KTGPFSGLKF KQNSFLSTVP SVTNMHSIHF
NAREAFLGVI RKALEPDAST PFPVRRAFDG LRGEILPNDT IKSAALKAQC SDIDKHPELK
AKMETLKEVI THHPQKEKLA EIALQFAREA GLTRQKGETD YVLSNVLDGL IGDGSWRAGP
AYESYLNKPG VDRVITTVDG LHMQR
