SIPA_SALTS
ID SIPA_SALTS Reviewed; 685 AA.
AC E1WAC6; Q56027; Q56034; Q8ZMH9;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Cell invasion protein SipA;
DE AltName: Full=Effector protein SipA;
GN Name=sipA; Synonyms=sspA; OrderedLocusNames=SL1344_2861;
OS Salmonella typhimurium (strain SL1344).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=216597;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL1344;
RX PubMed=22538806; DOI=10.1073/pnas.1201061109;
RA Kroger C., Dillon S.C., Cameron A.D., Papenfort K., Sivasankaran S.K.,
RA Hokamp K., Chao Y., Sittka A., Hebrard M., Handler K., Colgan A.,
RA Leekitcharoenphon P., Langridge G.C., Lohan A.J., Loftus B., Lucchini S.,
RA Ussery D.W., Dorman C.J., Thomson N.R., Vogel J., Hinton J.C.;
RT "The transcriptional landscape and small RNAs of Salmonella enterica
RT serovar Typhimurium.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:E1277-E1286(2012).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-65.
RC STRAIN=SL1344;
RX PubMed=8748032; DOI=10.1111/j.1365-2958.1995.mmi_18030479.x;
RA Hueck C.J., Hantman M.J., Bajaj V., Johnston C., Lee C.A., Miller S.I.;
RT "Salmonella typhimurium secreted invasion determinants are homologous to
RT Shigella Ipa proteins.";
RL Mol. Microbiol. 18:479-490(1995).
RN [4]
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 [5]
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).
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 -!- 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; U40013; AAA86618.1; -; Genomic_DNA.
DR EMBL; FQ312003; CBW18959.1; -; Genomic_DNA.
DR EMBL; U30491; AAC43549.1; -; Genomic_DNA.
DR PIR; S70550; S70550.
DR RefSeq; WP_000258811.1; NZ_QASL01000017.1.
DR AlphaFoldDB; E1WAC6; -.
DR SMR; E1WAC6; -.
DR EnsemblBacteria; CBW18959; CBW18959; SL1344_2861.
DR KEGG; sey:SL1344_2861; -.
DR PATRIC; fig|216597.6.peg.3183; -.
DR HOGENOM; CLU_410980_0_0_6; -.
DR OMA; DALDMCH; -.
DR BioCyc; SENT216597:SL1344_RS14920-MON; -.
DR Proteomes; UP000008962; 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 1: Evidence at protein level;
KW Actin-binding; Secreted; Virulence.
FT CHAIN 1..685
FT /note="Cell invasion protein SipA"
FT /id="PRO_0000406088"
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 CONFLICT 36..44
FT /note="ESATATLSG -> AKCHSDAVR (in Ref. 1; AAA86618)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="T -> A (in Ref. 1; AAA86618)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="H -> P (in Ref. 1; AAA86618)"
FT /evidence="ECO:0000305"
FT CONFLICT 313..316
FT /note="SRSH -> AEP (in Ref. 1; AAA86618)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="S -> G (in Ref. 1; AAA86618)"
FT /evidence="ECO:0000305"
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
