ID   SIPA_SALEN              Reviewed;         685 AA.
AC   Q8VQB5;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Cell invasion protein SipA;
DE   AltName: Full=Effector protein SipA;
GN   Name=sipA; Synonyms=sspA;
OS   Salmonella enteritidis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=149539;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=1009;
RA   Senocq D., Doz E., Virlogeux-Payant I.;
RL   Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
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:0000250}. Note=Secreted via the
CC       type III secretion system 1 (SPI-1 TTSS). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SipA/IpaA family. {ECO:0000305}.
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DR   EMBL; AF458099; AAL58882.1; -; Genomic_DNA.
DR   RefSeq; WP_000258819.1; NZ_WIAP01000022.1.
DR   AlphaFoldDB; Q8VQB5; -.
DR   SMR; Q8VQB5; -.
DR   PATRIC; fig|149539.316.peg.2926; -.
DR   OMA; DALDMCH; -.
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_0000221449"
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"
SQ   SEQUENCE   685 AA;  73972 MW;  5A6A012AFD34F49F CRC64;
     MVTSVRTQPP VIMPGMQTEI KTQATNLAAN LSAVRESATT 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