SPAS_SHISO
ID SPAS_SHISO Reviewed; 342 AA.
AC P0A1M9; P40707;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 52.
DE RecName: Full=Surface presentation of antigens protein SpaS;
DE AltName: Full=Spa40 protein;
GN Name=spaS; Synonyms=spa40;
OS Shigella sonnei.
OG Plasmid pINV.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=624;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=HW383;
RA Arakawa E., Kato J., Ito K., Watanabe H.;
RT "Comparison and high conservation of nucleotide sequences of spa-mxi
RT regions between S.sonnei and S.flexneri -- identification of a new gene
RT coding plausible membrane protein.";
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for surface presentation of invasion plasmid
CC antigens. Could play a role in preserving the translocation competence
CC of the ipa antigens. Required for invasion and for secretion of the
CC three ipa proteins (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the type III secretion exporter family.
CC {ECO:0000305}.
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DR EMBL; D50601; BAA09165.1; -; Genomic_DNA.
DR AlphaFoldDB; P0A1M9; -.
DR SMR; P0A1M9; -.
DR STRING; 216599.GCA_000283715_05247; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009306; P:protein secretion; IEA:InterPro.
DR Gene3D; 3.40.1690.10; -; 1.
DR InterPro; IPR006307; BsaZ.
DR InterPro; IPR006135; T3SS_substrate_exporter.
DR InterPro; IPR029025; T3SS_substrate_exporter_C.
DR PANTHER; PTHR30531; PTHR30531; 1.
DR Pfam; PF01312; Bac_export_2; 1.
DR PRINTS; PR00950; TYPE3IMSPROT.
DR SUPFAM; SSF160544; SSF160544; 1.
DR TIGRFAMs; TIGR01404; FlhB_rel_III; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Plasmid; Transmembrane;
KW Transmembrane helix; Virulence.
FT CHAIN 1..342
FT /note="Surface presentation of antigens protein SpaS"
FT /id="PRO_0000180958"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 342 AA; 39852 MW; 48BBF531BFE034BC CRC64;
MANKTEKPTP KKLKDAAKKG QSFKFKDLTT VVIILVGTFT IISFFSLSDV MLLYRYVIIN
DFEINEGKYF FAVVIVFFKI IGFPLFFCVL SAVLPTLVQT KFVLATKAIK IDFSVLNPVK
GLKKIFSIKT IKEFFKSILL LIILALTTYF FWINDRKIIF SQVFSSVDGL YLIWGRLFKD
IILFFLAFSI LVIILDFVIE FILYMKDMMM DKQEIKREYI EQEGHFETKS RRRELHIEIL
SEQTKSDIRN SKLVVMNPTH IAIGIYFNPE IAPAPFISLI ETNQCALAVR KYANEVGIPT
VRDVKLARKL YKTHTKYSFV DFEHLDEVLR LIVWLEQVEN TH