ID STXA_SHIDS Reviewed; 315 AA.
AC Q32GM1;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 15-MAR-2017, entry version 60.
DE RecName: Full=Shiga toxin subunit A;
DE EC=3.2.2.22;
DE Flags: Precursor;
GN Name=stxA; OrderedLocusNames=SDY_1389;
OS Shigella dysenteriae serotype 1 (strain Sd197).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA Qiang B., Hou Y., Yu J., Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic
RT agents of bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
CC -!- FUNCTION: The A subunit is responsible for inhibiting protein
CC synthesis through the catalytic inactivation of 60S ribosomal
CC subunits. After endocytosis, the A subunit is cleaved by furin in
CC two fragments, A1 and A2: A1 is the catalytically active fragment,
CC and A2 is essential for holotoxin assembly with the B subunits (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY: Endohydrolysis of the N-glycosidic bond at one
CC specific adenosine on the 28S rRNA.
CC -!- SUBUNIT: Shiga toxin contains a single subunit A and five copies
CC of subunit B. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ribosome-inactivating protein family.
CC {ECO:0000305}.
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DR EMBL; CP000034; ABB61534.1; -; Genomic_DNA.
DR RefSeq; WP_000691354.1; NC_007606.1.
DR RefSeq; YP_403025.1; NC_007606.1.
DR ProteinModelPortal; Q32GM1; -.
DR SMR; Q32GM1; -.
DR PRIDE; Q32GM1; -.
DR EnsemblBacteria; ABB61534; ABB61534; SDY_1389.
DR GeneID; 3796555; -.
DR KEGG; sdy:SDY_1389; -.
DR PATRIC; 18692394; VBIShiDys99784_1650.
DR HOGENOM; HOG000010102; -.
DR KO; K11006; -.
DR OMA; CNMKIII; -.
DR OrthoDB; POG091H0COS; -.
DR Proteomes; UP000002716; Chromosome.
DR GO; GO:0030598; F:rRNA N-glycosylase activity; IEA:UniProtKB-EC.
DR GO; GO:0017148; P:negative regulation of translation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.420.10; -; 1.
DR Gene3D; 4.10.470.10; -; 1.
DR InterPro; IPR001574; Ribosome_inactivat_prot.
DR InterPro; IPR017988; Ribosome_inactivat_prot_CS.
DR InterPro; IPR016138; Ribosome_inactivat_prot_sub1.
DR InterPro; IPR016139; Ribosome_inactivat_prot_sub2.
DR InterPro; IPR016331; Shiga-like_toxin_subunit_A.
DR Pfam; PF00161; RIP; 1.
DR PIRSF; PIRSF001924; Shigella_toxin_subunit_A; 1.
DR SUPFAM; SSF56371; SSF56371; 1.
DR PROSITE; PS00275; SHIGA_RICIN; 1.
PE 3: Inferred from homology;
KW Complete proteome; Disulfide bond; Hydrolase;
KW Protein synthesis inhibitor; Reference proteome; Signal; Toxin.
FT SIGNAL 1 22 {ECO:0000255}.
FT CHAIN 23 315 Shiga toxin subunit A.
FT /FTId=PRO_0000312303.
FT REGION 23 273 A1.
FT REGION 274 315 A2.
FT ACT_SITE 189 189 {ECO:0000250}.
FT SITE 273 274 Cleavage; by furin. {ECO:0000250}.
FT DISULFID 264 283 {ECO:0000250}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 184 200 ipat:SHIGA_RICIN [T]
FT MYHIT 31 232 ipfam:RIP [T]
SQ SEQUENCE 315 AA; 34814 MW; 8A423DF7ABF58F30 CRC64;
MKIIIFRVLT FFFVIFSVNV VAKEFTLDFS TAKTYVDSLN VIRSAIGTPL QTISSGGTSL
LMIDSGTGDN LFAVDVRGID PEEGRFNNLR LIVERNNLYV TGFVNRTNNV FYRFADFSHV
TFPGTTAVTL SGDSSYTTLQ RVAGISRTGM QINRHSLTTS YLDLMSHSGT SLTQSVARAM
LRFVTVTAEA LRFRQIQRGF RTTLDDLSGR SYVMTAEDVD LTLNWGRLSS VLPDYHGQDS
VRVGRISFGS INAILGSVAL ILNCHHHASR VARMASDEFP SMCPADGRVR GITHNKILWD
SSTLGAILMR RTISS
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