PTHA_SHIFL
ID PTHA_SHIFL Reviewed; 123 AA.
AC P59784;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=PTS system glucitol/sorbitol-specific EIIA component {ECO:0000250|UniProtKB:P05706};
DE AltName: Full=EIIA-Gut {ECO:0000250|UniProtKB:P05706};
DE AltName: Full=EIII-Gut {ECO:0000250|UniProtKB:P05706};
DE AltName: Full=Glucitol/sorbitol-specific phosphotransferase enzyme IIA component {ECO:0000250|UniProtKB:P05706};
GN Name=srlB; OrderedLocusNames=SF2727, S2918;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
CC -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC system (sugar PTS), a major carbohydrate active transport system,
CC catalyzes the phosphorylation of incoming sugar substrates
CC concomitantly with their translocation across the cell membrane. The
CC enzyme II complex composed of SrlA, SrlB and SrlE is involved in
CC glucitol/sorbitol transport. {ECO:0000250|UniProtKB:P05706}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P05706}.
CC -!- DOMAIN: The EIIA domain is phosphorylated by phospho-HPr on a histidyl
CC residue. Then, it transfers the phosphoryl group to the EIIB domain.
CC {ECO:0000255|PROSITE-ProRule:PRU00420}.
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DR EMBL; AE005674; AAN44218.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP18044.1; -; Genomic_DNA.
DR RefSeq; NP_708511.1; NC_004337.2.
DR RefSeq; WP_000216201.1; NZ_WPGW01000014.1.
DR AlphaFoldDB; P59784; -.
DR SMR; P59784; -.
DR STRING; 198214.SF2727; -.
DR EnsemblBacteria; AAN44218; AAN44218; SF2727.
DR EnsemblBacteria; AAP18044; AAP18044; S2918.
DR GeneID; 1025719; -.
DR GeneID; 66673427; -.
DR KEGG; sfl:SF2727; -.
DR KEGG; sfx:S2918; -.
DR PATRIC; fig|198214.7.peg.3248; -.
DR HOGENOM; CLU_138435_2_1_6; -.
DR OMA; MLITFKQ; -.
DR OrthoDB; 1589263at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; ISS:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 2.40.33.40; -; 1.
DR InterPro; IPR004716; PTS_IIA_glucitol/sorbitol-sp.
DR InterPro; IPR036665; PTS_IIA_glucitol/sorbitol_sf.
DR InterPro; IPR018454; PTS_IIA_glucitol/sorbitol_sub.
DR PANTHER; PTHR40398; PTHR40398; 1.
DR Pfam; PF03829; PTSIIA_gutA; 1.
DR SUPFAM; SSF141530; SSF141530; 1.
DR TIGRFAMs; TIGR00849; gutA; 1.
DR PROSITE; PS51097; PTS_EIIA_TYPE_5; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Kinase; Phosphoprotein; Phosphotransferase system;
KW Reference proteome; Sugar transport; Transferase; Transport.
FT CHAIN 1..123
FT /note="PTS system glucitol/sorbitol-specific EIIA
FT component"
FT /id="PRO_0000186569"
FT DOMAIN 1..116
FT /note="PTS EIIA type-5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00420"
FT ACT_SITE 43
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000305"
FT MOD_RES 43
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00420"
SQ SEQUENCE 123 AA; 13292 MW; F9FA893B8113C546 CRC64;
MTVIYQTTIT RIGASATDAL SDQMLITFRE GAPADLEEYC FIHCHGELKG ALHPGLQFSL
GQHRYPVTAV GSVAEDNLRE LGHVTLRFDG LNEAEFPGTV HVAGPVPDDI APGSVLKFES
VKE
