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PTKB_SHIFL
ID   PTKB_SHIFL              Reviewed;          94 AA.
AC   P0A437; Q8X7H5;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=PTS system galactitol-specific EIIB component {ECO:0000250|UniProtKB:P37188};
DE   AltName: Full=EIIB-Gat {ECO:0000250|UniProtKB:P37188};
DE   AltName: Full=Galactitol-specific phosphotransferase enzyme IIB component {ECO:0000250|UniProtKB:P37188};
DE            EC=2.7.1.200 {ECO:0000250|UniProtKB:P37188};
GN   Name=gatB; OrderedLocusNames=SF2155, S2281;
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 (PTS), a major carbohydrate active transport system, catalyzes
CC       the phosphorylation of incoming sugar substrates concomitant with their
CC       translocation across the cell membrane. The enzyme II complex composed
CC       of GatA, GatB and GatC is involved in galactitol transport.
CC       {ECO:0000250|UniProtKB:P37188}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=galactitol(out) + N(pros)-phospho-L-histidyl-[protein] =
CC         galactitol 1-phosphate(in) + L-histidyl-[protein];
CC         Xref=Rhea:RHEA:49248, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746,
CC         ChEBI:CHEBI:16813, ChEBI:CHEBI:29979, ChEBI:CHEBI:60083,
CC         ChEBI:CHEBI:64837; EC=2.7.1.200;
CC         Evidence={ECO:0000250|UniProtKB:P37188};
CC   -!- SUBUNIT: Forms a complex with one each of subunit of GatA, GatB and 2
CC       subunits of GatC. {ECO:0000250|UniProtKB:P37188}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: Constitutively expressed. {ECO:0000250|UniProtKB:P37188}.
CC   -!- DOMAIN: The EIIB domain is phosphorylated by phospho-EIIA on a
CC       cysteinyl or histidyl residue, depending on the transported sugar.
CC       Then, it transfers the phosphoryl group to the sugar substrate
CC       concomitantly with the sugar uptake processed by the EIIC domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00422}.
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DR   EMBL; AE005674; AAN43688.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP17514.1; -; Genomic_DNA.
DR   RefSeq; NP_707981.1; NC_004337.2.
DR   RefSeq; WP_000823288.1; NZ_WPGW01000098.1.
DR   AlphaFoldDB; P0A437; -.
DR   BMRB; P0A437; -.
DR   SMR; P0A437; -.
DR   STRING; 198214.SF2155; -.
DR   EnsemblBacteria; AAN43688; AAN43688; SF2155.
DR   EnsemblBacteria; AAP17514; AAP17514; S2281.
DR   GeneID; 1027334; -.
DR   GeneID; 58389578; -.
DR   KEGG; sfl:SF2155; -.
DR   KEGG; sfx:S2281; -.
DR   PATRIC; fig|198214.7.peg.2570; -.
DR   HOGENOM; CLU_159248_3_3_6; -.
DR   OMA; AHLICTT; -.
DR   OrthoDB; 1884107at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0019402; P:galactitol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   InterPro; IPR036095; PTS_EIIB-like_sf.
DR   InterPro; IPR013011; PTS_EIIB_2.
DR   InterPro; IPR003501; PTS_EIIB_2/3.
DR   Pfam; PF02302; PTS_IIB; 1.
DR   SUPFAM; SSF52794; SSF52794; 1.
DR   PROSITE; PS51099; PTS_EIIB_TYPE_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Galactitol metabolism; Phosphoprotein;
KW   Phosphotransferase system; Reference proteome; Sugar transport;
KW   Transferase; Transport.
FT   CHAIN           1..94
FT                   /note="PTS system galactitol-specific EIIB component"
FT                   /id="PRO_0000186575"
FT   DOMAIN          1..94
FT                   /note="PTS EIIB type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT   ACT_SITE        9
FT                   /note="Phosphocysteine intermediate; for EIIB activity"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         9
FT                   /note="Phosphocysteine; by EIIA"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   94 AA;  10195 MW;  44D4988E0ACACCCF CRC64;
     MKRKIIVACG GAVATSTMAA EEIKELCQSH NIPVELIQCR VNEIETYMDG VHLICTTARV
     DRSFGDIPLV HGMPFVSGVG IEALQNKILT ILQG
 
 
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