PTKB_ECOL6
ID PTKB_ECOL6 Reviewed; 94 AA.
AC P0A435; Q8X7H5;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=c2618;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
RN [2]
RP STRUCTURE BY NMR OF 2-94, ACTIVE SITE, SUBUNIT, AND PHOSPHORYLATION AT
RP CYS-9.
RX PubMed=16963640; DOI=10.1110/ps.062337406;
RA Volpon L., Young C.R., Matte A., Gehring K.;
RT "NMR structure of the enzyme GatB of the galactitol-specific
RT phosphoenolpyruvate-dependent phosphotransferase system and its interaction
RT with GatA.";
RL Protein Sci. 15:2435-2441(2006).
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 ECO:0000305|PubMed:16963640}.
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; AE014075; AAN81074.1; -; Genomic_DNA.
DR RefSeq; WP_000823288.1; NC_004431.1.
DR PDB; 1TVM; NMR; -; A=2-94.
DR PDBsum; 1TVM; -.
DR AlphaFoldDB; P0A435; -.
DR BMRB; P0A435; -.
DR SMR; P0A435; -.
DR STRING; 199310.c2618; -.
DR iPTMnet; P0A435; -.
DR EnsemblBacteria; AAN81074; AAN81074; c2618.
DR GeneID; 58389578; -.
DR KEGG; ecc:c2618; -.
DR eggNOG; COG3414; Bacteria.
DR HOGENOM; CLU_159248_3_3_6; -.
DR OMA; AHLICTT; -.
DR BioCyc; ECOL199310:C2618-MON; -.
DR EvolutionaryTrace; P0A435; -.
DR Proteomes; UP000001410; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Galactitol metabolism; Phosphoprotein;
KW Phosphotransferase system; Sugar transport; Transferase; Transport.
FT CHAIN 1..94
FT /note="PTS system galactitol-specific EIIB component"
FT /id="PRO_0000186573"
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|PubMed:16963640"
FT MOD_RES 9
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000305|PubMed:16963640"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:1TVM"
FT HELIX 15..29
FT /evidence="ECO:0007829|PDB:1TVM"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:1TVM"
FT TURN 41..46
FT /evidence="ECO:0007829|PDB:1TVM"
FT STRAND 52..58
FT /evidence="ECO:0007829|PDB:1TVM"
FT HELIX 73..77
FT /evidence="ECO:0007829|PDB:1TVM"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:1TVM"
FT HELIX 81..93
FT /evidence="ECO:0007829|PDB:1TVM"
SQ SEQUENCE 94 AA; 10195 MW; 44D4988E0ACACCCF CRC64;
MKRKIIVACG GAVATSTMAA EEIKELCQSH NIPVELIQCR VNEIETYMDG VHLICTTARV
DRSFGDIPLV HGMPFVSGVG IEALQNKILT ILQG
