PTKB_ECOLI
ID PTKB_ECOLI Reviewed; 94 AA.
AC P37188; P76412;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=PTS system galactitol-specific EIIB component {ECO:0000303|PubMed:7772602};
DE AltName: Full=EIIB-Gat {ECO:0000303|PubMed:7772602};
DE AltName: Full=Galactitol-specific phosphotransferase enzyme IIB component {ECO:0000303|PubMed:7772602};
DE EC=2.7.1.200 {ECO:0000269|PubMed:1100608};
GN Name=gatB {ECO:0000303|PubMed:7772602}; OrderedLocusNames=b2093, JW2077;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=EC3132;
RX PubMed=7772602; DOI=10.1016/0167-4781(95)00053-j;
RA Nobelmann B., Lengeler J.W.;
RT "Sequence of the gat operon for galactitol utilization from a wild-type
RT strain EC3132 of Escherichia coli.";
RL Biochim. Biophys. Acta 1262:69-72(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 1-20.
RC STRAIN=K12;
RX PubMed=9868784; DOI=10.1111/j.1574-6968.1998.tb13343.x;
RA Wasinger V.C., Humphery-Smith I.;
RT "Small genes/gene-products in Escherichia coli K-12.";
RL FEMS Microbiol. Lett. 169:375-382(1998).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP SPECIFICITY.
RX PubMed=1100608; DOI=10.1128/jb.124.1.39-47.1975;
RA Lengeler J.;
RT "Nature and properties of hexitol transport systems in Escherichia coli.";
RL J. Bacteriol. 124:39-47(1975).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=8955298; DOI=10.1128/jb.178.23.6790-6795.1996;
RA Nobelmann B., Lengeler J.W.;
RT "Molecular analysis of the gat genes from Escherichia coli and of their
RT roles in galactitol transport and metabolism.";
RL J. Bacteriol. 178:6790-6795(1996).
RN [8]
RP SUBUNIT.
RC STRAIN=BL21-DE3;
RX PubMed=16079137; DOI=10.1074/jbc.m506479200;
RA Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA von Heijne G., Daley D.O.;
RT "Protein complexes of the Escherichia coli cell envelope.";
RL J. Biol. Chem. 280:34409-34419(2005).
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. It can also
CC use D-glucitol. {ECO:0000269|PubMed:1100608,
CC ECO:0000269|PubMed:8955298}.
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:0000269|PubMed:1100608};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.4 uM for D-galactitol {ECO:0000269|PubMed:1100608};
CC KM=800 uM for D-glucitol {ECO:0000269|PubMed:1100608};
CC Vmax=3.2 nmol/min/mg enzyme with D-galactitol as substrate
CC {ECO:0000269|PubMed:1100608};
CC Vmax=3.2 nmol/min/mg enzyme with D-glucitol as substrate
CC {ECO:0000269|PubMed:1100608};
CC -!- SUBUNIT: Forms a complex with one each of subunit of GatA, GatB and 2
CC subunits of GatC. {ECO:0000269|PubMed:16079137}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:8955298}.
CC -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:8955298}.
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; X79837; CAA56229.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75154.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15956.1; -; Genomic_DNA.
DR PIR; D64976; D64976.
DR PIR; S55904; S55904.
DR RefSeq; NP_416596.1; NC_000913.3.
DR RefSeq; WP_000823270.1; NZ_SSZK01000011.1.
DR AlphaFoldDB; P37188; -.
DR SMR; P37188; -.
DR BioGRID; 4263510; 11.
DR BioGRID; 850956; 1.
DR ComplexPortal; CPX-5942; Galactitol-specific enzyme II complex.
DR DIP; DIP-9744N; -.
DR IntAct; P37188; 7.
DR STRING; 511145.b2093; -.
DR TCDB; 4.A.5.1.1; the pts galactitol (gat) family.
DR jPOST; P37188; -.
DR PaxDb; P37188; -.
DR PRIDE; P37188; -.
DR EnsemblBacteria; AAC75154; AAC75154; b2093.
DR EnsemblBacteria; BAA15956; BAA15956; BAA15956.
DR GeneID; 946610; -.
DR KEGG; ecj:JW2077; -.
DR KEGG; eco:b2093; -.
DR PATRIC; fig|1411691.4.peg.157; -.
DR EchoBASE; EB2314; -.
DR eggNOG; COG3414; Bacteria.
DR HOGENOM; CLU_159248_3_3_6; -.
DR OMA; AHLICTT; -.
DR PhylomeDB; P37188; -.
DR BioCyc; EcoCyc:GATB-MON; -.
DR BioCyc; MetaCyc:MON-124141; -.
DR BRENDA; 2.7.1.200; 2026.
DR PRO; PR:P37188; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:1902495; C:transmembrane transporter complex; IC:ComplexPortal.
DR GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR GO; GO:0090584; F:protein-phosphocysteine-galactitol-phosphotransferase system transporter activity; IDA:EcoCyc.
DR GO; GO:0019402; P:galactitol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0015796; P:galactitol transmembrane transport; IDA:EcoCyc.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IDA:EcoCyc.
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 Cytoplasm; Direct protein sequencing; Galactitol metabolism;
KW Phosphoprotein; Phosphotransferase system; Reference proteome;
KW Sugar transport; Transferase; Transport.
FT CHAIN 1..94
FT /note="PTS system galactitol-specific EIIB component"
FT /id="PRO_0000186572"
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"
FT CONFLICT 9
FT /note="C -> E (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="N -> S (in Ref. 1; CAA56229)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="K -> R (in Ref. 1; CAA56229)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="I -> V (in Ref. 1; CAA56229)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="I -> V (in Ref. 1; CAA56229)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 94 AA; 10222 MW; A8156F04894F0CD7 CRC64;
MKRKIIVACG GAVATSTMAA EEIKELCQNH NIPVELIQCR VNEIETYMDG VHLICTTAKV
DRSFGDIPLV HGMPFISGIG IEALQNKILT ILQG
