Entry sw: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   02-NOV-2016, entry version 142.
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};
GN   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-
RT   type 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.,
RA   Yamamoto Y., Horiuchi T.;
RT   "A 460-kb DNA sequence of the Escherichia coli K-12 genome
RT   corresponding to 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.,
RA   Mau B., 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
RT   MG1655 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
RP   SUBSTRATE SPECIFICITY.
RX   PubMed=1100608;
RA   Lengeler J.;
RT   "Nature and properties of hexitol transport systems in Escherichia
RT   coli.";
RL   J. Bacteriol. 124:39-47(1975).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX   PubMed=8955298;
RA   Nobelmann B., Lengeler J.W.;
RT   "Molecular analysis of the gat genes from Escherichia coli and of
RT   their 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
CC       phosphotransferase system (PTS), a major carbohydrate active
CC       transport system, catalyzes the phosphorylation of incoming sugar
CC       substrates concomitant with their translocation across the cell
CC       membrane. The enzyme II complex composed of GatA, GatB and GatC is
CC       involved in galactitol transport. It can also use D-glucitol.
CC       {ECO:0000269|PubMed:1100608, ECO:0000269|PubMed:8955298}.
CC   -!- CATALYTIC ACTIVITY: [Protein]-N(pi)-phospho-L-histidine +
CC       galactitol(Side 1) = [protein]-L-histidine + galactitol 1-
CC       phosphate(Side 2). {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
CC       and 2 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}.
CC   -!- SIMILARITY: Contains 1 PTS EIIB type-2 domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00422}.
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_LN832404.1.
DR   ProteinModelPortal; P37188; -.
DR   SMR; P37188; -.
DR   BioGrid; 4263510; 9.
DR   DIP; DIP-9744N; -.
DR   IntAct; P37188; 7.
DR   MINT; MINT-1222883; -.
DR   STRING; 511145.b2093; -.
DR   TCDB; 4.A.5.1.1; the pts galactitol (gat) family.
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; 32119519; VBIEscCol129921_2170.
DR   EchoBASE; EB2314; -.
DR   EcoGene; EG12415; gatB.
DR   eggNOG; ENOG41090UW; Bacteria.
DR   eggNOG; COG3414; LUCA.
DR   HOGENOM; HOG000230475; -.
DR   KO; K02774; -.
DR   OMA; ICTTAKI; -.
DR   PhylomeDB; P37188; -.
DR   BioCyc; EcoCyc:GATB-MONOMER; -.
DR   BioCyc; ECOL316407:JW2077-MONOMER; -.
DR   BioCyc; MetaCyc:GATB-MONOMER; -.
DR   PRO; PR:P37188; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
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 transport; IDA:EcoCyc.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IDA:EcoCyc.
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   Complete proteome; Cytoplasm; Direct protein sequencing;
KW   Galactitol metabolism; Phosphoprotein; Phosphotransferase system;
KW   Reference proteome; Sugar transport; Transferase; Transport.
FT   CHAIN         1     94       PTS system galactitol-specific EIIB
FT                                component.
FT                                /FTId=PRO_0000186572.
FT   DOMAIN        1     94       PTS EIIB type-2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00422}.
FT   ACT_SITE      9      9       Phosphocysteine intermediate; for EIIB
FT                                activity. {ECO:0000305}.
FT   MOD_RES       9      9       Phosphocysteine; by EIIA. {ECO:0000305}.
FT   CONFLICT      9      9       C -> E (in Ref. 5; AA sequence).
FT                                {ECO:0000305}.
FT   CONFLICT     29     29       N -> S (in Ref. 1; CAA56229).
FT                                {ECO:0000305}.
FT   CONFLICT     59     59       K -> R (in Ref. 1; CAA56229).
FT                                {ECO:0000305}.
FT   CONFLICT     76     76       I -> V (in Ref. 1; CAA56229).
FT                                {ECO:0000305}.
FT   CONFLICT     79     79       I -> V (in Ref. 1; CAA56229).
FT                                {ECO:0000305}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT         3     94       iprf:PTS_EIIB_TYPE_2 [T]
FT   MYHIT         4     84       ipfam:PTS_IIB [T]
SQ   SEQUENCE   94 AA;  10222 MW;  A8156F04894F0CD7 CRC64;
     MKRKIIVACG GAVATSTMAA EEIKELCQNH NIPVELIQCR VNEIETYMDG VHLICTTAKV
     DRSFGDIPLV HGMPFISGIG IEALQNKILT ILQG
//