Entry bact:PTHA_ECOLI

ID   PTHA_ECOLI              Reviewed;         123 AA.
AC   P05706; P77029; Q47243; Q47244; Q57043; Q57084; Q57246;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   15-MAR-2017, entry version 143.
DE   RecName: Full=PTS system glucitol/sorbitol-specific EIIA component {ECO:0000303|PubMed:3553176};
DE            EC=2.7.1.198 {ECO:0000269|PubMed:1100608};
DE   AltName: Full=EIIA-Gut {ECO:0000303|PubMed:3553176};
DE   AltName: Full=EIII-Gut {ECO:0000303|PubMed:3553176};
DE   AltName: Full=Glucitol/sorbitol-specific phosphotransferase enzyme IIA component {ECO:0000303|PubMed:3553176};
GN   Name=srlB; Synonyms=gutB {ECO:0000303|PubMed:3553176};
GN   OrderedLocusNames=b2704, JW2673;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RX   PubMed=3553176;
RA   Yamada M., Saier M.H. Jr.;
RT   "Glucitol-specific enzymes of the phosphotransferase system in
RT   Escherichia coli. Nucleotide sequence of the gut operon.";
RL   J. Biol. Chem. 262:5455-5463(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Various ECOR strains;
RX   PubMed=1630305;
RA   Hall B.G., Sharp P.M.;
RT   "Molecular population genetics of Escherichia coli: DNA sequence
RT   diversity at the celC, crr, and gutB loci of natural isolates.";
RL   Mol. Biol. Evol. 9:654-665(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA   Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K.,
RA   Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N.,
RA   Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H.,
RA   Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S.,
RA   Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C.,
RA   Yamagata S., Horiuchi T.;
RT   "Construction of a contiguous 874-kb sequence of the Escherichia coli-
RT   K12 genome corresponding to 50.0-68.8 min on the linkage map and
RT   analysis of its sequence features.";
RL   DNA Res. 4:91-113(1997).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION
RP   TO 122.
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   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, AND 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   INDUCTION.
RX   PubMed=3062173; DOI=10.1016/0022-2836(88)90193-3;
RA   Yamada M., Saier M.H. Jr.;
RT   "Positive and negative regulators for glucitol (gut) operon expression
RT   in Escherichia coli.";
RL   J. Mol. Biol. 203:569-583(1988).
CC   -!- FUNCTION: The phosphoenolpyruvate-dependent sugar
CC       phosphotransferase system (sugar PTS), a major carbohydrate active
CC       transport system, catalyzes the phosphorylation of incoming sugar
CC       substrates concomitantly with their translocation across the cell
CC       membrane. The enzyme II complex composed of SrlA, SrlB and SrlE is
CC       involved in glucitol/sorbitol transport. It can also use D-
CC       mannitol. {ECO:0000269|PubMed:1100608}.
CC   -!- CATALYTIC ACTIVITY: [Protein]-N(pi)-phospho-L-histidine + D-
CC       sorbitol(Side 1) = [protein]-L-histidine + D-sorbitol 6-
CC       phosphate(Side 2). {ECO:0000269|PubMed:1100608}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:3553176}.
CC   -!- INDUCTION: Regulated by an unusual system which consists of the
CC       activator GutM and the repressor GutR in addition to the cAMP-CRP
CC       complex. {ECO:0000269|PubMed:3062173}.
CC   -!- DOMAIN: The EIIA domain is phosphorylated by phospho-HPr on a
CC       histidyl residue. Then, it transfers the phosphoryl group to the
CC       EIIB domain. {ECO:0000255|PROSITE-ProRule:PRU00420}.
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DR   EMBL; J02708; AAC13412.1; -; Genomic_DNA.
DR   EMBL; M93583; AAA23937.1; -; Genomic_DNA.
DR   EMBL; M93585; AAA23939.1; -; Genomic_DNA.
DR   EMBL; M93586; AAA23946.1; -; Genomic_DNA.
DR   EMBL; M93588; AAA23942.1; -; Genomic_DNA.
DR   EMBL; M93589; AAA23938.1; -; Genomic_DNA.
DR   EMBL; M93590; AAA23940.1; -; Genomic_DNA.
DR   EMBL; M93599; AAA23941.1; -; Genomic_DNA.
DR   EMBL; M93600; AAA23943.1; -; Genomic_DNA.
DR   EMBL; M93601; AAA23944.1; -; Genomic_DNA.
DR   EMBL; M93602; AAA23945.1; -; Genomic_DNA.
DR   EMBL; M93603; AAA23947.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75746.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA16565.2; -; Genomic_DNA.
DR   PIR; B26725; WQEC3S.
DR   RefSeq; NP_417184.1; NC_000913.3.
DR   RefSeq; WP_000216194.1; NZ_LN832404.1.
DR   ProteinModelPortal; P05706; -.
DR   SMR; P05706; -.
DR   BioGrid; 4259356; 11.
DR   IntAct; P05706; 3.
DR   STRING; 511145.b2704; -.
DR   TCDB; 4.A.4.1.1; the pts glucitol (gut) family.
DR   PaxDb; P05706; -.
DR   PRIDE; P05706; -.
DR   EnsemblBacteria; AAC75746; AAC75746; b2704.
DR   EnsemblBacteria; BAA16565; BAA16565; BAA16565.
DR   GeneID; 948971; -.
DR   KEGG; ecj:JW2673; -.
DR   KEGG; eco:b2704; -.
DR   PATRIC; 32120806; VBIEscCol129921_2795.
DR   EchoBASE; EB0963; -.
DR   EcoGene; EG10970; srlB.
DR   eggNOG; ENOG4105VI0; Bacteria.
DR   eggNOG; COG3731; LUCA.
DR   InParanoid; P05706; -.
DR   KO; K02781; -.
DR   OMA; YQTTITH; -.
DR   PhylomeDB; P05706; -.
DR   BioCyc; EcoCyc:GUTB-MONOMER; -.
DR   BioCyc; MetaCyc:GUTB-MONOMER; -.
DR   PRO; PR:P05706; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016301; F:kinase activity; IMP:EcoCyc.
DR   GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IDA:UniProtKB.
DR   GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IDA:UniProtKB.
DR   Gene3D; 2.40.33.40; -; 1.
DR   InterPro; IPR004716; PTS_IIA_glucitol/sorbitol-sp.
DR   InterPro; IPR018454; PTS_IIA_glucitol/sorbitol_sub.
DR   PANTHER; PTHR40398; PTHR40398; 1.
DR   Pfam; PF03829; PTSIIA_gutA; 1.
DR   ProDom; PD015842; PTS_IIA_glucitol/sorbitol-sp; 1.
DR   SUPFAM; SSF141530; SSF141530; 1.
DR   TIGRFAMs; TIGR00849; gutA; 1.
DR   PROSITE; PS51097; PTS_EIIA_TYPE_5; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; Kinase; Phosphoprotein;
KW   Phosphotransferase system; Reference proteome; Sugar transport;
KW   Transferase; Transport.
FT   CHAIN         1    123       PTS system glucitol/sorbitol-specific
FT                                EIIA component.
FT                                /FTId=PRO_0000186568.
FT   DOMAIN        3    116       PTS EIIA type-5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00420}.
FT   ACT_SITE     43     43       Tele-phosphohistidine intermediate.
FT                                {ECO:0000305}.
FT   MOD_RES      43     43       Phosphohistidine; by HPr.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00420}.
FT   VARIANT      17     17       I -> T (in strain: ECOR 6, ECOR 28, ECOR
FT                                35, ECOR 37, ECOR 51, ECOR 58, ECOR 61,
FT                                ECOR 66 and ECOR 69).
FT   VARIANT      51     51       A -> E (in strain: ECOR 58).
FT   VARIANT      59     59       S -> T (in strain: ECOR 28, ECOR 37, ECOR
FT                                58 and ECOR 69).
FT   VARIANT      62     62       Q -> R (in strain: ECOR 51).
FT   VARIANT      92     92       N -> S (in strain: ECOR 51, ECOR 61 and
FT                                ECOR 66).
FT   CONFLICT    122    122       K -> T (in Ref. 3). {ECO:0000305}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT         3    116       iprf:PTS_EIIA_TYPE_5 [T]
FT   MYHIT         4    115       ipfam:PTSIIA_gutA [T]
SQ   SEQUENCE   123 AA;  13304 MW;  3BB3A2AA2399EDE4 CRC64;
     MTVIYQTTIT RIGASAIDAL SDQMLITFRE GAPADLEEYC FIHCHGELKG ALHPGLQFSL
     GQHRYPVTAV GSVAEDNLRE LGHVTLRFDG LNEAEFPGTV HVAGPVPDDI APGSVLKFES
     VKE
//