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 03-AUG-2022, entry version 168.
DE RecName: Full=PTS system glucitol/sorbitol-specific EIIA component {ECO:0000303|PubMed:3553176};
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; DOI=10.1016/s0021-9258(18)45594-9;
RA Yamada M., Saier M.H. Jr.;
RT "Glucitol-specific enzymes of the phosphotransferase system in Escherichia
RT 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; DOI=10.1093/oxfordjournals.molbev.a040751;
RA Hall B.G., Sharp P.M.;
RT "Molecular population genetics of Escherichia coli: DNA sequence diversity
RT 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., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT 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., Mau B.,
RA 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 TO
RP 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 MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE 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 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 in
RT Escherichia coli.";
RL J. Mol. Biol. 203:569-583(1988).
CC -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC system (sugar PTS), a major carbohydrate active transport system,
CC catalyzes the phosphorylation of incoming sugar substrates
CC concomitantly with their translocation across the cell membrane. The
CC enzyme II complex composed of SrlA, SrlB and SrlE is involved in
CC glucitol/sorbitol transport. It can also use D-mannitol.
CC {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 histidyl
CC residue. Then, it transfers the phosphoryl group to the EIIB domain.
CC {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 AlphaFoldDB; P05706; -.
DR SMR; P05706; -.
DR BioGRID; 4259356; 14.
DR ComplexPortal; CPX-5969; Glucitol/sorbitol enzyme II complex.
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; fig|1411691.4.peg.4038; -.
DR EchoBASE; EB0963; -.
DR eggNOG; COG3731; Bacteria.
DR HOGENOM; CLU_138435_2_1_6; -.
DR InParanoid; P05706; -.
DR OMA; MLITFKQ; -.
DR PhylomeDB; P05706; -.
DR BioCyc; EcoCyc:GUTB-MON; -.
DR BioCyc; MetaCyc:GUTB-MON; -.
DR PRO; PR:P05706; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1902495; C:transmembrane transporter complex; IC:ComplexPortal.
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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0015795; P:sorbitol transmembrane transport; IC:ComplexPortal.
DR Gene3D; 2.40.33.40; -; 1.
DR InterPro; IPR004716; PTS_IIA_glucitol/sorbitol-sp.
DR InterPro; IPR036665; PTS_IIA_glucitol/sorbitol_sf.
DR InterPro; IPR018454; PTS_IIA_glucitol/sorbitol_sub.
DR PANTHER; PTHR40398; PTHR40398; 1.
DR Pfam; PF03829; PTSIIA_gutA; 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 Cytoplasm; Kinase; Phosphoprotein; Phosphotransferase system;
KW Reference proteome; Sugar transport; Transferase; Transport.
FT CHAIN 1..123
FT /note="PTS system glucitol/sorbitol-specific EIIA
FT component"
FT /id="PRO_0000186568"
FT DOMAIN 3..116
FT /note="PTS EIIA type-5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00420"
FT ACT_SITE 43
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000305"
FT MOD_RES 43
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00420"
FT VARIANT 17
FT /note="I -> T (in strain: ECOR 6, ECOR 28, ECOR 35, ECOR
FT 37, ECOR 51, ECOR 58, ECOR 61, ECOR 66 and ECOR 69)"
FT VARIANT 51
FT /note="A -> E (in strain: ECOR 58)"
FT VARIANT 59
FT /note="S -> T (in strain: ECOR 28, ECOR 37, ECOR 58 and
FT ECOR 69)"
FT VARIANT 62
FT /note="Q -> R (in strain: ECOR 51)"
FT VARIANT 92
FT /note="N -> S (in strain: ECOR 51, ECOR 61 and ECOR 66)"
FT CONFLICT 122
FT /note="K -> T (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 123 AA; 13304 MW; 3BB3A2AA2399EDE4 CRC64;
MTVIYQTTIT RIGASAIDAL SDQMLITFRE GAPADLEEYC FIHCHGELKG ALHPGLQFSL
GQHRYPVTAV GSVAEDNLRE LGHVTLRFDG LNEAEFPGTV HVAGPVPDDI APGSVLKFES
VKE
