PTHC_ECOLI
ID PTHC_ECOLI Reviewed; 187 AA.
AC P56579; P05705; P78102; P78214;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=PTS system glucitol/sorbitol-specific EIIC component {ECO:0000303|PubMed:3553176};
DE AltName: Full=EIIC-Gut {ECO:0000303|PubMed:3553176};
DE AltName: Full=Glucitol/sorbitol permease IIC component {ECO:0000303|PubMed:3553176};
GN Name=srlA; Synonyms=gutA, sbl; OrderedLocusNames=b2702, JW5429;
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], AND SEQUENCE REVISION.
RA Reizer J., Reizer A., Yamada M., Saier M.H. Jr.;
RT "The glucitol permease of Escherichia coli: a tripartite permease of the
RT phosphotransferase system.";
RL Microbiology 144:1463-1464(1998).
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 SEQUENCE REVISION TO 21.
RX PubMed=16397293; DOI=10.1093/nar/gkj405;
RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA Thomson N.R., Wishart D., Wanner B.L.;
RT "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT -- 2005.";
RL Nucleic Acids Res. 34:1-9(2006).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
RC STRAIN=K12;
RX PubMed=1334233; DOI=10.1038/360606a0;
RA Wang M.X., Church G.M.;
RT "A whole genome approach to in vivo DNA-protein interactions in E. coli.";
RL Nature 360:606-610(1992).
RN [8]
RP FUNCTION, 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 [9]
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).
RN [10]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(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 SrlA, SrlB and SrlE is involved in glucitol/sorbitol transport. It
CC can also use D-mannitol. {ECO:0000269|PubMed:1100608}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00430, ECO:0000305|PubMed:3553176}; Multi-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00430,
CC 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 EIIC domain forms the PTS system translocation channel and
CC contains the specific substrate-binding site. {ECO:0000255|PROSITE-
CC ProRule:PRU00430}.
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DR EMBL; J02708; AAC13411.1; -; Genomic_DNA.
DR EMBL; U00096; AAT48148.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA18886.2; -; Genomic_DNA.
DR EMBL; X70016; CAA49614.1; -; Genomic_DNA.
DR PIR; A26725; WQEC2S.
DR RefSeq; WP_000573321.1; NZ_SSZK01000017.1.
DR RefSeq; YP_026180.1; NC_000913.3.
DR AlphaFoldDB; P56579; -.
DR BioGRID; 4262078; 18.
DR BioGRID; 851891; 1.
DR ComplexPortal; CPX-5969; Glucitol/sorbitol enzyme II complex.
DR IntAct; P56579; 1.
DR STRING; 511145.b2702; -.
DR TCDB; 4.A.4.1.1; the pts glucitol (gut) family.
DR PaxDb; P56579; -.
DR PRIDE; P56579; -.
DR EnsemblBacteria; AAT48148; AAT48148; b2702.
DR EnsemblBacteria; BAA18886; BAA18886; BAA18886.
DR GeneID; 66673429; -.
DR GeneID; 947575; -.
DR KEGG; ecj:JW5429; -.
DR KEGG; eco:b2702; -.
DR PATRIC; fig|1411691.4.peg.4040; -.
DR EchoBASE; EB0962; -.
DR eggNOG; COG3730; Bacteria.
DR HOGENOM; CLU_093147_0_0_6; -.
DR InParanoid; P56579; -.
DR OMA; HINPGEY; -.
DR PhylomeDB; P56579; -.
DR BioCyc; EcoCyc:G8210-MON; -.
DR BioCyc; MetaCyc:G8210-MON; -.
DR PRO; PR:P56579; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1902495; C:transmembrane transporter complex; IC:ComplexPortal.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IDA:EcoCyc.
DR GO; GO:0015795; P:sorbitol transmembrane transport; IC:ComplexPortal.
DR InterPro; IPR004699; PTS_IID_sorb.
DR PANTHER; PTHR40399; PTHR40399; 1.
DR Pfam; PF03608; EII-GUT; 1.
DR PIRSF; PIRSF038321; PTS_glc_srb_IIC; 1.
DR TIGRFAMs; TIGR00821; EII-GUT; 1.
DR PROSITE; PS51107; PTS_EIIC_TYPE_5; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Phosphotransferase system;
KW Reference proteome; Sugar transport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..187
FT /note="PTS system glucitol/sorbitol-specific EIIC
FT component"
FT /id="PRO_0000186565"
FT TOPO_DOM 1..28
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00430"
FT TOPO_DOM 50..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00430"
FT TOPO_DOM 89..131
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00430"
FT TOPO_DOM 153..187
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1..187
FT /note="PTS EIIC type-5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00430"
SQ SEQUENCE 187 AA; 20580 MW; 86A10715BD9DE287 CRC64;
MIETITHGAE WFIGLFQKGG EVFTGMVTGI LPLLISLLVI MNALINFIGQ HRIERFAQRC
AGNPVSRYLL LPCIGTFVFC NPMTLSLGRF MPEKYKPSYY AAASYSCHSM NGLFPHINPG
ELFVYLGIAS GLTTLNLPLG PLAVSYLLVG LVTNFFRGWV TDLTTAIFEK KMGIQLEQKV
HLAGATS
