ID   Q1R498_ECOUT            Unreviewed;       502 AA.
AC   Q1R498;
DT   16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 118.
DE   RecName: Full=PTS system glucose-specific EIICB component {ECO:0000256|ARBA:ARBA00021468};
DE            EC=2.7.1.199 {ECO:0000256|ARBA:ARBA00011910};
DE   AltName: Full=EIICB-Glc {ECO:0000256|ARBA:ARBA00032303};
GN   OrderedLocusNames=UTI89_C4399 {ECO:0000313|EMBL:ABE09816.1};
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106 {ECO:0000313|EMBL:ABE09816.1, ECO:0000313|Proteomes:UP000001952};
RN   [1] {ECO:0000313|EMBL:ABE09816.1, ECO:0000313|Proteomes:UP000001952}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC {ECO:0000313|Proteomes:UP000001952};
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glucose(out) + N(pros)-phospho-L-histidyl-[protein] = D-
CC         glucose 6-phosphate(in) + L-histidyl-[protein]; Xref=Rhea:RHEA:33367,
CC         Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746, ChEBI:CHEBI:4167,
CC         ChEBI:CHEBI:29979, ChEBI:CHEBI:61548, ChEBI:CHEBI:64837;
CC         EC=2.7.1.199; Evidence={ECO:0000256|ARBA:ARBA00001289};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP000243; ABE09816.1; -; Genomic_DNA.
DR   RefSeq; WP_000037973.1; NZ_CP064825.1.
DR   AlphaFoldDB; Q1R498; -.
DR   SMR; Q1R498; -.
DR   KEGG; eci:UTI89_C4399; -.
DR   HOGENOM; CLU_012312_1_0_6; -.
DR   Proteomes; UP000001952; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005355; F:glucose transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00212; PTS_IIB_glc; 1.
DR   Gene3D; 3.30.1360.60; Glucose permease domain IIB; 1.
DR   InterPro; IPR036878; Glu_permease_IIB.
DR   InterPro; IPR018113; PTrfase_EIIB_Cys.
DR   InterPro; IPR003352; PTS_EIIC.
DR   InterPro; IPR013013; PTS_EIIC_1.
DR   InterPro; IPR001996; PTS_IIB_1.
DR   InterPro; IPR011299; PTS_IIBC_glc.
DR   NCBIfam; TIGR00826; EIIB_glc; 1.
DR   NCBIfam; TIGR02002; PTS-II-BC-glcB; 1.
DR   PANTHER; PTHR30009; CYTOCHROME C-TYPE SYNTHESIS PROTEIN AND PTS TRANSMEMBRANE COMPONENT; 1.
DR   PANTHER; PTHR30009:SF20; PTS SYSTEM GLUCOSE-SPECIFIC EIICB COMPONENT-RELATED; 1.
DR   Pfam; PF00367; PTS_EIIB; 1.
DR   Pfam; PF02378; PTS_EIIC; 1.
DR   SUPFAM; SSF55604; Glucose permease domain IIB; 1.
DR   PROSITE; PS51098; PTS_EIIB_TYPE_1; 1.
DR   PROSITE; PS01035; PTS_EIIB_TYPE_1_CYS; 1.
DR   PROSITE; PS51103; PTS_EIIC_TYPE_1; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphotransferase system {ECO:0000256|ARBA:ARBA00022683};
KW   Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABE09816.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        21..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        45..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        76..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        108..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        155..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        254..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        288..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        312..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        343..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        366..388
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          8..400
FT                   /note="PTS EIIC type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51103"
FT   DOMAIN          412..494
FT                   /note="PTS EIIB type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51098"
FT   ACT_SITE        434
FT                   /note="Phosphocysteine intermediate; for EIIB activity"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00421"
SQ   SEQUENCE   502 AA;  54520 MW;  479BCB7EBDE8AC13 CRC64;
     MSKKITSLFN FKKLQKFSSA LMLPIAILPA AGLILAIGIS FNIELLANCG GLIFANLPLL
     FCVGIVIGLT GDGSSSLSAI ISYMIMNATM GTQLGITAES VAASNGDYAM ILGVPTLQTG
     VFGGLIVAIF VYLLYTRFHN IELPQFLGFF GGKRFVPIIT AVAAIIVGYL LPWLWIPVQK
     GLASLSTLVT SGHNANFAAF IYAVGERSLI PFGLHHIWNV PFYYNFGDYM TKSGQLVTGD
     IPVFFAQLRD GVPLTAGLFM TGRFPIMMFA LPAAALAMYQ EAKPERKALI KGLLLSGALT
     TFVTGITEPL EYAFLFAAPV LYIIHIFLYA TSFVLMNILN VHIGHPFAGG LIDFVLNGVM
     PNRTPWYLVF LAGAGYAAIY YTVFRVLIRK LNLKTPGRED EEIAVATTLT REERPYQIIE
     AVGGFDNIED VDACATRLRL ALVDDKKVNE KRLKELGAAG LVKLGDGGVQ VIFGGKSQIL
     RDEIKTVMSR PRPTEMTVAC AN
//