ID Q6LRA9_PHOPR Unreviewed; 462 AA.
AC Q6LRA9;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 122.
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 Name=Y1767 {ECO:0000313|EMBL:CAG20167.1};
GN OrderedLocusNames=PBPRA1760 {ECO:0000313|EMBL:CAG20167.1};
OS Photobacterium profundum (strain SS9).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=298386 {ECO:0000313|EMBL:CAG20167.1, ECO:0000313|Proteomes:UP000000593};
RN [1] {ECO:0000313|Proteomes:UP000000593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1253 / SS9 {ECO:0000313|Proteomes:UP000000593};
RX PubMed=15746425; DOI=10.1126/science.1103341;
RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA Bartlett D.H., Valle G.;
RT "Life at depth: Photobacterium profundum genome sequence and expression
RT analysis.";
RL Science 307:1459-1461(2005).
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; CR378668; CAG20167.1; -; Genomic_DNA.
DR RefSeq; WP_011218475.1; NC_006370.1.
DR AlphaFoldDB; Q6LRA9; -.
DR SMR; Q6LRA9; -.
DR STRING; 298386.PBPRA1760; -.
DR KEGG; ppr:PBPRA1760; -.
DR eggNOG; COG1263; Bacteria.
DR eggNOG; COG1264; Bacteria.
DR HOGENOM; CLU_012312_1_0_6; -.
DR Proteomes; UP000000593; Chromosome 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000000593};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
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 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 92..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 240..258
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 264..282
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 289..317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 341..362
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..374
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000259|PROSITE:PS51103"
FT DOMAIN 387..462
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000259|PROSITE:PS51098"
FT ACT_SITE 409
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00421"
SQ SEQUENCE 462 AA; 48918 MW; 280F9864B614D54F CRC64;
MNIFSTMQKM GRSLMLPVAC MPAAGILLGI GGNSEVAKFL PDIVAQIMTE AGLGVFANMA
LLFAIGVALG FTKNDGVAAL AATLGYLTMT RVLGVVAEGT DTGVFGGVIM GLVAAQLFNK
YHDIKLPTYL GFFGGKRFVP IVTSLAACVV AAALALIWQP IGAGIAAFSE WAAYQSPEVA
FGIYGIVERS LIPFGLHHIW NAPFFYEVGE FTTAAGEVVK GEIPRYLAGD PTAGNLAGGY
MFKMFGLPAA CLAMYVTAKK ENKLMVASIL GSAALTSFLT GITEPIEFAF LFVAPVLYVA
HALLAGSAFV VMILLGIKHG TTFSHGLFDF TLLFGQSTNG WLLPVIGLVY AVIYFLVFVT
LIKALDLKTP GREDKEEMSV AVNTSKDGLA QDIAMAFGGK ENIKDLEACI TRLRVTVFDS
SKVDIPRLKA LGAAGVFAKG DNYQAVFGTH SEIIKGQIEV LA
//
