ID N9VB89_9GAMM Unreviewed; 483 AA.
AC N9VB89;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 62.
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 ORFNames=G114_07545 {ECO:0000313|EMBL:ENY72512.1};
OS Aeromonas diversa CDC 2478-85.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=1268237 {ECO:0000313|EMBL:ENY72512.1, ECO:0000313|Proteomes:UP000023775};
RN [1] {ECO:0000313|EMBL:ENY72512.1, ECO:0000313|Proteomes:UP000023775}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2478-85 {ECO:0000313|EMBL:ENY72512.1,
RC ECO:0000313|Proteomes:UP000023775};
RX PubMed=23792745; DOI=10.1128/genomeA.00330-13;
RA Farfan M., Spataro N., Sanglas A., Albarral V., Loren J.G., Bosch E.,
RA Fuste M.C.;
RT "Draft Genome Sequence of the Aeromonas diversa Type Strain.";
RL Genome Announc. 1:S69-S82(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ENY72512.1}.
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DR EMBL; APVG01000015; ENY72512.1; -; Genomic_DNA.
DR RefSeq; WP_005351032.1; NZ_CDCE01000025.1.
DR AlphaFoldDB; N9VB89; -.
DR PATRIC; fig|1268237.3.peg.1489; -.
DR eggNOG; COG1263; Bacteria.
DR eggNOG; COG1264; Bacteria.
DR OrthoDB; 7571469at2; -.
DR Proteomes; UP000023775; Unassembled WGS sequence.
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};
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 16..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 78..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 120..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 282..300
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 307..333
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 359..380
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 3..392
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000259|PROSITE:PS51103"
FT DOMAIN 405..483
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000259|PROSITE:PS51098"
FT ACT_SITE 427
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00421"
SQ SEQUENCE 483 AA; 50961 MW; 5460481FEB4C1DE6 CRC64;
MLKNAFSNLQ KVGKSLMLPV SVLPVAGILL GVGAAKFSWL PAIVSQIMEQ AGGAVFGNMA
LIFAIGVALG FTNNDGVAAL AATVGYAILT KTIGVVAPIV AGLDPAAADY AAMADKVSNV
GVLGGIVAGG IAAYMFNRFY RIQLPEYLGF FAGKRFVPII TGLAVIIAGV VMAFIWPPVG
GLIQSFSHWA AYQNPALAFG IYGIVERSLI PFGLHHIWNV PFFFEAGSYT NAAGQVFTGE
IARYIAGDPT AGNLAGGYMF KMYGLPAAAI AMWHSAKPEN RAKVGGIMVS AALTSFLTGI
TEPIEFAFLF VAPVLYAIHA LLAGSAFVVM ILLGMKHGTT FSHGLIDYVV LFSQSTKGWM
FPLVGLCYAA AYYIIFRVAI KALDLKTPGR EDATEEESVG EMAEHYMAEQ LVLAFGGKEN
IASLDACITR LRVGVKDVAK VDQAGLKKLG AAGVVVAGSG VQAIFGTKSD NLKTDMDMWM
KSH
//
