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Database: UniProt
Entry: D8MPP5_ERWBE
LinkDB: D8MPP5_ERWBE
Original site: D8MPP5_ERWBE 
ID   D8MPP5_ERWBE            Unreviewed;       668 AA.
AC   D8MPP5;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 76.
DE   SubName: Full=PTS system, glucose-specific IIBC component {ECO:0000313|EMBL:CAX58802.1};
DE            EC=2.7.1.69 {ECO:0000313|EMBL:CAX58802.1};
GN   Name=ptsG {ECO:0000313|EMBL:CAX58802.1};
GN   OrderedLocusNames=EbC_12710 {ECO:0000313|EMBL:CAX58802.1};
OS   Erwinia billingiae (strain Eb661).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=634500 {ECO:0000313|Proteomes:UP000008793};
RN   [1] {ECO:0000313|EMBL:CAX58802.1, ECO:0000313|Proteomes:UP000008793}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Eb661 {ECO:0000313|EMBL:CAX58802.1,
RC   ECO:0000313|Proteomes:UP000008793};
RX   PubMed=20565991; DOI=10.1186/1471-2164-11-393;
RA   Kube M., Migdoll A.M., Gehring I., Heitmann K., Mayer Y., Kuhl H.,
RA   Knaust F., Geider K., Reinhardt R.;
RT   "Genome comparison of the epiphytic bacteria Erwinia billingiae and E.
RT   tasmaniensis with the pear pathogen E. pyrifoliae.";
RL   BMC Genomics 11:393-393(2010).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; FP236843; CAX58802.1; -; Genomic_DNA.
DR   AlphaFoldDB; D8MPP5; -.
DR   STRING; 634500.EbC_12710; -.
DR   KEGG; ebi:EbC_12710; -.
DR   eggNOG; COG1263; Bacteria.
DR   eggNOG; COG1264; Bacteria.
DR   eggNOG; COG2190; Bacteria.
DR   HOGENOM; CLU_012312_1_3_6; -.
DR   OMA; IVHCARP; -.
DR   Proteomes; UP000008793; Chromosome.
DR   GO; GO:0019866; C:organelle inner membrane; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0103111; F:D-glucosamine PTS permease activity; IEA:UniProtKB-EC.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015572; F:N-acetylglucosamine transmembrane transporter activity; IEA:InterPro.
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; cd00210; PTS_IIA_glc; 1.
DR   CDD; cd00212; PTS_IIB_glc; 1.
DR   Gene3D; 2.70.70.10; Glucose Permease (Domain IIA); 1.
DR   Gene3D; 3.30.1360.60; Glucose permease domain IIB; 1.
DR   InterPro; IPR011055; Dup_hybrid_motif.
DR   InterPro; IPR036878; Glu_permease_IIB.
DR   InterPro; IPR018113; PTrfase_EIIB_Cys.
DR   InterPro; IPR001127; PTS_EIIA_1_perm.
DR   InterPro; IPR003352; PTS_EIIC.
DR   InterPro; IPR013013; PTS_EIIC_1.
DR   InterPro; IPR001996; PTS_IIB_1.
DR   InterPro; IPR010974; PTS_IIBC_nag.
DR   NCBIfam; TIGR00826; EIIB_glc; 1.
DR   NCBIfam; TIGR00830; PTBA; 1.
DR   NCBIfam; TIGR01998; PTS-II-BC-nag; 1.
DR   PANTHER; PTHR30009; CYTOCHROME C-TYPE SYNTHESIS PROTEIN AND PTS TRANSMEMBRANE COMPONENT; 1.
DR   PANTHER; PTHR30009:SF4; PTS SYSTEM N-ACETYLGLUCOSAMINE-SPECIFIC EIICBA COMPONENT; 1.
DR   Pfam; PF00358; PTS_EIIA_1; 1.
DR   Pfam; PF00367; PTS_EIIB; 1.
DR   Pfam; PF02378; PTS_EIIC; 1.
DR   SUPFAM; SSF51261; Duplicated hybrid motif; 1.
DR   SUPFAM; SSF55604; Glucose permease domain IIB; 1.
DR   PROSITE; PS51093; PTS_EIIA_TYPE_1; 1.
DR   PROSITE; PS00371; PTS_EIIA_TYPE_1_HIS; 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:UP000008793};
KW   Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CAX58802.1};
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        32..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        56..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        112..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        150..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        250..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        277..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        300..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        355..377
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          19..389
FT                   /note="PTS EIIC type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51103"
FT   DOMAIN          408..490
FT                   /note="PTS EIIB type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51098"
FT   DOMAIN          537..641
FT                   /note="PTS EIIA type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51093"
FT   ACT_SITE        430
FT                   /note="Phosphocysteine intermediate; for EIIB activity"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00421"
SQ   SEQUENCE   668 AA;  70221 MW;  51E11C5F2E440D15 CRC64;
     MIKTENGYLR LADLKGGNVN ILGFFQRLGR SLQLPIAVLP VAALMLRFGQ PDLLNMPFIA
     QGGGAIFDNL ALIFAIGVAS TWSKDNAGAA ALAGAVGYFI LTKSMVTINP AINMGVLAGI
     ITGLVAGATY NRWSDIKLPD FLSFFGGRRF VPIATGFFCL ILAAVFGYIW PPVQAAIHAG
     GEWIVSEGAF GAGVFGFVNR LLIPTGLHQV LNTIAWFQIG EFHNAAGAVF HGDINRFYAG
     DGTAGMFMSG FFPIMMFGLP GAALAMYLAA PKERRPMVGG MLLSVAITAF LTGVTEPLEF
     LFMFLAPMLY LIHALLTGIS LYIATALGIH AGFSFSAGAI DYALMYNLPA ASKNVWMLLV
     MGVVAFGIYF VLFTAVIRMF NLKTPGREDA SADVVDSEAN SNTEEGLNQL SQQYIAAIGG
     SDNLQIIDAC ITRLRLSVKD AGLVNDAACK RLGASGIVKL NKQTVQVIVG AKAESIAEVM
     KKLIAKGPIA AWSSTTAPAP QAVKVAPQAV PNAPKGIIAT LVAPVSGEVV ALEQVPDEAF
     ASKAVGDGLA IRPTSSTVLS PAAGTVVKIF NTNHAFCLET ENGAEIVVHM GLDTVGLEGK
     GFTRLVEEGA QVTAGQPVLE MDLAFLNANA RSMISPVVVS NIDDYSGITL VAGQTVVAGE
     SRLFDING
//
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