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Database: UniProt
Entry: A7GKX4_BACCN
LinkDB: A7GKX4_BACCN
Original site: A7GKX4_BACCN 
ID   A7GKX4_BACCN            Unreviewed;       497 AA.
AC   A7GKX4;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   SubName: Full=PTS system, N-acetylglucosamine-specific IIBC subunit {ECO:0000313|EMBL:ABS20782.1};
GN   OrderedLocusNames=Bcer98_0427 {ECO:0000313|EMBL:ABS20782.1};
OS   Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315749 {ECO:0000313|EMBL:ABS20782.1, ECO:0000313|Proteomes:UP000002300};
RN   [1] {ECO:0000313|EMBL:ABS20782.1, ECO:0000313|Proteomes:UP000002300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98
RC   {ECO:0000313|Proteomes:UP000002300};
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA   Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP000764; ABS20782.1; -; Genomic_DNA.
DR   RefSeq; WP_011983539.1; NC_009674.1.
DR   AlphaFoldDB; A7GKX4; -.
DR   STRING; 315749.Bcer98_0427; -.
DR   GeneID; 56415979; -.
DR   KEGG; bcy:Bcer98_0427; -.
DR   eggNOG; COG1263; Bacteria.
DR   eggNOG; COG1264; Bacteria.
DR   HOGENOM; CLU_012312_1_0_9; -.
DR   OrthoDB; 9764327at2; -.
DR   Proteomes; UP000002300; Chromosome.
DR   GO; GO:0019866; C:organelle inner membrane; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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; 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; IPR010974; PTS_IIBC_nag.
DR   NCBIfam; TIGR00826; EIIB_glc; 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; 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        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        50..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        133..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        171..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        200..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        271..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        321..343
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        375..395
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..407
FT                   /note="PTS EIIC type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51103"
FT   DOMAIN          421..497
FT                   /note="PTS EIIB type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51098"
FT   ACT_SITE        443
FT                   /note="Phosphocysteine intermediate; for EIIB activity"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00421"
SQ   SEQUENCE   497 AA;  52692 MW;  816EFDED508BFACE CRC64;
     MLQFLQRIGK ALMLPIAVLP AAGLLLRLGQ PDVFDIPVMA QAGAAIFDNL ALIFAIGVAI
     GLSVDGSGAA GLAGAIGYLV MKNTTNTLSV SYSTAELNDK LKSVQDLLGS VDPSKLADTM
     TKVSKAAALT PKINMAILGG IIAGIVAGLL YNKFHKIKLP EWLGFFAGKR FVPIITSVVM
     LLLGLVFGQI WPTIQSGIDA VAHGIVNLGS IGSGLFGLLN RLLIPIGLHH VMNTYFWFVL
     GDFTNAAGDI VHGDIARFFA KDPSAGMFMT GFFPVMMFGL PAACFAMIAA AKPEKRKMVT
     GMLAGLALTS FLTGITEPIE FSFMFLSPVL YGIHAVLTGI SLFVTTSLGI HDGFSFSAGA
     IDYFLNFGIA TKPLLLAGIG LIYAAIYFVV FYFLIKKFNL KTPGREDDEE LATDDEAPVA
     GSIGEAYVTA LGGKDNLTVI DNCATRLRLQ VKDANLVNES ALKRAGARGV MKLSNTSVQV
     IVGTNVESVA EDMKKHV
//
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