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Database: UniProt
Entry: A0A3E2N8C1_9CLOT
LinkDB: A0A3E2N8C1_9CLOT
Original site: A0A3E2N8C1_9CLOT 
ID   A0A3E2N8C1_9CLOT        Unreviewed;       487 AA.
AC   A0A3E2N8C1;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=PTS glucose transporter subunit IIBC {ECO:0000313|EMBL:RFZ77160.1};
GN   ORFNames=DS742_20215 {ECO:0000313|EMBL:RFZ77160.1};
OS   Clostridium indicum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=759821 {ECO:0000313|EMBL:RFZ77160.1, ECO:0000313|Proteomes:UP000260680};
RN   [1] {ECO:0000313|EMBL:RFZ77160.1, ECO:0000313|Proteomes:UP000260680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PI-S10-A1B {ECO:0000313|EMBL:RFZ77160.1,
RC   ECO:0000313|Proteomes:UP000260680};
RA   Krishna G., Summeta K., Shikha S., Prabhu P.B., Suresh K.;
RT   "New species, Clostridium PI-S10-A1B.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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:RFZ77160.1}.
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DR   EMBL; QOHO01000067; RFZ77160.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3E2N8C1; -.
DR   OrthoDB; 9764327at2; -.
DR   Proteomes; UP000260680; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000260680};
KW   Sugar transport {ECO:0000256|ARBA:ARBA00022597,
KW   ECO:0000313|EMBL:RFZ77160.1}; 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..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        44..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        86..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        122..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        160..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        185..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        219..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        251..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        282..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        305..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        361..381
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..393
FT                   /note="PTS EIIC type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51103"
FT   DOMAIN          410..487
FT                   /note="PTS EIIB type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51098"
FT   ACT_SITE        432
FT                   /note="Phosphocysteine intermediate; for EIIB activity"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00421"
SQ   SEQUENCE   487 AA;  52059 MW;  A1429DBD8D74DD1D CRC64;
     MKYLQKLGKS LMLPVACLPA AGILMGIGYW IAPSIISGQG TATGVWSVIA VFLIKAGAAI
     IDNLPILFAV GVGIGMSDDQ EGTSALAALV SWLMITTILS TGTVALLFKI DASQVNPAFG
     KIANPCIGII SGLIGANCYN KFKKTKLPDA LAFFSGKRSV AIVTALSSLV VSIVLLFVWP
     AIYSAIVAFG EMILSLGPVG AGLYGFFNRL LIPLGLHHAL NAVFWFDLAG VNDIGKFWGT
     AEGGILGQTG QYMSGFFPVM MFGLPAATLA MYHTAKPGKK KMVYGLFFSA ALCSFFTGIT
     EPIEFAFMFL APGLYLIHAA LTAISMTIIA ILPVRAGFFF SAGFVDWFLS FKAPFAENSW
     LLIPIGIVYG AVYYIIFRLA IPLFNFKTPG REEDDEVNES TVTLANNDYT AVASIILEGL
     GGKENITSID ACITRLRLEI ADYTKVNEKK IKSSGVAGVI RPGKNSVQVV VGTQVQHVAD
     EFKKLCK
//
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