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Database: UniProt
Entry: A0A135L6S6_9BACI
LinkDB: A0A135L6S6_9BACI
Original site: A0A135L6S6_9BACI 
ID   A0A135L6S6_9BACI        Unreviewed;       679 AA.
AC   A0A135L6S6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   13-SEP-2023, entry version 28.
DE   SubName: Full=PTS glucose transporter subunit IICBA {ECO:0000313|EMBL:KXG44714.1};
GN   ORFNames=U473_12290 {ECO:0000313|EMBL:KXG44714.1};
OS   Tepidibacillus decaturensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Tepidibacillus.
OX   NCBI_TaxID=1413211 {ECO:0000313|EMBL:KXG44714.1, ECO:0000313|Proteomes:UP000070352};
RN   [1] {ECO:0000313|EMBL:KXG44714.1, ECO:0000313|Proteomes:UP000070352}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Z9 {ECO:0000313|EMBL:KXG44714.1,
RC   ECO:0000313|Proteomes:UP000070352};
RA   Dong Y., Chang J.Y., Sanford R., Fouke B.W.;
RT   "Draft Genome for Tepidibacillus decaturensis nov. sp. Strain Z9, an
RT   Anaerobic, Moderately Thermophilic and Heterotrophic Bacterium from Deep
RT   Subsurface of the Illinois Basin, USA.";
RL   Submitted (FEB-2016) 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:KXG44714.1}.
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DR   EMBL; LSKU01000001; KXG44714.1; -; Genomic_DNA.
DR   RefSeq; WP_068726769.1; NZ_LSKU01000001.1.
DR   AlphaFoldDB; A0A135L6S6; -.
DR   STRING; 1413211.U473_12290; -.
DR   OrthoDB; 9764327at2; -.
DR   Proteomes; UP000070352; 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; 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; IPR011299; PTS_IIBC_glc.
DR   NCBIfam; TIGR00826; EIIB_glc; 1.
DR   NCBIfam; TIGR00830; PTBA; 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; 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:UP000070352};
KW   Sugar transport {ECO:0000256|ARBA:ARBA00022597,
KW   ECO:0000313|EMBL:KXG44714.1}; 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        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        63..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        89..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        123..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        210..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        277..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        302..319
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        325..349
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        356..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        379..401
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          3..413
FT                   /note="PTS EIIC type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51103"
FT   DOMAIN          425..506
FT                   /note="PTS EIIB type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51098"
FT   DOMAIN          547..651
FT                   /note="PTS EIIA type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51093"
FT   ACT_SITE        447
FT                   /note="Phosphocysteine intermediate; for EIIB activity"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00421"
SQ   SEQUENCE   679 AA;  73293 MW;  E412494DFC2F975F CRC64;
     MFKKIFGILQ QVGKSLMLPV AILPAAGILL AFGNAFQNPA LVQRLTFLSN PTFQLVAKVM
     EEAGGIIFGN LSLLFAVGVA VGLAGGEGVA GLAAIIGFLI MNITMGVILG VTPDMVAADK
     SYAMVVGIPT LQTGVFGGII VGILASYLYK KYYNIELPQF LGFFAGKRFV PIVTAGSALL
     LGILMIFIWP PIQHALNTFS YSMIDTNRTL AAFIFGLIER SLIPFGLHHI FYSPFWFEFG
     EYVNKAGQVI RGDQSIFFAQ LKDGVPLTAG TFMTGKFPFM MFGLPAAALA MYHEARPEKR
     KLVGGILASA ALTSFLTGIT EPIEFTFLFV APALFAVHAV FAGLSFMIMH ILNVKIGMTF
     SGGVIDYILF GVLPNRTNWW LVIPVGLVFS VIYYFGFRFA IRTWNLRTPG RELDEEQVQG
     TEKAGNLAVG VLKGLGGKEN IANLDACITR LRVSVHDISK VNKDLLKQLG AAGVLEVGNN
     IQAIFGPKSD QLKEQIKAVI NGKSPEEIKD VKATPSTTSD IETVIDGVEF IVAPLTGEVI
     DITEVPDQVF AGKMMGDGFA MKPEKGEIVS PIKGKVVNAF PTKHAIGLVS HSGLEVLIHV
     GIDTVKLEGK GFELLVNEGD EVEVGTSLLK VDLPYIEKHA TSTITPIVFT NLQENQVLKV
     NKGKAVAKET EVAIIDKKD
//
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