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Database: UniProt
Entry: W1SDK5_9BACI
LinkDB: W1SDK5_9BACI
Original site: W1SDK5_9BACI 
ID   W1SDK5_9BACI            Unreviewed;       453 AA.
AC   W1SDK5;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   SubName: Full=PTS system sucrose-specific transporter subunit IIBC {ECO:0000313|EMBL:ETI66119.1};
GN   ORFNames=BAVI_24268 {ECO:0000313|EMBL:ETI66119.1};
OS   Neobacillus vireti LMG 21834.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX   NCBI_TaxID=1131730 {ECO:0000313|EMBL:ETI66119.1, ECO:0000313|Proteomes:UP000018877};
RN   [1] {ECO:0000313|EMBL:ETI66119.1, ECO:0000313|Proteomes:UP000018877}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21834 {ECO:0000313|EMBL:ETI66119.1,
RC   ECO:0000313|Proteomes:UP000018877};
RX   PubMed=24708037; DOI=10.1111/1462-2920.12478;
RA   Mania D., Heylen K., van Spanning R.J., Frostegard A.;
RT   "The nitrate-ammonifying and nosZ-carrying bacterium Bacillus vireti is a
RT   potent source and sink for nitric and nitrous oxide under high nitrate
RT   conditions.";
RL   Environ. Microbiol. 16:3196-3210(2014).
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:ETI66119.1}.
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DR   EMBL; ALAN01000180; ETI66119.1; -; Genomic_DNA.
DR   RefSeq; WP_024031007.1; NZ_ALAN01000180.1.
DR   AlphaFoldDB; W1SDK5; -.
DR   STRING; 220686.AA980_18900; -.
DR   PATRIC; fig|1131730.3.peg.5068; -.
DR   eggNOG; COG1263; Bacteria.
DR   eggNOG; COG1264; Bacteria.
DR   OrthoDB; 9769191at2; -.
DR   Proteomes; UP000018877; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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   PANTHER; PTHR30175; PHOSPHOTRANSFERASE SYSTEM TRANSPORT PROTEIN; 1.
DR   PANTHER; PTHR30175:SF3; PTS SYSTEM N-ACETYLMURAMIC ACID-SPECIFIC EIIBC 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; 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:UP000018877};
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        119..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        153..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        185..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        211..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        240..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        282..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        323..342
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        354..375
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        396..416
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        422..443
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          6..88
FT                   /note="PTS EIIB type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51098"
FT   DOMAIN          114..453
FT                   /note="PTS EIIC type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51103"
FT   ACT_SITE        28
FT                   /note="Phosphocysteine intermediate; for EIIB activity"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00421"
SQ   SEQUENCE   453 AA;  46708 MW;  B40FC34BEA7B0244 CRC64;
     MAGENKILAE KILEQLGGPA NIGNYTHCMT RLRVTPNDES KVNKAAIKKI DGVLGVVEEE
     TLQIILGPGK VNRVTEEFGK LVDAAGGIDL KAKAASNKAE INKKNATPFK LFLRKISSIF
     IPLIPALVAS GLITGITKAI IQAGWLAGDS QLATILTVIG GGLFGYLGIL VGINAAKEFG
     GSPALGALAG ILIINPAVAG IKLFGADLLP GRGGLIGVLF AAIFIALVEK RVRKFVPQSL
     DLFITPTVAL LVTGIVTYLV FMPLGGLVSD AITKGLTSLL DMGGVVAGFV LGATFLPLVV
     TGLHQGLTPI HLELINSTGI DPLLPILAMG GAGQVGAAFA IYFKTKKTRL KRAIGGGLPA
     GILGIGEPLI FGVTLPLGRP FLTACLGAGV GGAFQAAFKI ATTAIGVSGL PLAFLVVTGQ
     VLLYLLGVLI AYAAGFLFTY LFGFKDDMAG EFE
//
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