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Database: UniProt
Entry: A0A1X7MWL8_9LACT
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Original site: A0A1X7MWL8_9LACT 
ID   A0A1X7MWL8_9LACT        Unreviewed;       638 AA.
AC   A0A1X7MWL8;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=PTS system beta-glucoside-specific IIA component, Glc family /PTS system beta-glucoside-specific IIB component, Glc family /PTS system beta-glucoside-specific IIC component, Glc family {ECO:0000313|EMBL:SMH28453.1};
GN   ORFNames=SAMN04488700_0915 {ECO:0000313|EMBL:SMH28453.1};
OS   Carnobacterium iners.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Carnobacterium.
OX   NCBI_TaxID=1073423 {ECO:0000313|EMBL:SMH28453.1, ECO:0000313|Proteomes:UP000193435};
RN   [1] {ECO:0000313|EMBL:SMH28453.1, ECO:0000313|Proteomes:UP000193435}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG26642 {ECO:0000313|EMBL:SMH28453.1,
RC   ECO:0000313|Proteomes:UP000193435};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; FXBJ01000002; SMH28453.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X7MWL8; -.
DR   STRING; 1073423.SAMN04488700_0915; -.
DR   OrthoDB; 9769191at2; -.
DR   Proteomes; UP000193435; 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; 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; IPR011297; PTS_IIABC_b_glu.
DR   InterPro; IPR001996; PTS_IIB_1.
DR   NCBIfam; TIGR00830; PTBA; 1.
DR   NCBIfam; TIGR01995; PTS-II-ABC-beta; 1.
DR   PANTHER; PTHR30175; PHOSPHOTRANSFERASE SYSTEM TRANSPORT PROTEIN; 1.
DR   PANTHER; PTHR30175:SF1; PTS SYSTEM ARBUTIN-, CELLOBIOSE-, AND SALICIN-SPECIFIC EIIBC 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:UP000193435};
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        99..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        172..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        211..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        253..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        282..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        308..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        333..353
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        391..415
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        435..458
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          4..86
FT                   /note="PTS EIIB type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51098"
FT   DOMAIN          101..474
FT                   /note="PTS EIIC type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51103"
FT   DOMAIN          508..612
FT                   /note="PTS EIIA type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51093"
FT   ACT_SITE        26
FT                   /note="Phosphocysteine intermediate; for EIIB activity"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00421"
SQ   SEQUENCE   638 AA;  68187 MW;  005D3BE798E7B7DC CRC64;
     MKYEALAKSI IENVGGTKNI NDVTHCVTRL RFKLKDDSKA NTNFLKKMDG IVTVIKSGGQ
     YQVVIGNHVP DVYDEIVKIG NFQTSNQELD NDTNIFNKFI DLISGIFAPT LGTLAATGMI
     KGFNALFVAL GLLTIESGTY QLLNAIGDSL FYFFPIFLAL TASKKMKVNQ FTAMAIGASL
     VYPTLSGLTA GEPLYTLFVG TIIESPVFIE FLGVPVILMS YASSVIPIIL SILFASKVEK
     GLKKLIPDVV KTFLIPFFTL LVVVPLTFII IGPVAIWAGN LVGAGTLVIY NLSPVLAGLI
     IGGYWQVFVI FGLHWGLVPI ALNNLALYGF DPVLAMSFAA SFAQTGAVIA VFMKTKEKKL
     KSLSIPSIIS GLFGVTEPAI YGITLPLKKP FIMSCVAGGI GGAAIGLIGG KFYMVGGLGI
     FGITNFLNPV GGNNATVLGI ATIVTGSLIL GFILTYLVGF GKLYEDETII AKSINEGIVG
     LGDEVYIVKD TIESPLKGSV VTLSDVQDEA FSSGAMGKGI AIDPVEGKLV SPVSGEITMI
     FPTSHAVGIT SDEGTEILIH IGMDTVKMNE EGFIPHVKQG DRVIKGQLLI EFDIFKIQDA
     GYSVITPIVI TNSKDYLDVI TTDKELIDPK DQLMTIVI
//
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