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Database: UniProt
Entry: A0A1D2L529_BROTH
LinkDB: A0A1D2L529_BROTH
Original site: A0A1D2L529_BROTH 
ID   A0A1D2L529_BROTH        Unreviewed;       619 AA.
AC   A0A1D2L529;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=PTS beta-glucoside transporter subunit EIIBCA {ECO:0000313|EMBL:ATF25838.1};
GN   ORFNames=CNY62_05190 {ECO:0000313|EMBL:ATF25838.1};
OS   Brochothrix thermosphacta (Microbacterium thermosphactum).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Brochothrix.
OX   NCBI_TaxID=2756 {ECO:0000313|EMBL:ATF25838.1, ECO:0000313|Proteomes:UP000243591};
RN   [1] {ECO:0000313|EMBL:ATF25838.1, ECO:0000313|Proteomes:UP000243591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BI {ECO:0000313|EMBL:ATF25838.1,
RC   ECO:0000313|Proteomes:UP000243591};
RA   Paoli G.C., Wijey C., Chen C.-Y., Nguyen L., Yan X., Irwin P.L.;
RT   "Complete Genome Sequences of Two Strains of the Meat Spoilage Bacterium
RT   Brochothrix thermosphacta Isolated from Ground Chicken.";
RL   Submitted (SEP-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; CP023483; ATF25838.1; -; Genomic_DNA.
DR   RefSeq; WP_069125907.1; NZ_RSDU01000005.1.
DR   AlphaFoldDB; A0A1D2L529; -.
DR   STRING; 2756.BFR44_06670; -.
DR   KEGG; bths:CNY62_05190; -.
DR   OrthoDB; 9769191at2; -.
DR   Proteomes; UP000243591; Chromosome.
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; cd00210; PTS_IIA_glc; 1.
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:UP000243591};
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        111..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        140..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        196..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        243..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        282..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        318..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        350..368
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        380..403
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        423..444
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          102..460
FT                   /note="PTS EIIC type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51103"
FT   DOMAIN          490..594
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   619 AA;  65942 MW;  057DA17AD1647E92 CRC64;
     MKYTNTAKEI LKTVGGEDNI ESLVHCMTRL RFVLKDESQA DDAYMKNIPG VMGVMKKGGQ
     YQVIMGNDVA SYFKELQKIS TFSTNANTTS SKKKNPFEAF VDIISSCMSP LIPALLGGGM
     IKVLLILLPL MGLLDAKGQT YTILAFFGDA PFYFLPIMLA YTAAIKFNVT PMLAVSVAGI
     MLHPNFAAMV TAGDPVFLFG IPVTLASYSS SVIPILIMVW LMQYIESFFE KIIPTAIKSF
     MKPLLIILIS GFLALVVVGP LGTYAGELLS TIILGIQDKA GWLALGLMAA FMPLIIMTGM
     HWAFAPIFLI ASPATPDILI LPAMLASNIA QGAATLAVSL KAKNKNLKQI SAAASISALV
     AGVTEPALYG VNLKLKKPLY AAMISGGIVG IYIGITGLKS FAFAVPSVVS LPQFIGGGSN
     INIFNALVVT VGSFLLTFIL TWIFGFDEEP ENAPVPNSEA ENTVQSGSGD TKKIAAPTSG
     KVVPLEKVAD TVFSEKMMGD GIAILPDDNT FVAPFNGTVT TVFPTKHAIG LTSDSGIELL
     IHIGLETVSL DGKFFTTFVE AGDTITEGQK LVEVALDQLI AAGYDITTPV IVTNTDAYID
     IISKDVTTIK KSETILYVV
//
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