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Database: UniProt
Entry: A0A0R1V9T7_9LACO
LinkDB: A0A0R1V9T7_9LACO
Original site: A0A0R1V9T7_9LACO 
ID   A0A0R1V9T7_9LACO        Unreviewed;       623 AA.
AC   A0A0R1V9T7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Beta-glucosides PTS, EIIBCA {ECO:0000313|EMBL:KRL98699.1};
GN   ORFNames=FD50_GL000506 {ECO:0000313|EMBL:KRL98699.1};
OS   Liquorilactobacillus satsumensis DSM 16230 = JCM 12392.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Liquorilactobacillus.
OX   NCBI_TaxID=1423801 {ECO:0000313|EMBL:KRL98699.1, ECO:0000313|Proteomes:UP000051166};
RN   [1] {ECO:0000313|EMBL:KRL98699.1, ECO:0000313|Proteomes:UP000051166}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16230 {ECO:0000313|EMBL:KRL98699.1,
RC   ECO:0000313|Proteomes:UP000051166};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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:KRL98699.1}.
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DR   EMBL; AZFQ01000036; KRL98699.1; -; Genomic_DNA.
DR   RefSeq; WP_056960666.1; NZ_AZFQ01000036.1.
DR   AlphaFoldDB; A0A0R1V9T7; -.
DR   STRING; 1423801.FD50_GL000506; -.
DR   PATRIC; fig|1423801.4.peg.515; -.
DR   OrthoDB; 9769191at2; -.
DR   Proteomes; UP000051166; 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   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        100..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        142..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        204..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        236..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        281..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        316..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        349..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        376..396
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        416..438
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          103..455
FT                   /note="PTS EIIC type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51103"
FT   DOMAIN          490..596
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   623 AA;  67468 MW;  36517C3F1174EE8E CRC64;
     MNDKEITQTL IAELGGAKNI QSFTHCATRL RFQLKDEKKA NKNKIENIPS VISVVKAAGQ
     YQVVFGPKVV DIFNEMNELI DVDNKVSVIQ RRDKKNIFNA LIDFVSSVFT PILYVLIGSG
     IIKGLLAIFT SLNWMKATSG TYTILNAAGD SLYYFLPMFL AVTCARKLKT NLFVSLAIGG
     SLVYPNIAAL YGKTTDFLNM PIDIATFKSS VFPIIFAIFS LKYLEKIMKK TIPSAVENIF
     APLISLILLV PLTIILFGPL GSILSNEIAS LYMNLYGLNR MIAGAFIGFF AQAMVVFGIH
     WGLFPIIFSD IQKYGYDTIL AVFGPSIIAQ SGAAFGILMR TKNSTMKKIS SSATIMGFFG
     ISEAAIYGVT LKYKRAFLMA MIGGGLGGAI AGAAGSRATA VAVASVPSFP VYFGHGFLQF
     IVAYFAAFLV AAVLTYFFGF DKNIEASGEA PAKVDITSVS GNKEKGEPWE PLVIYSPVDG
     EVKKLADVAD KVFASGSLGK GLVVKPNKTR QSVLSPVDGV VTVTYTTRHA YGITTDDGRQ
     FLIHIGINTV DLNGEQFSDP IQKNKRIKKG EPLCIANFEE IAAKGYDSSV IVTLINSTSV
     TEIKSIKIGE HVSAKDELAS FID
//
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