ID A0A0R2MT96_9LACO Unreviewed; 652 AA.
AC A0A0R2MT96;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Beta-glucosides PTS, EIIABC {ECO:0000313|EMBL:KRO14707.1};
GN ORFNames=IV64_GL000880 {ECO:0000313|EMBL:KRO14707.1};
OS Lactiplantibacillus xiangfangensis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactiplantibacillus.
OX NCBI_TaxID=942150 {ECO:0000313|EMBL:KRO14707.1, ECO:0000313|Proteomes:UP000051783};
RN [1] {ECO:0000313|EMBL:KRO14707.1, ECO:0000313|Proteomes:UP000051783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 26013 {ECO:0000313|EMBL:KRO14707.1,
RC ECO:0000313|Proteomes:UP000051783};
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:KRO14707.1}.
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DR EMBL; JQCL01000008; KRO14707.1; -; Genomic_DNA.
DR RefSeq; WP_057705263.1; NZ_JQCL01000008.1.
DR AlphaFoldDB; A0A0R2MT96; -.
DR STRING; 942150.IV64_GL000880; -.
DR PATRIC; fig|942150.3.peg.903; -.
DR OrthoDB; 9769191at2; -.
DR Proteomes; UP000051783; 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; IPR001996; PTS_IIB_1.
DR NCBIfam; TIGR00830; PTBA; 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 288..312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 332..355
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 362..382
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 394..416
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 479..500
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 512..533
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 545..564
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 570..588
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 616..637
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 29..133
FT /note="PTS EIIA type-1"
FT /evidence="ECO:0000259|PROSITE:PS51093"
FT DOMAIN 181..263
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000259|PROSITE:PS51098"
FT DOMAIN 306..652
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000259|PROSITE:PS51103"
FT ACT_SITE 203
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00421"
SQ SEQUENCE 652 AA; 68650 MW; 59BD9E7289BA9ACC CRC64;
MSKMAAETVM TTLCAPVAGR LHELKVMDDP VFSQGLMGVG FAIEPTDGRV YAPVSGKVTM
VAKTKHAVGL RTVTGVEVLL HLGIDTVELD GRPFELMVKV GEQVVAGQVL VRMDLTMIKE
VHKVPTVITV VTNSTALQAQ LFLKSEAGLV QPHVPVAMVT TLEEASPAMT SSATGQTGAY
TQLATQIIQG VGGRDNVTSV IHCITRLRFY LKDETLVQRT QLTELSGVID VAHAADQLQV
VIGSAVNDVY DAVMAQLGPQ FMGENTEAVV EPPKQKSKSL LGVIKQSLNS LIGVMTASMI
PVIGILAGSG ILKGILAALT GFKILNPTDG TYMVLNAVGD AVFYFLPIIL GFTAAKRLGS
NPIVLAVVGG ILVYPSLISA AGKAATAQIT VFGLPVHLMT YSASVFPIIL AAWLGVYVEK
GLKKLLPVAL RGVFSPIIEA LVLGLVILGI VGPLMTVVSQ VLADAILATY NFSPALSGLV
VGGLYQLMVI FGLHWGLVPI VVNDLATNGH SYLNALISVT MVAQGGAALA VALKTRHRKL
KRLSLAAAVS AFCGVTEPAI YGVNLKYKRV FIVGSIASAL GGLLTGLLRV NNYALSGALI
GFPAFITPDV GIGSNFYGYL ISHYGTLLIA MVAVYFFGFS DKMRTEKALD SH
//
