ID D5GZB9_LACCS Unreviewed; 635 AA.
AC D5GZB9;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=PTS system, beta-glucoside-specific IIABC component {ECO:0000313|EMBL:CBL51128.1};
GN Name=bglF3 {ECO:0000313|EMBL:CBL51128.1};
GN OrderedLocusNames=LCRIS_01681 {ECO:0000313|EMBL:CBL51128.1};
OS Lactobacillus crispatus (strain ST1).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=748671 {ECO:0000313|EMBL:CBL51128.1, ECO:0000313|Proteomes:UP000002371};
RN [1] {ECO:0000313|EMBL:CBL51128.1, ECO:0000313|Proteomes:UP000002371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST1 {ECO:0000313|EMBL:CBL51128.1,
RC ECO:0000313|Proteomes:UP000002371};
RX PubMed=20435723; DOI=10.1128/JB.00399-10;
RA Ojala T., Kuparinen V., Koskinen J.P., Alatalo E., Holm L., Auvinen P.,
RA Edelman S., Westerlund-Wikstrom B., Korhonen T.K., Paulin L., Kankainen M.;
RT "Genome sequence of Lactobacillus crispatus ST1.";
RL J. Bacteriol. 192:3547-3548(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ST1;
RA Ojala T., Kuparinen V., Koskinen J.P., Alatalo E., Holm L., Auvinen P.,
RA Edelman S., Westerlund-Wikstroem B., Korhonen T.K., Paulin L.,
RA Kankainen M.;
RT "Genome Sequence of Lactobacillus crispatus ST1.";
RL Submitted (MAR-2010) 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; FN692037; CBL51128.1; -; Genomic_DNA.
DR RefSeq; WP_013086816.1; NC_014106.1.
DR AlphaFoldDB; D5GZB9; -.
DR KEGG; lcr:LCRIS_01681; -.
DR PATRIC; fig|748671.3.peg.1653; -.
DR eggNOG; COG1263; Bacteria.
DR eggNOG; COG1264; Bacteria.
DR eggNOG; COG2190; Bacteria.
DR HOGENOM; CLU_012312_2_3_9; -.
DR Proteomes; UP000002371; 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; 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; 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 152..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 211..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 253..272
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 278..301
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 387..409
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 429..452
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 108..466
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000259|PROSITE:PS51103"
FT DOMAIN 501..605
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 635 AA; 69111 MW; 1DCF653579A03A76 CRC64;
MKYKKMCEQI IKAVGGESNI QSVVHCSTRL RFVLKDESKA NDKEAENING VLQVVKKAGQ
YQLVIGNTVE DVYDELMQLI HVDNSDSSSN DNDNQPKKKQ NLFDTIISVI TGSIAPAIPL
LAGAGMGKVL LLLLTITNVL SDKSQTYQML NLIFDTGYYF MPVYVGFSAA KVFNTNQMLG
AFLGLVTEHP LWVQIVNAKK PFSFLGINVP LIQYSSTLIT AIMSVWIMSY VYKVVKKITP
GMVKVFLEPM LTMLIMGPLT FIVLGPISNW ISQGIGFIAM WLYHNAGLVA IPILAAAYPW
LVSIGIHKAL SPISIQLVAT QGFDPIIRVV ALCSNMSQAA ASLAVGLKSK NKELKSLALS
SSATAYLGGI TEPALFGVNL RLKKPMYGAM IGGAIAGVVA SFLKIKAFIY VTPAFLSLPM
WISKTENFVL QAIIIIVVSS VATFIATWLI GFDDPVDREE IKKETEAAKE QEKKKFAKEN
GKHELQSPVT GTLESITKVD DPTFSSGVMG KGIAVVPSEG KIYAPDDGII TATFETNHAI
GLHLNNDADV LIHVGIDTVQ MQGDGFKALV KKGDHVKAGQ EILDFDIDKI KKAGYDPTVM
MIILNSKDFL EVLPTLKDTE KTESIKHGAD VMVLA
//
