ID A0A0R1HSG3_9LACO Unreviewed; 657 AA.
AC A0A0R1HSG3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Beta-glucosides pts, eiibca {ECO:0000313|EMBL:KRK45543.1};
GN ORFNames=FC66_GL001359 {ECO:0000313|EMBL:KRK45543.1};
OS Dellaglioa algida DSM 15638.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Dellaglioa.
OX NCBI_TaxID=1423719 {ECO:0000313|EMBL:KRK45543.1, ECO:0000313|Proteomes:UP000051450};
RN [1] {ECO:0000313|EMBL:KRK45543.1, ECO:0000313|Proteomes:UP000051450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15638 {ECO:0000313|EMBL:KRK45543.1,
RC ECO:0000313|Proteomes:UP000051450};
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:KRK45543.1}.
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DR EMBL; AZDI01000007; KRK45543.1; -; Genomic_DNA.
DR RefSeq; WP_057974414.1; NZ_AZDI01000007.1.
DR AlphaFoldDB; A0A0R1HSG3; -.
DR STRING; 1423719.FC66_GL001359; -.
DR PATRIC; fig|1423719.4.peg.1381; -.
DR OrthoDB; 9769191at2; -.
DR Proteomes; UP000051450; 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:UP000051450};
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 114..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 175..197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 217..244
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 264..285
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 305..331
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 375..394
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 401..425
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 445..464
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 104..482
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000259|PROSITE:PS51103"
FT DOMAIN 520..624
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 657 AA; 69941 MW; F40A7AB7A9B89660 CRC64;
MSYDKLAKDI LKNVGGEANV NSVVHCTTRL RFKLKDEDKA NTDILKDMDG VVTVVKSGGQ
YQVVVGNQVP EVYDELVKGS GLAGDGIVPD DDGEKMKPLD AFIDMISGIF APTLGVLAAT
GMIKGLVAML VAFNWVAATS GTYIILNALG DSFFYFFPII LAYSASKKFH VNPLLAMVIG
ASLVYPTIVA QLPATLAATG GKALYTLFAG TIFESPIYMT FLGIPVIMMS YASSVVPIIV
SIWFASKVEP FFQKRIPEVV RTFLVPMLTA LVVVPITFIF IGPLTTWASD IVATGFSAVY
SLSPIAAGAV LGGLWQVLVI FGLHWGLIPL ALLNISTQGS DPILALMLGT TFAQIGSVLA
ITIKTKNNKL KALGYSSFIS GIFGVTEPAI YGITLPRKKP FVITCISAAI GGMILGLFGT
KGYLLGGLGI FSIPSYLNPK TGIDMSFYAV PIAIVVSFVL SYVLTMMFGL TKADQEVPVV
AETTNATTTA SAPVKSEQVE EEVLVSPLKG QVLPLADVKD PVFNSGAMGN GIAILPEIGQ
LYAPADGVIS LVFPTGHAVG MKTDSGAEIL MHIGMDTVEL GGKFFEIQTE MDKVVKKGDL
LLKFDIDEIK KAGYEIITPI IVTNTPRYKE VNPIAKEQSN VIVGDDLLDL ETNLGGK
//
