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Database: UniProt
Entry: A0A0A0DEN4_9STRE
LinkDB: A0A0A0DEN4_9STRE
Original site: A0A0A0DEN4_9STRE 
ID   A0A0A0DEN4_9STRE        Unreviewed;       628 AA.
AC   A0A0A0DEN4;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=PTS system, sucrose-specific IIB component {ECO:0000313|EMBL:KGM36515.1};
DE            EC=2.7.1.69 {ECO:0000313|EMBL:KGM36515.1};
GN   ORFNames=SSIN_1728 {ECO:0000313|EMBL:KGM36515.1};
OS   Streptococcus sinensis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=176090 {ECO:0000313|EMBL:KGM36515.1, ECO:0000313|Proteomes:UP000030019};
RN   [1] {ECO:0000313|EMBL:KGM36515.1, ECO:0000313|Proteomes:UP000030019}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HKU4 {ECO:0000313|EMBL:KGM36515.1,
RC   ECO:0000313|Proteomes:UP000030019};
RA   Teng J.L., Huang Y., Tse H., Lau S.K., Woo P.C.;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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:KGM36515.1}.
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DR   EMBL; JPEN01000099; KGM36515.1; -; Genomic_DNA.
DR   RefSeq; WP_037617888.1; NZ_JPEN01000099.1.
DR   AlphaFoldDB; A0A0A0DEN4; -.
DR   STRING; 176090.SSIN_1728; -.
DR   PATRIC; fig|176090.4.peg.1675; -.
DR   eggNOG; COG1263; Bacteria.
DR   eggNOG; COG1264; Bacteria.
DR   eggNOG; COG2190; Bacteria.
DR   Proteomes; UP000030019; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0103111; F:D-glucosamine PTS permease activity; IEA:UniProtKB-EC.
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; IPR001996; PTS_IIB_1.
DR   InterPro; IPR010973; PTS_IIBC_sucr.
DR   NCBIfam; TIGR00826; EIIB_glc; 1.
DR   NCBIfam; TIGR00830; PTBA; 1.
DR   NCBIfam; TIGR01996; PTS-II-BC-sucr; 1.
DR   PANTHER; PTHR30175:SF7; NEGATIVE REGULATOR OF SACY ACTIVITY; 1.
DR   PANTHER; PTHR30175; PHOSPHOTRANSFERASE SYSTEM TRANSPORT PROTEIN; 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, ECO:0000313|EMBL:KGM36515.1};
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..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        144..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        208..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        244..269
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        275..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        327..345
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        357..379
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        385..405
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        426..448
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          4..87
FT                   /note="PTS EIIB type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51098"
FT   DOMAIN          106..463
FT                   /note="PTS EIIC type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51103"
FT   DOMAIN          498..602
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   628 AA;  65458 MW;  7E19865CB4E8146A CRC64;
     MNNTEIAKKV IEALGGRENV NSVAHCATRL RVMVKDEEKI DKDTVENLEK VQGAFFNSGQ
     YQIIFGTGTV NKIYEEVVAL GLPTSSKAEM KAEAAKQGNW FQRAIRTFGD VFVPIIPVIV
     ATGLFMGVRG LLTALGMTLP EDVTTYTQIL TDTAFIILPG LVVWSTFRVF GGNPAVGIVL
     GMMLVSGSLP NAWAVASGGE VTAMQFFGFI PVVGLQGSVL PAFIIGVVGA KFEKAVRKVV
     PDVLDLLVTP FVTLLVMSIL GLFVIGPVFH VVENYILIGT KAILGLPFGL GGLLIGGVHQ
     LIVVSGVHHI FNLLEVQLLA ADHANPFNAI ITAAMTAQGA ATVAVGVKTK NPKLKTLAFP
     AALSAFLGIT EPAIFGVNLR YRKPFFLSLI AGAIGGGLAS ILGLAGTGNG ITIIPGTMLY
     IGNGQLVQYI LMVAVSFALG FALTYMFGYE DEETVTEKAE TEKLVEEETT GNVPAALQDE
     TIISPVVGQA VALADVNDPV FASGAMGQGI AIKPTEGVVY APADAEVTIA FATGHAYGLK
     TANGAEILIH VGIDTVSMNG EGFDQKVSQG STVKAGDVLG TFDSAKIAAA GLDDTTMVIV
     TNTADYASVT PVAAGAVAKG DAIIEVKA
//
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