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Database: UniProt
Entry: A0A2N5G5T6_9BACI
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ID   A0A2N5G5T6_9BACI        Unreviewed;       467 AA.
AC   A0A2N5G5T6;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=protein-N(pi)-phosphohistidine--sucrose phosphotransferase {ECO:0000256|ARBA:ARBA00044053};
DE            EC=2.7.1.211 {ECO:0000256|ARBA:ARBA00044053};
GN   ORFNames=CU633_17600 {ECO:0000313|EMBL:PLR76090.1};
OS   Bacillus sp. V3-13.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2053728 {ECO:0000313|EMBL:PLR76090.1, ECO:0000313|Proteomes:UP000234805};
RN   [1] {ECO:0000313|EMBL:PLR76090.1, ECO:0000313|Proteomes:UP000234805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=V3-13 {ECO:0000313|EMBL:PLR76090.1,
RC   ECO:0000313|Proteomes:UP000234805};
RA   Seuylemezian A., Cooper K., Vaishampayan P.;
RT   "Comparitive Functional Genomics of Dry Heat Resistant strains isolated
RT   from the Viking Spacecraft.";
RL   Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(pros)-phospho-L-histidyl-[protein](out) + sucrose = L-
CC         histidyl-[protein] + sucrose 6(G)-phosphate(in);
CC         Xref=Rhea:RHEA:49236, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746,
CC         ChEBI:CHEBI:17992, ChEBI:CHEBI:29979, ChEBI:CHEBI:64837,
CC         ChEBI:CHEBI:91002; EC=2.7.1.211;
CC         Evidence={ECO:0000256|ARBA:ARBA00043763};
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:PLR76090.1}.
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DR   EMBL; PGUZ01000053; PLR76090.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N5G5T6; -.
DR   OrthoDB; 9769191at2; -.
DR   Proteomes; UP000234805; 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:0015574; F:trehalose transmembrane transporter 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; 3.30.1360.60; Glucose permease domain IIB; 1.
DR   InterPro; IPR036878; Glu_permease_IIB.
DR   InterPro; IPR018113; PTrfase_EIIB_Cys.
DR   InterPro; IPR003352; PTS_EIIC.
DR   InterPro; IPR013013; PTS_EIIC_1.
DR   InterPro; IPR001996; PTS_IIB_1.
DR   InterPro; IPR010973; PTS_IIBC_sucr.
DR   InterPro; IPR011296; PTS_IIBC_treh.
DR   NCBIfam; TIGR00826; EIIB_glc; 1.
DR   NCBIfam; TIGR01996; PTS-II-BC-sucr; 1.
DR   NCBIfam; TIGR01992; PTS-IIBC-Tre; 1.
DR   PANTHER; PTHR30175; PHOSPHOTRANSFERASE SYSTEM TRANSPORT PROTEIN; 1.
DR   PANTHER; PTHR30175:SF4; PTS SYSTEM TREHALOSE-SPECIFIC EIIBC COMPONENT; 1.
DR   Pfam; PF00367; PTS_EIIB; 1.
DR   Pfam; PF02378; PTS_EIIC; 1.
DR   SUPFAM; SSF55604; Glucose permease domain IIB; 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:UP000234805};
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        113..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        153..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        187..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        227..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        258..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        340..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        398..419
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        439..461
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          5..88
FT                   /note="PTS EIIB type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51098"
FT   DOMAIN          108..467
FT                   /note="PTS EIIC type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51103"
FT   ACT_SITE        27
FT                   /note="Phosphocysteine intermediate; for EIIB activity"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00421"
SQ   SEQUENCE   467 AA;  50062 MW;  455B40E30C544B00 CRC64;
     MSDNRKSAEQ IVEAVGGKDN IAAATHCVTR LRFALKDEDK VDKEKLEDID LVKGSFSANG
     QFQVVIGQGT VDKVYNEMVD ITGIGRASKE EIKTAAAEKL NPLQKAIKTL ADIFIPILPA
     IVTAGLLMGI NNIMTAPDIF FDDQSFVDVY ENWADLAGMI NLIANTAFVF LPGLIGWSAV
     NRFGGSPLLG IVLGLMLVHP DLLNAWGYGA ADEVPTWNLF GLEVQQVGYQ GQVLPVLVAS
     YVLARIEIFL RKRIPDGFQL LTVAPIALLV TGFLSFIAIG PITFYIGNLI TDGVVAIFDV
     APALGGLIYG GLYAPLVITG MHHTFLAVDL QLIGTIGGTF LWPMVALSNI AQGAAAFAMM
     VIHRKNDKLK GLALTSSISA WLGITEPAMF GVNLRFRYPF FAAIIGSAIA GVLLAINAVQ
     AASIGVGGLP GIFSIMAEYW SVFFIGMLIV LIVPFVLTIV FSRLKKA
//
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