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Database: UniProt
Entry: A0A1X9M682_9BACI
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ID   A0A1X9M682_9BACI        Unreviewed;       469 AA.
AC   A0A1X9M682;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=protein-N(pi)-phosphohistidine--sucrose phosphotransferase {ECO:0000256|ARBA:ARBA00044053};
DE            EC=2.7.1.211 {ECO:0000256|ARBA:ARBA00044053};
GN   Name=treB_2 {ECO:0000313|EMBL:ARK28955.1};
GN   ORFNames=BkAM31D_03260 {ECO:0000313|EMBL:ARK28955.1};
OS   Halalkalibacter krulwichiae.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halalkalibacter.
OX   NCBI_TaxID=199441 {ECO:0000313|EMBL:ARK28955.1, ECO:0000313|Proteomes:UP000193006};
RN   [1] {ECO:0000313|EMBL:ARK28955.1, ECO:0000313|Proteomes:UP000193006}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AM31D {ECO:0000313|EMBL:ARK28955.1,
RC   ECO:0000313|Proteomes:UP000193006};
RA   Krulwich T.A., Anastor L., Ehrlich R., Ehrlich G.D., Janto B.;
RT   "Bacillus krulwichiae AM31D Genome sequencing and assembly.";
RL   Submitted (APR-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}.
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DR   EMBL; CP020814; ARK28955.1; -; Genomic_DNA.
DR   RefSeq; WP_066157838.1; NZ_CP020814.1.
DR   AlphaFoldDB; A0A1X9M682; -.
DR   STRING; 199441.BkAM31D_03260; -.
DR   KEGG; bkw:BkAM31D_03260; -.
DR   Proteomes; UP000193006; 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: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:UP000193006};
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..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        155..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        187..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        228..248
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        260..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        292..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        342..365
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        399..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        441..463
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..469
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   469 AA;  49941 MW;  704C637B8D6472FE CRC64;
     MSDLKQAAKE VLAAIGGNEN IASATHCVTR LRFALVDEGK VDKEALEKID VVRGSFSTNG
     QFQVVIGQGT VDKVYKELVD LSGISESSKE ETKRAADKNL NPLQRAVKML ADIFIPILPA
     IVTAGLLMGI NNILTAQGIF GEQAVVEMFP QWADIANIIN LIANTAFVFL PGLIGWSAVK
     RFGGSELLGI VLGLMLVHPD LLNAWGYGAA QEAGEIPYWN LFGLDVAMVG YQGQVLPILV
     ASFVLAKIEL ALRKRVPDGF QLLVVAPVAL LVTGFIAFVA IGPITFAIGN GITNLFVGIF
     SNFAALGGLL YGAIYAPLVI TGMHHTFLAV DLQLIGSIGG TFLWPIVALS NIAQGSAALA
     MYFILKDEKV KGLSLTSSIS AYLGITEPAM FGVNLRYRFP FICAIIGSAI AAIWITVNSV
     IAPSIGVGGL PGIFSIEASG WFAFFIGMII AVTVPFVLTY LFARTRKTL
//
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