ID A0A0F0CB52_9CLOT Unreviewed; 634 AA.
AC A0A0F0CB52;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=bglF_3 {ECO:0000313|EMBL:KJJ71205.1};
GN ORFNames=CLFS41_25890 {ECO:0000313|EMBL:KJJ71205.1};
OS Clostridium sp. FS41.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1609975 {ECO:0000313|EMBL:KJJ71205.1, ECO:0000313|Proteomes:UP000033604};
RN [1] {ECO:0000313|EMBL:KJJ71205.1, ECO:0000313|Proteomes:UP000033604}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FS41 {ECO:0000313|EMBL:KJJ71205.1,
RC ECO:0000313|Proteomes:UP000033604};
RA Poehlein A., Daniel R.;
RT "Genome sequencing of Clostridium sp. FS41.";
RL Submitted (FEB-2015) 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:KJJ71205.1}.
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DR EMBL; JYHN01000059; KJJ71205.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F0CB52; -.
DR PATRIC; fig|1609975.3.peg.2790; -.
DR Proteomes; UP000033604; 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; IPR001996; PTS_IIB_1.
DR InterPro; IPR010973; PTS_IIBC_sucr.
DR NCBIfam; TIGR00830; PTBA; 1.
DR NCBIfam; TIGR01996; PTS-II-BC-sucr; 1.
DR PANTHER; PTHR30175; PHOSPHOTRANSFERASE SYSTEM TRANSPORT PROTEIN; 1.
DR PANTHER; PTHR30175:SF4; PTS SYSTEM TREHALOSE-SPECIFIC EIIBC COMPONENT; 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:UP000033604};
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 109..130
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 182..200
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 212..237
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 258..276
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 282..307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 435..457
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 117..474
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000259|PROSITE:PS51103"
FT DOMAIN 505..609
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 634 AA; 67801 MW; 42D6DE742E9D8C2D CRC64;
MDYAKIAGLV IQYVGGKENI RSVAHCATRL RFQLRDNGLR NEEAISDIEG VKGVFLTQSQ
FQIIFGSGTV NLVCAEVQKQ LGVMEEKPED KNEEKGNPVQ RFIKMLSDIF VPIIPAIVAG
GLLMGLNNLL TSPLIHGQAV IALFPQWQGL ATAINTFANA PFVFLPVLIG FSATKKFGGN
PFLGAAMGMI MVHPDLLNAY QIGIADPPMW NIFGFQIAAI GYQGTVLPVL AVSWILANIE
KRLRRVTPSW LDNLTTPLLS ILITSFLTFI FVGPVLREAG NLLAAGITWL YNTLGPVGGA
LFGFAYAPIT MTGMHHSFIA IETQLLADSV HTGGSFIFST ASMNNVAQGA AVLAVLLMTK
NDKIKSICSA SGISALLGIT EPAMFGVTLK LKYPFYAAMA GSAVGSAYLA ATKTLAQALG
AAGLPGFISM KPDHYMNFAI GIILSMGVSF ALTIVFWKKF GLEKQDSTKA APVSGLPAPE
TPDTQTAVLY APMKGEMIPV ERSEDEVFAS KALGDGVAIN PEDGMVYAPC DGTVTLLFPT
RHAVGIRTES GVEVLIHIGI NTVQLDGQGF EAYVAQGDTV KQGDQLILAD LDLIREKGLN
PQTMMILPEG AGLRIRRSAD SQVDKDTRAV AVYK
//
