ID   PTRB_LACCA              Reviewed;         164 AA.
AC   Q9RGG4; F2M4V0;
DT   05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=PTS system sorbose-specific EIIB component {ECO:0000303|PubMed:10613875};
DE   AltName: Full=EIIB-Sor {ECO:0000303|PubMed:10613875};
DE   AltName: Full=Sorbose-specific phosphotransferase enzyme IIB component {ECO:0000303|PubMed:10613875};
DE            EC=2.7.1.206 {ECO:0000305|PubMed:10613875};
GN   Name=sorB {ECO:0000303|PubMed:10613875};
OS   Lactobacillus casei.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=1582;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   SUBCELLULAR LOCATION, INDUCTION, AND PHOSPHORYLATION AT HIS-14.
RC   STRAIN=ATCC 393 / DSM 20011 / BCRC 10697 / JCM 1134 / NBRC 15883 / NCIMB
RC   11970 / NCDO 161 / WDCM 00100;
RX   PubMed=10613875; DOI=10.1128/jb.182.1.155-163.2000;
RA   Yebra M.J., Veyrat A., Santos M.A., Perez-Martinez G.;
RT   "Genetics of L-sorbose transport and metabolism in Lactobacillus casei.";
RL   J. Bacteriol. 182:155-163(2000).
CC   -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC       system (PTS), a major carbohydrate active transport system, catalyzes
CC       the phosphorylation of incoming sugar substrates concomitant with their
CC       translocation across the cell membrane. The enzyme II SorABCD PTS
CC       system is involved in L-sorbose transport.
CC       {ECO:0000269|PubMed:10613875}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=keto-L-sorbose(out) + N(pros)-phospho-L-histidyl-[protein] =
CC         L-histidyl-[protein] + L-sorbose 1-phosphate(in);
CC         Xref=Rhea:RHEA:49296, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746,
CC         ChEBI:CHEBI:13172, ChEBI:CHEBI:29979, ChEBI:CHEBI:64837,
CC         ChEBI:CHEBI:137409; EC=2.7.1.206;
CC         Evidence={ECO:0000305|PubMed:10613875};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:10613875}.
CC   -!- INDUCTION: Induced by L-sorbose and repressed by D-glucose.
CC       {ECO:0000269|PubMed:10613875}.
CC   -!- DOMAIN: The PTS EIIB type-4 domain is phosphorylated by phospho-EIIA on
CC       a histidyl residue. Then, it transfers the phosphoryl group to the
CC       sugar substrate concomitantly with the sugar uptake processed by the
CC       PTS EIIC type-4 domain. {ECO:0000255|PROSITE-ProRule:PRU00424}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF129168; AAF24132.1; -; Genomic_DNA.
DR   RefSeq; WP_003586823.1; NZ_MODT01000074.1.
DR   AlphaFoldDB; Q9RGG4; -.
DR   SMR; Q9RGG4; -.
DR   STRING; 543734.LCABL_04260; -.
DR   TCDB; 4.A.6.1.26; the pts mannose-fructose-sorbose (man) family.
DR   iPTMnet; Q9RGG4; -.
DR   eggNOG; COG3444; Bacteria.
DR   OMA; IYLDERF; -.
DR   BRENDA; 2.7.1.206; 2854.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0022871; F:protein-N(PI)-phosphohistidine-sorbose phosphotransferase system transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00001; PTS_IIB_man; 1.
DR   Gene3D; 3.40.35.10; -; 1.
DR   InterPro; IPR004720; PTS_IIB_sorbose-sp.
DR   InterPro; IPR036667; PTS_IIB_sorbose-sp_sf.
DR   InterPro; IPR018455; PTS_IIB_sorbose-sp_subgr.
DR   Pfam; PF03830; PTSIIB_sorb; 1.
DR   SUPFAM; SSF52728; SSF52728; 1.
DR   TIGRFAMs; TIGR00854; pts-sorbose; 1.
DR   PROSITE; PS51101; PTS_EIIB_TYPE_4; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Kinase; Phosphoprotein; Phosphotransferase system;
KW   Sugar transport; Transferase; Transport.
FT   CHAIN           1..164
FT                   /note="PTS system sorbose-specific EIIB component"
FT                   /id="PRO_0000437531"
FT   DOMAIN          1..164
FT                   /note="PTS EIIB type-4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00424"
FT   ACT_SITE        14
FT                   /note="Pros-phosphohistidine intermediate"
FT                   /evidence="ECO:0000305|PubMed:10613875"
FT   MOD_RES         14
FT                   /note="Phosphohistidine; by EIIA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00424,
FT                   ECO:0000305|PubMed:10613875"
SQ   SEQUENCE   164 AA;  18304 MW;  5EBB7251BCE377C9 CRC64;
     MIITLARVDD RLIHGQVTTV WSKESNADRI IIVSSEVYKD DIRKTLLKQA APPGMKVNIV
     DVPKAIAVYN NPKYQNEKVF YLFTNPREVV DLVKGGIPLE KLNIGGMQFK QGKTQISKAV
     SLDADDVAAF RELHQLGVKL DLRVVKTDPS SDILAKIDEV FGKE