PTRB_KLEPN
ID PTRB_KLEPN Reviewed; 164 AA.
AC P37081;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=PTS system sorbose-specific EIIB component {ECO:0000303|PubMed:2287279};
DE AltName: Full=EIIB-Sor {ECO:0000303|PubMed:2287279};
DE AltName: Full=EIII-B-Sor;
DE AltName: Full=Sorbose-specific phosphotransferase enzyme IIB component {ECO:0000303|PubMed:2287279};
DE EC=2.7.1.206 {ECO:0000305|PubMed:6361004};
GN Name=sorB {ECO:0000303|PubMed:2287279};
OS Klebsiella pneumoniae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=1033-5P14 / KAY2026;
RX PubMed=7947968; DOI=10.1016/0167-4838(94)90124-4;
RA Wehmeier U.F., Lengeler J.W.;
RT "Sequence of the sor-operon for L-sorbose utilization from Klebsiella
RT pneumoniae KAY2026.";
RL Biochim. Biophys. Acta 1208:348-351(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7700234; DOI=10.1007/bf00298968;
RA Wehmeier U.F., Wohrl B.M., Lengeler J.W.;
RT "Molecular analysis of the phosphoenolpyruvate-dependent L-sorbose:
RT phosphotransferase system from Klebsiella pneumoniae and of its multidomain
RT structure.";
RL Mol. Gen. Genet. 246:610-618(1995).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=1033-5P14 / KAY2026;
RX PubMed=6361004; DOI=10.1128/jb.157.1.39-45.1984;
RA Sprenger G.A., Lengeler J.W.;
RT "L-Sorbose metabolism in Klebsiella pneumoniae and Sor+ derivatives of
RT Escherichia coli K-12 and chemotaxis toward sorbose.";
RL J. Bacteriol. 157:39-45(1984).
RN [4]
RP FUNCTION, AND INDUCTION.
RX PubMed=2287279; DOI=10.1111/j.1365-2958.1990.tb02067.x;
RA Woehrl B.M., Lengeler J.W.;
RT "Cloning and physical mapping of the sor genes for L-sorbose transport and
RT metabolism from Klebsiella pneumoniae.";
RL Mol. Microbiol. 4:1557-1565(1990).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), ACTIVE SITE, AND SUBUNIT.
RX PubMed=12662934; DOI=10.1016/s0022-2836(03)00215-8;
RA Orriss G.L., Erni B., Schirmer T.;
RT "Crystal structure of the IIB(Sor) domain of the sorbose permease from
RT Klebsiella pneumoniae solved to 1.75A resolution.";
RL J. Mol. Biol. 327:1111-1119(2003).
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 SorABFM PTS
CC system is involved in L-sorbose transport. {ECO:0000269|PubMed:6361004,
CC ECO:0000305|PubMed:2287279, ECO:0000305|PubMed:7700234}.
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:6361004};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=30 uM for L-sorbose {ECO:0000269|PubMed:6361004};
CC -!- SUBUNIT: Dimer of dimers. {ECO:0000269|PubMed:12662934}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: By L-sorbose. {ECO:0000269|PubMed:2287279}.
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}.
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DR EMBL; X66059; CAA46858.1; -; Genomic_DNA.
DR PIR; S50188; S50188.
DR RefSeq; WP_004151751.1; NZ_WYAL01000049.1.
DR PDB; 1NRZ; X-ray; 1.75 A; A/B/C/D=1-164.
DR PDBsum; 1NRZ; -.
DR AlphaFoldDB; P37081; -.
DR SMR; P37081; -.
DR TCDB; 4.A.6.1.3; the pts mannose-fructose-sorbose (man) family.
DR GeneID; 56941193; -.
DR OMA; IYLDERF; -.
DR OrthoDB; 1696140at2; -.
DR SABIO-RK; P37081; -.
DR EvolutionaryTrace; P37081; -.
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 3D-structure; 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_0000186666"
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:12662934"
FT MOD_RES 14
FT /note="Phosphohistidine; by EIIA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00424"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:1NRZ"
FT HELIX 15..25
FT /evidence="ECO:0007829|PDB:1NRZ"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:1NRZ"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:1NRZ"
FT HELIX 41..49
FT /evidence="ECO:0007829|PDB:1NRZ"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:1NRZ"
FT HELIX 62..69
FT /evidence="ECO:0007829|PDB:1NRZ"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:1NRZ"
FT STRAND 78..85
FT /evidence="ECO:0007829|PDB:1NRZ"
FT HELIX 86..93
FT /evidence="ECO:0007829|PDB:1NRZ"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:1NRZ"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:1NRZ"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:1NRZ"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:1NRZ"
FT HELIX 124..135
FT /evidence="ECO:0007829|PDB:1NRZ"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:1NRZ"
FT HELIX 153..158
FT /evidence="ECO:0007829|PDB:1NRZ"
SQ SEQUENCE 164 AA; 18456 MW; A9614133B19E1567 CRC64;
MQITLARIDD RLIHGQVTTV WSKVANAQRI IICNDDVFND EVRRTLLRQA APPGMKVNVV
SLEKAVAVYH NPQYQDETVF YLFTNPHDVL TMVRQGVQIA TLNIGGMAWR PGKKQLTKAV
SLDPQDIQAF RELDKLGVKL DLRVVASDPS VNILDKINET AFCE
