LSRE_SALTY
ID LSRE_SALTY Reviewed; 254 AA.
AC Q8ZKP8;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Putative epimerase LsrE;
DE EC=5.1.3.- {ECO:0000250|UniProtKB:P32719};
GN Name=lsrE; OrderedLocusNames=STM4080;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP INDUCTION.
RC STRAIN=ATCC 14028 / SGSG 2980 / CDC 6516-60 / NCTC 12023;
RX PubMed=11722742; DOI=10.1046/j.1365-2958.2001.02669.x;
RA Taga M.E., Semmelhack J.L., Bassler B.L.;
RT "The LuxS-dependent autoinducer AI-2 controls the expression of an ABC
RT transporter that functions in AI-2 uptake in Salmonella typhimurium.";
RL Mol. Microbiol. 42:777-793(2001).
RN [3]
RP INDUCTION.
RC STRAIN=ATCC 14028 / SGSG 2980 / CDC 6516-60 / NCTC 12023;
RX PubMed=14622426; DOI=10.1046/j.1365-2958.2003.03781.x;
RA Taga M.E., Miller S.T., Bassler B.L.;
RT "Lsr-mediated transport and processing of AI-2 in Salmonella typhimurium.";
RL Mol. Microbiol. 50:1411-1427(2003).
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:P32719};
CC Note=Binds 1 divalent metal cation per subunit.
CC {ECO:0000250|UniProtKB:P32719};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: In the absence of AI-2, repressed by LsrR. Induced by AI-2,
CC via release of the LsrR repressor. {ECO:0000269|PubMed:11722742,
CC ECO:0000269|PubMed:14622426}.
CC -!- SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family.
CC {ECO:0000305}.
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DR EMBL; AE006468; AAL22920.1; -; Genomic_DNA.
DR RefSeq; NP_462961.1; NC_003197.2.
DR RefSeq; WP_001088049.1; NC_003197.2.
DR AlphaFoldDB; Q8ZKP8; -.
DR SMR; Q8ZKP8; -.
DR STRING; 99287.STM4080; -.
DR PaxDb; Q8ZKP8; -.
DR EnsemblBacteria; AAL22920; AAL22920; STM4080.
DR GeneID; 1255607; -.
DR KEGG; stm:STM4080; -.
DR PATRIC; fig|99287.12.peg.4300; -.
DR HOGENOM; CLU_054856_3_0_6; -.
DR OMA; GQFSPFF; -.
DR PhylomeDB; Q8ZKP8; -.
DR BioCyc; SENT99287:STM4080-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004750; F:D-ribulose-phosphate 3-epimerase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IBA:GO_Central.
DR GO; GO:0044262; P:cellular carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IBA:GO_Central.
DR CDD; cd00429; RPE; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000056; Ribul_P_3_epim-like.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR PANTHER; PTHR11749; PTHR11749; 1.
DR Pfam; PF00834; Ribul_P_3_epim; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Isomerase; Membrane; Metal-binding; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..254
FT /note="Putative epimerase LsrE"
FT /id="PRO_0000351561"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 52
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT ACT_SITE 199
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 50
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 52
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 81
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 166..169
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 199..201
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 199
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000250|UniProtKB:P32719"
FT BINDING 221..222
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P32719"
SQ SEQUENCE 254 AA; 27635 MW; F8272A0A05F15451 CRC64;
MNSQFAGLTR EACVALLASY PLSVGILAGQ WIALHRYLQQ LEALNQPLLH LDLMDGQFCP
QFTVGPWAVG QLPQTFIKDV HLMVADQWTA AQACVKAGAH CITLQAEGDI HLHHTLSWLG
QQTVPVIGGE MPVIRGISLC PATPLDVIIP ILSDVEVIQL LAVNPGYGSK MRSSDLHERV
AQLLCLLGDK REGKIIVIDG SLTQDQLPSL IAQGIDRVVS GSALFRDDRL VENTRSWRAM
FKVAGDTTFL PSTA
