OTSB_ECOLI
ID OTSB_ECOLI Reviewed; 266 AA.
AC P31678;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Trehalose-6-phosphate phosphatase;
DE Short=TPP;
DE EC=3.1.3.12 {ECO:0000269|PubMed:16990279};
DE AltName: Full=Osmoregulatory trehalose synthesis protein B;
DE AltName: Full=Trehalose 6-phosphate phosphatase;
DE AltName: Full=Trehalose-phosphatase;
GN Name=otsB; OrderedLocusNames=b1897, JW1886;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=K12 / CSH7;
RX PubMed=8045430; DOI=10.1016/0378-1119(94)90316-6;
RA Kaasen I., McDougall J., Stroem A.R.;
RT "Analysis of the otsBA operon for osmoregulatory trehalose synthesis in
RT Escherichia coli and homology of the OtsA and OtsB proteins to the yeast
RT trehalose-6-phosphate synthase/phosphatase complex.";
RL Gene 145:9-15(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP INDUCTION, AND NOMENCLATURE.
RX PubMed=3131312; DOI=10.1128/jb.170.6.2841-2849.1988;
RA Giaever H.M., Styrvold O.B., Kaasen I., Stroem A.R.;
RT "Biochemical and genetic characterization of osmoregulatory trehalose
RT synthesis in Escherichia coli.";
RL J. Bacteriol. 170:2841-2849(1988).
RN [6]
RP INDUCTION.
RX PubMed=1744047; DOI=10.1128/jb.173.24.7918-7924.1991;
RA Hengge-Aronis R., Klein W., Lange R., Rimmele M., Boos W.;
RT "Trehalose synthesis genes are controlled by the putative sigma factor
RT encoded by rpoS and are involved in stationary-phase thermotolerance in
RT Escherichia coli.";
RL J. Bacteriol. 173:7918-7924(1991).
RN [7]
RP FUNCTION AS A TREHALOSE-PHOSPHATE PHOSPHATASE, AND INDUCTION.
RX PubMed=1310094; DOI=10.1128/jb.174.3.889-898.1992;
RA Kaasen I., Falkenberg P., Styrvold O.B., Strom A.R.;
RT "Molecular cloning and physical mapping of the otsBA genes, which encode
RT the osmoregulatory trehalose pathway of Escherichia coli: evidence that
RT transcription is activated by katF (AppR).";
RL J. Bacteriol. 174:889-898(1992).
RN [8]
RP INDUCTION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=12105274; DOI=10.1073/pnas.142314099;
RA Kandror O., DeLeon A., Goldberg A.L.;
RT "Trehalose synthesis is induced upon exposure of Escherichia coli to cold
RT and is essential for viability at low temperatures.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9727-9732(2002).
RN [9]
RP INDUCTION.
RX PubMed=17015655; DOI=10.1128/jb.00508-06;
RA Weber A., Kogl S.A., Jung K.;
RT "Time-dependent proteome alterations under osmotic stress during aerobic
RT and anaerobic growth in Escherichia coli.";
RL J. Bacteriol. 188:7165-7175(2006).
RN [10]
RP FUNCTION AS A PHOSPHATASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBSTRATE SPECIFICITY, AND COFACTOR.
RX PubMed=16990279; DOI=10.1074/jbc.m605449200;
RA Kuznetsova E., Proudfoot M., Gonzalez C.F., Brown G., Omelchenko M.V.,
RA Borozan I., Carmel L., Wolf Y.I., Mori H., Savchenko A.V., Arrowsmith C.H.,
RA Koonin E.V., Edwards A.M., Yakunin A.F.;
RT "Genome-wide analysis of substrate specificities of the Escherichia coli
RT haloacid dehalogenase-like phosphatase family.";
RL J. Biol. Chem. 281:36149-36161(2006).
CC -!- FUNCTION: Removes the phosphate from trehalose 6-phosphate (Tre6P) to
CC produce free trehalose. Also catalyzes the dephosphorylation of
CC glucose-6-phosphate (Glu6P) and 2-deoxyglucose-6-phosphate (2dGlu6P).
CC {ECO:0000269|PubMed:1310094, ECO:0000269|PubMed:16990279}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-
CC trehalose + phosphate; Xref=Rhea:RHEA:23420, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16551, ChEBI:CHEBI:43474, ChEBI:CHEBI:58429; EC=3.1.3.12;
CC Evidence={ECO:0000269|PubMed:16990279};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23421;
CC Evidence={ECO:0000269|PubMed:16990279};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:16990279};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:16990279};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:16990279};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:16990279};
CC Note=Magnesium. Can also use other divalent metal cations as manganese,
CC cobalt or zinc. {ECO:0000269|PubMed:16990279};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.61 mM for Tre6P (with magnesium ions as cofactor and at pH 9)
CC {ECO:0000269|PubMed:16990279};
CC pH dependence:
CC Optimum pH is between 6 and 7.5. {ECO:0000269|PubMed:16990279};
CC -!- PATHWAY: Glycan biosynthesis; trehalose biosynthesis.
CC -!- INDUCTION: By cold-shock, osmotic-shock and during the transition to
CC stationary phase. Expression is partially dependent on RpoS.
CC {ECO:0000269|PubMed:12105274, ECO:0000269|PubMed:1310094,
CC ECO:0000269|PubMed:17015655, ECO:0000269|PubMed:1744047,
CC ECO:0000269|PubMed:3131312}.
CC -!- SIMILARITY: Belongs to the trehalose phosphatase family. {ECO:0000305}.
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DR EMBL; X69160; CAA48912.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74967.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15718.1; -; Genomic_DNA.
DR PIR; I83401; I83401.
DR RefSeq; NP_416411.1; NC_000913.3.
DR RefSeq; WP_001295645.1; NZ_SSZK01000001.1.
DR AlphaFoldDB; P31678; -.
DR SMR; P31678; -.
DR BioGRID; 4262243; 15.
DR IntAct; P31678; 15.
DR STRING; 511145.b1897; -.
DR SWISS-2DPAGE; P31678; -.
DR jPOST; P31678; -.
DR PaxDb; P31678; -.
DR PRIDE; P31678; -.
DR DNASU; 946406; -.
DR EnsemblBacteria; AAC74967; AAC74967; b1897.
DR EnsemblBacteria; BAA15718; BAA15718; BAA15718.
DR GeneID; 946406; -.
DR KEGG; ecj:JW1886; -.
DR KEGG; eco:b1897; -.
DR PATRIC; fig|1411691.4.peg.352; -.
DR EchoBASE; EB1702; -.
DR eggNOG; COG1877; Bacteria.
DR HOGENOM; CLU_037265_2_0_6; -.
DR InParanoid; P31678; -.
DR OMA; YGAERWD; -.
DR PhylomeDB; P31678; -.
DR BioCyc; EcoCyc:TREHALOSEPHOSPHASYN-MON; -.
DR BioCyc; MetaCyc:TREHALOSEPHOSPHASYN-MON; -.
DR BRENDA; 3.1.3.12; 2026.
DR UniPathway; UPA00299; -.
DR PRO; PR:P31678; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0004805; F:trehalose-phosphatase activity; IDA:EcoCyc.
DR GO; GO:0006970; P:response to osmotic stress; IEP:EcoCyc.
DR GO; GO:0005992; P:trehalose biosynthetic process; IMP:EcoCyc.
DR GO; GO:0070415; P:trehalose metabolism in response to cold stress; IMP:EcoCyc.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006379; HAD-SF_hydro_IIB.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR044651; OTSB-like.
DR InterPro; IPR003337; Trehalose_PPase.
DR PANTHER; PTHR43768; PTHR43768; 1.
DR Pfam; PF02358; Trehalose_PPase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01484; HAD-SF-IIB; 1.
DR TIGRFAMs; TIGR00685; T6PP; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..266
FT /note="Trehalose-6-phosphate phosphatase"
FT /id="PRO_0000058100"
FT ACT_SITE 20
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 20..22
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 20
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 22
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 266 AA; 29175 MW; 015E90EAD981B155 CRC64;
MTEPLTETPE LSAKYAWFFD LDGTLAEIKP HPDQVVVPDN ILQGLQLLAT ASDGALALIS
GRSMVELDAL AKPYRFPLAG VHGAERRDIN GKTHIVHLPD AIARDISVQL HTVIAQYPGA
ELEAKGMAFA LHYRQAPQHE DALMTLAQRI TQIWPQMALQ QGKCVVEIKP RGTSKGEAIA
AFMQEAPFIG RTPVFLGDDL TDESGFAVVN RLGGMSVKIG TGATQASWRL AGVPDVWSWL
EMITTALQQK RENNRSDDYE SFSRSI
