PSPE_ECOLI
ID PSPE_ECOLI Reviewed; 104 AA.
AC P23857;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Thiosulfate sulfurtransferase PspE;
DE Short=TST;
DE EC=2.8.1.1;
DE AltName: Full=Phage shock protein E;
DE Flags: Precursor;
GN Name=pspE; OrderedLocusNames=b1308, JW1301;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=1712397; DOI=10.1016/0022-2836(91)90379-k;
RA Brissette J.L., Weiner L., Ripmaster T.L., Model P.;
RT "Characterization and sequence of the Escherichia coli stress-induced psp
RT operon.";
RL J. Mol. Biol. 220:35-48(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(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 PROTEIN SEQUENCE OF 20-29.
RC STRAIN=K12;
RX PubMed=9868784; DOI=10.1111/j.1574-6968.1998.tb13343.x;
RA Wasinger V.C., Humphery-Smith I.;
RT "Small genes/gene-products in Escherichia coli K-12.";
RL FEMS Microbiol. Lett. 169:375-382(1998).
RN [6]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, INDUCTION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=11997041; DOI=10.1016/s0014-5793(02)02695-9;
RA Adams H., Teertstra W., Koster M., Tommassen J.;
RT "PspE (phage-shock protein E) of Escherichia coli is a rhodanese.";
RL FEBS Lett. 518:173-176(2002).
RN [7]
RP BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM, SUBSTRATE SPECIFICITY,
RP INDUCTION, AND ACTIVITY REGULATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=19088907; DOI=10.2174/1874285800802010018;
RA Cheng H., Donahue J.L., Battle S.E., Ray W.K., Larson T.J.;
RT "Biochemical and genetic characterization of pspE and glpE, two single-
RT domain sulfurtransferases of Escherichia coli.";
RL Open Microbiol. J. 2:18-28(2008).
RN [8]
RP STRUCTURE BY NMR, AND SUBUNIT.
RX PubMed=18355042; DOI=10.1021/bi800039n;
RA Li H., Yang F., Kang X., Xia B., Jin C.;
RT "Solution structures and backbone dynamics of Escherichia coli rhodanese
RT PspE in its sulfur-free and persulfide-intermediate forms: implications for
RT the catalytic mechanism of rhodanese.";
RL Biochemistry 47:4377-4385(2008).
CC -!- FUNCTION: The phage shock protein (psp) operon (pspABCDE) may play a
CC significant role in the competition for survival under nutrient- or
CC energy-limited conditions. PspE catalyzes the sulfur-transfer reaction
CC from thiosulfate to cyanide, to form sulfite and thiocyanate. Also able
CC to use dithiol (dithiothreitol) as an alternate sulfur acceptor. Also
CC possesses a very low mercaptopyruvate sulfurtransferase activity.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydrogen cyanide + thiosulfate = 2 H(+) + sulfite +
CC thiocyanate; Xref=Rhea:RHEA:16881, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17359, ChEBI:CHEBI:18022, ChEBI:CHEBI:18407,
CC ChEBI:CHEBI:33542; EC=2.8.1.1;
CC Evidence={ECO:0000269|PubMed:11997041};
CC -!- ACTIVITY REGULATION: Inhibited by thiosulfate above 100 mM,
CC particularly at low cyanide concentrations (<5 mM). Inhibited by sodium
CC sulfate or sodium chloride at 0.25 M which gives around 50% inhibition
CC of rhodanese activity. Addition of sodium phosphate at the same
CC concentration results in about 65% inhibition. Sulfite strongly
CC inhibits PspE activity (1 mM sodium sulfite resulted in more than 50%
CC inhibition of rhodanese activity). {ECO:0000269|PubMed:11997041,
CC ECO:0000269|PubMed:19088907}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.7 mM for thiosulfate (at pH 8.6 and at 25 degrees Celsius)
CC {ECO:0000269|PubMed:11997041, ECO:0000269|PubMed:19088907};
CC KM=10 mM for dithiothreitol (at pH 8.6 and at 25 degrees Celsius)
CC {ECO:0000269|PubMed:11997041, ECO:0000269|PubMed:19088907};
CC KM=32 mM for cyanide (at pH 8.6 and at 25 degrees Celsius)
CC {ECO:0000269|PubMed:11997041, ECO:0000269|PubMed:19088907};
CC Vmax=410 umol/min/mg enzyme toward cyanide (at pH 8.6 and at 25
CC degrees Celsius) {ECO:0000269|PubMed:11997041,
CC ECO:0000269|PubMed:19088907};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18355042}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:1712397}.
CC -!- INDUCTION: By heat, ethanol, osmotic shock and infection by filamentous
CC bacteriophages. Expression is positively regulated by cyclic AMP-cAMP
CC receptor protein (cAMP-CRP). Expressed at higher levels during growth
CC on glycerol, acetate or proline as carbon source relative to expression
CC during growth on glucose. {ECO:0000269|PubMed:11997041,
CC ECO:0000269|PubMed:1712397, ECO:0000269|PubMed:19088907}.
CC -!- MISCELLANEOUS: Catalysis proceeds by a classical ping-pong bi-bi
CC reaction mechanism, whereby a covalent enzyme-sulfur intermediate is
CC formed on the active site cysteine.
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DR EMBL; X57560; CAA40793.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74390.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA14877.1; -; Genomic_DNA.
DR PIR; S17125; S17125.
DR RefSeq; NP_415824.1; NC_000913.3.
DR RefSeq; WP_000473109.1; NZ_STEB01000005.1.
DR PDB; 2JTQ; NMR; -; A=20-104.
DR PDB; 2JTR; NMR; -; A=20-104.
DR PDB; 2JTS; NMR; -; A=20-104.
DR PDBsum; 2JTQ; -.
DR PDBsum; 2JTR; -.
DR PDBsum; 2JTS; -.
DR AlphaFoldDB; P23857; -.
DR SMR; P23857; -.
DR BioGRID; 4263234; 411.
DR BioGRID; 850024; 1.
DR DIP; DIP-10591N; -.
DR IntAct; P23857; 3.
DR STRING; 511145.b1308; -.
DR jPOST; P23857; -.
DR PaxDb; P23857; -.
DR PRIDE; P23857; -.
DR EnsemblBacteria; AAC74390; AAC74390; b1308.
DR EnsemblBacteria; BAA14877; BAA14877; BAA14877.
DR GeneID; 66674864; -.
DR GeneID; 945652; -.
DR KEGG; ecj:JW1301; -.
DR KEGG; eco:b1308; -.
DR PATRIC; fig|1411691.4.peg.971; -.
DR EchoBASE; EB0773; -.
DR eggNOG; COG0607; Bacteria.
DR HOGENOM; CLU_089574_15_1_6; -.
DR InParanoid; P23857; -.
DR OMA; RSHMAMQ; -.
DR PhylomeDB; P23857; -.
DR BioCyc; EcoCyc:EG10780-MON; -.
DR BioCyc; MetaCyc:EG10780-MON; -.
DR SABIO-RK; P23857; -.
DR EvolutionaryTrace; P23857; -.
DR PRO; PR:P23857; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0042597; C:periplasmic space; IDA:EcoCyc.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IDA:EcoCyc.
DR Gene3D; 3.40.250.10; -; 1.
DR InterPro; IPR014323; Phageshock_PspE.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR Pfam; PF00581; Rhodanese; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52821; SSF52821; 1.
DR TIGRFAMs; TIGR02981; phageshock_pspE; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Periplasm; Reference proteome;
KW Signal; Stress response; Transferase.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:9868784"
FT CHAIN 20..104
FT /note="Thiosulfate sulfurtransferase PspE"
FT /id="PRO_0000030431"
FT DOMAIN 20..104
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT ACT_SITE 67
FT /note="Cysteine persulfide intermediate"
FT SITE 93
FT /note="May be important for providing the necessary
FT conformational flexibility for enzymatic catalysis"
FT STRAND 21..25
FT /evidence="ECO:0007829|PDB:2JTQ"
FT HELIX 29..32
FT /evidence="ECO:0007829|PDB:2JTQ"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:2JTQ"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:2JTS"
FT HELIX 45..55
FT /evidence="ECO:0007829|PDB:2JTQ"
FT STRAND 61..70
FT /evidence="ECO:0007829|PDB:2JTQ"
FT HELIX 71..82
FT /evidence="ECO:0007829|PDB:2JTQ"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:2JTQ"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:2JTQ"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:2JTQ"
SQ SEQUENCE 104 AA; 11475 MW; 52D52FB8FC0CC943 CRC64;
MFKKGLLALA LVFSLPVFAA EHWIDVRVPE QYQQEHVQGA INIPLKEVKE RIATAVPDKN
DTVKVYCNAG RQSGQAKEIL SEMGYTHVEN AGGLKDIAMP KVKG
