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Protein

Thiosulfate sulfurtransferase PspE

Gene

pspE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The phage shock protein (psp) operon (pspABCDE) may play a significant role in the competition for survival under nutrient- or energy-limited conditions. PspE catalyzes the sulfur-transfer reaction from thiosulfate to cyanide, to form sulfite and thiocyanate. Also able to use dithiol (dithiothreitol) as an alternate sulfur acceptor. Also possesses a very low mercaptopyruvate sulfurtransferase activity.

Catalytic activityi

Thiosulfate + cyanide = sulfite + thiocyanate.1 Publication

Enzyme regulationi

Inhibited by thiosulfate above 100 mM, particularly at low cyanide concentrations (<5 mM). Inhibited by sodium sulfate or sodium chloride at 0.25 M which gives around 50% inhibition of rhodanese activity. Addition of sodium phosphate at the same concentration results in about 65% inhibition. Sulfite strongly inhibits PspE activity (1 mM sodium sulfite resulted in more than 50% inhibition of rhodanese activity).2 Publications

Kineticsi

  1. KM=2.7 mM for thiosulfate (at pH 8.6 and at 25 degrees Celsius)2 Publications
  2. KM=10 mM for dithiothreitol (at pH 8.6 and at 25 degrees Celsius)2 Publications
  3. KM=32 mM for cyanide (at pH 8.6 and at 25 degrees Celsius)2 Publications
  1. Vmax=410 µmol/min/mg enzyme toward cyanide (at pH 8.6 and at 25 degrees Celsius)2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei67 – 671Cysteine persulfide intermediate
Sitei93 – 931May be important for providing the necessary conformational flexibility for enzymatic catalysis

GO - Molecular functioni

  • thiosulfate sulfurtransferase activity Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Stress response

Enzyme and pathway databases

BioCyciEcoCyc:EG10780-MONOMER.
ECOL316407:JW1301-MONOMER.
MetaCyc:EG10780-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Thiosulfate sulfurtransferase PspE (EC:2.8.1.1)
Short name:
TST
Alternative name(s):
Phage shock protein E
Gene namesi
Name:pspE
Ordered Locus Names:b1308, JW1301
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10780. pspE.

Subcellular locationi

GO - Cellular componenti

  • outer membrane-bounded periplasmic space Source: EcoCyc
  • periplasmic space Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Chaini20 – 10485Thiosulfate sulfurtransferase PspEPRO_0000030431Add
BLAST

Proteomic databases

EPDiP23857.
PaxDbiP23857.
PRIDEiP23857.

Expressioni

Inductioni

By heat, ethanol, osmotic shock and infection by filamentous bacteriophages. Expression is positively regulated by cyclic AMP-cAMP receptor protein (cAMP-CRP). Expressed at higher levels during growth on glycerol, acetate or proline as carbon source relative to expression during growth on glucose.3 Publications

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi4263234. 400 interactions.
DIPiDIP-10591N.
IntActiP23857. 3 interactions.
STRINGi511145.b1308.

Structurei

Secondary structure

1
104
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi21 – 255Combined sources
Helixi29 – 324Combined sources
Beta strandi35 – 373Combined sources
Beta strandi40 – 423Combined sources
Helixi45 – 5511Combined sources
Beta strandi61 – 7010Combined sources
Helixi71 – 8212Combined sources
Beta strandi86 – 938Combined sources
Turni94 – 963Combined sources
Beta strandi101 – 1033Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JTQNMR-A20-104[»]
2JTRNMR-A20-104[»]
2JTSNMR-A20-104[»]
ProteinModelPortaliP23857.
SMRiP23857. Positions 20-104.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23857.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 10485RhodanesePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 rhodanese domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105K8Z. Bacteria.
COG0607. LUCA.
HOGENOMiHOG000247776.
InParanoidiP23857.
KOiK03972.
OMAiANEIWID.
OrthoDBiEOG68DD6K.
PhylomeDBiP23857.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
InterProiIPR014323. Phageshock_PspE.
IPR001763. Rhodanese-like_dom.
[Graphical view]
PfamiPF00581. Rhodanese. 1 hit.
[Graphical view]
SMARTiSM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMiSSF52821. SSF52821. 1 hit.
TIGRFAMsiTIGR02981. phageshock_pspE. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P23857-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFKKGLLALA LVFSLPVFAA EHWIDVRVPE QYQQEHVQGA INIPLKEVKE
60 70 80 90 100
RIATAVPDKN DTVKVYCNAG RQSGQAKEIL SEMGYTHVEN AGGLKDIAMP

KVKG
Length:104
Mass (Da):11,475
Last modified:November 1, 1991 - v1
Checksum:i52D52FB8FC0CC943
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57560 Genomic DNA. Translation: CAA40793.1.
U00096 Genomic DNA. Translation: AAC74390.1.
AP009048 Genomic DNA. Translation: BAA14877.1.
PIRiS17125.
RefSeqiNP_415824.1. NC_000913.3.
WP_000473109.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74390; AAC74390; b1308.
BAA14877; BAA14877; BAA14877.
GeneIDi945652.
KEGGiecj:JW1301.
eco:b1308.
PATRICi32117888. VBIEscCol129921_1364.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57560 Genomic DNA. Translation: CAA40793.1.
U00096 Genomic DNA. Translation: AAC74390.1.
AP009048 Genomic DNA. Translation: BAA14877.1.
PIRiS17125.
RefSeqiNP_415824.1. NC_000913.3.
WP_000473109.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JTQNMR-A20-104[»]
2JTRNMR-A20-104[»]
2JTSNMR-A20-104[»]
ProteinModelPortaliP23857.
SMRiP23857. Positions 20-104.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263234. 400 interactions.
DIPiDIP-10591N.
IntActiP23857. 3 interactions.
STRINGi511145.b1308.

Proteomic databases

EPDiP23857.
PaxDbiP23857.
PRIDEiP23857.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74390; AAC74390; b1308.
BAA14877; BAA14877; BAA14877.
GeneIDi945652.
KEGGiecj:JW1301.
eco:b1308.
PATRICi32117888. VBIEscCol129921_1364.

Organism-specific databases

EchoBASEiEB0773.
EcoGeneiEG10780. pspE.

Phylogenomic databases

eggNOGiENOG4105K8Z. Bacteria.
COG0607. LUCA.
HOGENOMiHOG000247776.
InParanoidiP23857.
KOiK03972.
OMAiANEIWID.
OrthoDBiEOG68DD6K.
PhylomeDBiP23857.

Enzyme and pathway databases

BioCyciEcoCyc:EG10780-MONOMER.
ECOL316407:JW1301-MONOMER.
MetaCyc:EG10780-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP23857.
PROiP23857.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
InterProiIPR014323. Phageshock_PspE.
IPR001763. Rhodanese-like_dom.
[Graphical view]
PfamiPF00581. Rhodanese. 1 hit.
[Graphical view]
SMARTiSM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMiSSF52821. SSF52821. 1 hit.
TIGRFAMsiTIGR02981. phageshock_pspE. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization and sequence of the Escherichia coli stress-induced psp operon."
    Brissette J.L., Weiner L., Ripmaster T.L., Model P.
    J. Mol. Biol. 220:35-48(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, INDUCTION.
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Small genes/gene-products in Escherichia coli K-12."
    Wasinger V.C., Humphery-Smith I.
    FEMS Microbiol. Lett. 169:375-382(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 20-29.
    Strain: K12.
  6. "PspE (phage-shock protein E) of Escherichia coli is a rhodanese."
    Adams H., Teertstra W., Koster M., Tommassen J.
    FEBS Lett. 518:173-176(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, INDUCTION, BIOPHYSICOCHEMICAL PROPERTIES.
  7. "Biochemical and genetic characterization of pspE and glpE, two single-domain sulfurtransferases of Escherichia coli."
    Cheng H., Donahue J.L., Battle S.E., Ray W.K., Larson T.J.
    Open Microbiol. J. 2:18-28(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, REACTION MECHANISM, SUBSTRATE SPECIFICITY, INDUCTION, ENZYME REGULATION.
    Strain: K12 / MG1655 / ATCC 47076.
  8. "Solution structures and backbone dynamics of Escherichia coli rhodanese PspE in its sulfur-free and persulfide-intermediate forms: implications for the catalytic mechanism of rhodanese."
    Li H., Yang F., Kang X., Xia B., Jin C.
    Biochemistry 47:4377-4385(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, SUBUNIT.

Entry informationi

Entry nameiPSPE_ECOLI
AccessioniPrimary (citable) accession number: P23857
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: March 16, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Catalysis proceeds by a classical ping-pong bi-bi reaction mechanism, whereby a covalent enzyme-sulfur intermediate is formed on the active site cysteine.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.