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Protein

Periplasmic chaperone Spy

Gene

spy

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

Functioni

An ATP-independent periplasmic chaperone, decreases protein aggregation and helps protein refolding. Binds substrate over a large region of its convex inner surface (PubMed:21317898, PubMed:24497545). Substrate protein folds while it is bound to chaperone (PubMed:26619265). Increasing Spy flexibility increases its substrate affinity and overall chaperone activity (shown for 3 different substrates) (PubMed:24497545). Protects proteins in vitro against tannin inactivation; tannins have antimicrobial activity (PubMed:21317898). Overexpression enhances the stability of otherwise unstable periplasmic proteins (PubMed:21317898).3 Publications

GO - Biological processi

  • ATP-independent chaperone mediated protein folding Source: UniProtKB
  • chaperone-mediated protein folding Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Enzyme and pathway databases

BioCyciEcoCyc:G6939-MONOMER.
ECOL316407:JW1732-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Periplasmic chaperone Spy1 Publication
Alternative name(s):
Spheroplast protein Y1 Publication
Gene namesi
Name:spy1 Publication
Ordered Locus Names:b1743, JW1732
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13490. spy.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Disruption phenotypei

No observed growth phenotype (PubMed:9068658). Increased levels of degP and rpoH transcription; may induce the sigma factor E regulon (rpoE) (PubMed:10972835). Loss of about 50% of periplasmic alkaline phosphatase activity; very sensitive to tannic acid (PubMed:21317898).3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi48Q → R: Increased chaperone activity, substrate affinity and chaperone flexibility. 1 Publication1
Mutagenesisi55L → P: Increased chaperone activity, substrate affinity and chaperone flexibility. 1 Publication1
Mutagenesisi72Q → L: Increased chaperone activity, substrate affinity and chaperone flexibility, despite decreased Spy stability. 1 Publication1
Mutagenesisi119H → L: Increased chaperone activity, substrate affinity and chaperone flexibility. 1 Publication1
Mutagenesisi123Q → L: Increased chaperone activity, substrate affinity and chaperone flexibility. 1 Publication1
Mutagenesisi138F → I or L: Increased chaperone activity, substrate affinity and chaperone flexibility. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 232 PublicationsAdd BLAST23
ChainiPRO_000002240524 – 161Periplasmic chaperone SpyAdd BLAST138

Proteomic databases

EPDiP77754.
PaxDbiP77754.
PRIDEiP77754.

Expressioni

Developmental stagei

Produced abundantly in spheroplasts, not detected in intact cells.1 Publication

Inductioni

Induced by many sorts of periplasmic stress. Produced upon spheroplast formation, not induced by growth in 0.5 M sucrose or 0.35 M NaCl, nor by mutants that have a leaky periplasmic space (at protein level) (PubMed:9068658). Induction is partially dependent on the Cpx envelope stress response encoded by cpxA-cpxR; does not depend on sigma factor E (rpoE) (PubMed:10972835). Induction is also partially dependent on the Bae envelope stress response encoded by baeS-baeR; cpx and baeS effects are independent (PubMed:12354228). Overexpression of P pili protein PapG induces spy expression via both Cpx and Bae, overexpression of outer membrane protein NlpE induces spy via only Cpx whereas indole induces spy expression only via Bae (PubMed:12354228). Induced by 1 mM zinc (at protein level) (PubMed:9694902), via Bae, which also regulates ethanol induction of spy (PubMed:24999585). Induced by copper via Cpx (PubMed:24999585). Induced by tannic acid (to 25% of total periplasmic protein), butanol (to 20% total periplasmic protein) and ethanol (to 5% total periplasmic protein) (at protein level) (PubMed:21317898).6 Publications

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi4262237. 141 interactors.
DIPiDIP-10914N.
IntActiP77754. 2 interactors.
STRINGi511145.b1743.

Structurei

Secondary structure

1161
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi53 – 55Combined sources3
Helixi59 – 69Combined sources11
Helixi81 – 91Combined sources11
Beta strandi92 – 95Combined sources4
Helixi98 – 106Combined sources9
Helixi109 – 127Combined sources19
Helixi132 – 143Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5INAX-ray1.79A/B52-147[»]
5IOAX-ray1.87A/B52-147[»]
5IOEX-ray1.87A/B52-147[»]
5IOGX-ray1.77A/B52-147[»]
ProteinModelPortaliP77754.
SMRiP77754.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

Has an elongated cradle shape.By similarity1 Publication

Sequence similaritiesi

Belongs to the CpxP/Spy family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4108SPG. Bacteria.
COG3678. LUCA.
HOGENOMiHOG000285733.
InParanoidiP77754.
OMAiKMYNLLT.
PhylomeDBiP77754.

Family and domain databases

CDDicd09916. CpxP_like. 1 hit.
InterProiIPR012899. LTXXQ.
[Graphical view]
PfamiPF07813. LTXXQ. 1 hit.
[Graphical view]
PIRSFiPIRSF034445. CpxP_Spy. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P77754-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKLTALFVA STLALGAANL AHAADTTTAA PADAKPMMHH KGKFGPHQDM
60 70 80 90 100
MFKDLNLTDA QKQQIREIMK GQRDQMKRPP LEERRAMHDI IASDTFDKVK
110 120 130 140 150
AEAQIAKMEE QRKANMLAHM ETQNKIYNIL TPEQKKQFNA NFEKRLTERP
160
AAKGKMPATA E
Length:161
Mass (Da):18,199
Last modified:February 1, 1997 - v1
Checksum:iB4733B967FC5F5BD
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti38M → MM AA sequence (PubMed:9068658).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y07714 Genomic DNA. Translation: CAA68986.1.
U00096 Genomic DNA. Translation: AAC74813.1.
AP009048 Genomic DNA. Translation: BAA15531.1.
PIRiG64933.
RefSeqiNP_416257.1. NC_000913.3.
WP_001228984.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74813; AAC74813; b1743.
BAA15531; BAA15531; BAA15531.
GeneIDi946253.
KEGGiecj:JW1732.
eco:b1743.
PATRICi32118795. VBIEscCol129921_1815.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y07714 Genomic DNA. Translation: CAA68986.1.
U00096 Genomic DNA. Translation: AAC74813.1.
AP009048 Genomic DNA. Translation: BAA15531.1.
PIRiG64933.
RefSeqiNP_416257.1. NC_000913.3.
WP_001228984.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5INAX-ray1.79A/B52-147[»]
5IOAX-ray1.87A/B52-147[»]
5IOEX-ray1.87A/B52-147[»]
5IOGX-ray1.77A/B52-147[»]
ProteinModelPortaliP77754.
SMRiP77754.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262237. 141 interactors.
DIPiDIP-10914N.
IntActiP77754. 2 interactors.
STRINGi511145.b1743.

Proteomic databases

EPDiP77754.
PaxDbiP77754.
PRIDEiP77754.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74813; AAC74813; b1743.
BAA15531; BAA15531; BAA15531.
GeneIDi946253.
KEGGiecj:JW1732.
eco:b1743.
PATRICi32118795. VBIEscCol129921_1815.

Organism-specific databases

EchoBASEiEB3263.
EcoGeneiEG13490. spy.

Phylogenomic databases

eggNOGiENOG4108SPG. Bacteria.
COG3678. LUCA.
HOGENOMiHOG000285733.
InParanoidiP77754.
OMAiKMYNLLT.
PhylomeDBiP77754.

Enzyme and pathway databases

BioCyciEcoCyc:G6939-MONOMER.
ECOL316407:JW1732-MONOMER.

Miscellaneous databases

PROiP77754.

Family and domain databases

CDDicd09916. CpxP_like. 1 hit.
InterProiIPR012899. LTXXQ.
[Graphical view]
PfamiPF07813. LTXXQ. 1 hit.
[Graphical view]
PIRSFiPIRSF034445. CpxP_Spy. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSPY_ECOLI
AccessioniPrimary (citable) accession number: P77754
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: November 2, 2016
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.