spy

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
Inferred from direct assayⁱ
- 26619265
chaperone-mediated protein folding
Source: EcoCyc
Inferred from direct assayⁱ
- 21317898

Complete GO annotation...

Keywordsⁱ

Molecular function	Chaperone
Biological process	Stress response

Enzyme and pathway databases

BioCycⁱ	EcoCyc:G6939-MONOMER.

BioCycⁱ

EcoCyc:G6939-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
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG13490. spy.

EcoGeneⁱ

EG13490. spy.

Subcellular locationⁱ

Periplasm
3 Publications
Manual assertion based on experiment inⁱ
- Ref.1
  "A new periplasmic protein of Escherichia coli which is synthesized in spheroplasts but not in intact cells."
  Hagenmaier S., Stierhof Y.-D., Henning U.
  J. Bacteriol. 179:2073-2076(1997) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 24-40, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INDUCTION, DISRUPTION PHENOTYPE.
- Ref.5
  "Identification of a novel transcription regulator from Proteus mirabilis, PMTR, revealed a possible role of YJAI protein in balancing zinc in Escherichia coli."
  Noll M., Petrukhin K., Lutsenko S.
  J. Biol. Chem. 273:21393-21401(1998) [PubMed] [Europe PMC] [Abstract]
  Cited for: PROTEIN SEQUENCE OF 24-38, SUBCELLULAR LOCATION, INDUCTION BY ZINC.
- Ref.8
  "Genetic selection designed to stabilize proteins uncovers a chaperone called Spy."
  Quan S., Koldewey P., Tapley T., Kirsch N., Ruane K.M., Pfizenmaier J., Shi R., Hofmann S., Foit L., Ren G., Jakob U., Xu Z., Cygler M., Bardwell J.C.
  Nat. Struct. Mol. Biol. 18:262-269(2011) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, SUBSTRATE-BINDING, SUBCELLULAR LOCATION, INDUCTION, DISRUPTION PHENOTYPE.

GO - Cellular componentⁱ

outer membrane-bounded periplasmic space
Source: EcoCyc
Inferred from direct assayⁱ
- 9068658

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 key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	48	Q → R: Increased chaperone activity, substrate affinity and chaperone flexibility. 1 Publication	1
Mutagenesisⁱ	55	L → P: Increased chaperone activity, substrate affinity and chaperone flexibility. 1 Publication	1
Mutagenesisⁱ	72	Q → L: Increased chaperone activity, substrate affinity and chaperone flexibility, despite decreased Spy stability. 1 Publication	1
Mutagenesisⁱ	119	H → L: Increased chaperone activity, substrate affinity and chaperone flexibility. 1 Publication	1
Mutagenesisⁱ	123	Q → L: Increased chaperone activity, substrate affinity and chaperone flexibility. 1 Publication	1
Mutagenesisⁱ	138	F → I or L: Increased chaperone activity, substrate affinity and chaperone flexibility. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Signal peptideⁱ	1 – 23	2 PublicationsAdd BLAST		23
ChainⁱPRO_0000022405	24 – 161	Periplasmic chaperone SpyAdd BLAST		138

Proteomic databases

EPDⁱ	P77754.
PaxDbⁱ	P77754.
PRIDEⁱ	P77754.

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

BioGridⁱ	4262237. 141 interactors.
Database of interacting proteins More...DIPⁱ	DIP-10914N.
IntActⁱ	P77754. 2 interactors.
STRINGⁱ	511145.b1743.

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Show more details

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	53 – 55	Combined sources	3
Helixⁱ	59 – 69	Combined sources	11
Helixⁱ	81 – 91	Combined sources	11
Beta strandⁱ	92 – 95	Combined sources	4
Helixⁱ	98 – 106	Combined sources	9
Helixⁱ	109 – 127	Combined sources	19
Helixⁱ	132 – 143	Combined sources	12

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	5INA	X-ray	1.79	A/B	52-147	[»]
	5IOA	X-ray	1.87	A/B	52-147	[»]
	5IOE	X-ray	1.87	A/B	52-147	[»]
	5IOG	X-ray	1.77	A/B	52-147	[»]
ProteinModelPortalⁱ	P77754.
SMRⁱ	P77754.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

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

eggNOGⁱ	ENOG4108SPG. Bacteria. COG3678. LUCA.
HOGENOMⁱ	HOG000285733.
InParanoidⁱ	P77754.
PhylomeDBⁱ	P77754.

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd09916. CpxP_like. 1 hit.
InterProⁱ	View protein in InterPro IPR012899. LTXXQ.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF07813. LTXXQ. 1 hit.
PIRSFⁱ	PIRSF034445. CpxP_Spy. 1 hit.

Sequenceⁱ

Sequence statusⁱ: Complete.

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

P77754-1 [UniParc]FASTA Add 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 key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	38	M → MM AA sequence (PubMed:9068658).Curated		1

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.
PIRⁱ	G64933.
NCBI Reference Sequences More...RefSeqⁱ	NP_416257.1. NC_000913.3. WP_001228984.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaⁱ	AAC74813; AAC74813; b1743. BAA15531; BAA15531; BAA15531.
GeneIDⁱ	946253.
KEGGⁱ	ecj:JW1732. eco:b1743.
PATRICⁱ	fig\|1411691.4.peg.513.

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.
PIRⁱ	G64933.
NCBI Reference Sequences More...RefSeqⁱ	NP_416257.1. NC_000913.3. WP_001228984.1. NZ_LN832404.1.

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	5INA	X-ray	1.79	A/B	52-147	[»]
	5IOA	X-ray	1.87	A/B	52-147	[»]
	5IOE	X-ray	1.87	A/B	52-147	[»]
	5IOG	X-ray	1.77	A/B	52-147	[»]
ProteinModelPortalⁱ	P77754.
SMRⁱ	P77754.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4262237. 141 interactors.
Database of interacting proteins More...DIPⁱ	DIP-10914N.
IntActⁱ	P77754. 2 interactors.
STRINGⁱ	511145.b1743.

Proteomic databases

EPDⁱ	P77754.
PaxDbⁱ	P77754.
PRIDEⁱ	P77754.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC74813; AAC74813; b1743. BAA15531; BAA15531; BAA15531.
GeneIDⁱ	946253.
KEGGⁱ	ecj:JW1732. eco:b1743.
PATRICⁱ	fig\|1411691.4.peg.513.

Organism-specific databases

EchoBASEⁱ	EB3263.
EcoGeneⁱ	EG13490. spy.

Phylogenomic databases

eggNOGⁱ	ENOG4108SPG. Bacteria. COG3678. LUCA.
HOGENOMⁱ	HOG000285733.
InParanoidⁱ	P77754.
PhylomeDBⁱ	P77754.

Enzyme and pathway databases

BioCycⁱ	EcoCyc:G6939-MONOMER.

BioCycⁱ

EcoCyc:G6939-MONOMER.

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:P77754.

PROⁱ

PR:P77754.

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd09916. CpxP_like. 1 hit.
InterProⁱ	View protein in InterPro IPR012899. LTXXQ.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF07813. LTXXQ. 1 hit.
PIRSFⁱ	PIRSF034445. CpxP_Spy. 1 hit.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	SPY_ECOLI
Accessionⁱ	P77754Primary (citable) accession number: P77754
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
	Last sequence update:	February 1, 1997
	Last modified:	June 7, 2017
	This is version 111 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

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

Documents

Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
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.

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P77754 (SPY_ECOLI)

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Periplasmic chaperone Spy

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

Functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequenceⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ