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Protein

Phage shock protein A

Gene

pspA

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. PspA negatively regulates expression of the pspABCDE promoter and of pspG through negative regulation of the psp-specific transcriptional activator PspF. Is also required for membrane integrity, efficient translocation and maintenance of the proton motive force.5 Publications

GO - Molecular functioni

  • identical protein binding Source: EcoCyc
  • phospholipid binding Source: EcoCyc

GO - Biological processi

  • negative regulation of sequence-specific DNA binding transcription factor activity Source: EcoCyc
  • phage shock Source: EcoliWiki
  • response to heat Source: EcoliWiki
Complete GO annotation...

Keywords - Biological processi

Stress response

Enzyme and pathway databases

BioCyciEcoCyc:EG10776-MONOMER.
ECOL316407:JW1297-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Phage shock protein A
Gene namesi
Name:pspA
Ordered Locus Names:b1304, JW1297
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10776. pspA.

Subcellular locationi

GO - Cellular componenti

  • cell pole Source: EcoCyc
  • cytosol Source: EcoCyc
  • extrinsic component of cytoplasmic side of plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Disruption phenotypei

Not required for induction of, or recovery from, contact-dependent growth inhibition (CDI).1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 222221Phage shock protein APRO_0000166292Add
BLAST

Proteomic databases

EPDiP0AFM6.
PaxDbiP0AFM6.
PRIDEiP0AFM6.

Expressioni

Inductioni

By heat, ethanol, osmotic shock and infection by filamentous bacteriophages (PubMed:1712397). Induced during contact-dependent growth inhibition (CDI), but not during recovery from CDI (PubMed:19124575).2 Publications

Interactioni

Subunit structurei

Exists in at least two different oligomeric assemblies. Regulatory function involves the formation of a complex with PspF, which is composed of around 6 PspF subunits and 6 PspA subunits. Maintenance of membrane integrity involves the formation of a 36-mer ring complex. Interacts with PspB and PspC.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
crlP242511EBI-1123459,EBI-1114986

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4262874. 304 interactions.
DIPiDIP-10587N.
IntActiP0AFM6. 4 interactions.
STRINGi511145.b1304.

Structurei

Secondary structure

1
222
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 115Combined sources
Helixi25 – 8056Combined sources
Helixi84 – 14158Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4WHEX-ray1.80A1-144[»]
ProteinModelPortaliP0AFM6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili30 – 187158Sequence analysisAdd
BLAST
Coiled coili204 – 22219Sequence analysisAdd
BLAST

Domaini

All four putative helical domains of PspA are critical for the formation of the 36-mer. In contrast, not all four helical domains are required for the formation of the inhibitory PspA-PspF complex.1 Publication

Sequence similaritiesi

Belongs to the PspA/IM30 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG41087YS. Bacteria.
COG1842. LUCA.
HOGENOMiHOG000227267.
InParanoidiP0AFM6.
KOiK03969.
OMAiQKTIIMR.
OrthoDBiEOG6H7FJ5.
PhylomeDBiP0AFM6.

Family and domain databases

InterProiIPR014319. Phageshock_PspA.
IPR007157. PspA_IM30.
[Graphical view]
PfamiPF04012. PspA_IM30. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02977. phageshock_pspA. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P0AFM6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGIFSRFADI VNANINALLE KAEDPQKLVR LMIQEMEDTL VEVRSTSARA
60 70 80 90 100
LAEKKQLTRR IEQASAREVE WQEKAELALL KEREDLARAA LIEKQKLTDL
110 120 130 140 150
IKSLEHEVTL VDDTLARMKK EIGELENKLS ETRARQQALM LRHQAANSSR
160 170 180 190 200
DVRRQLDSGK LDEAMARFES FERRIDQMEA EAESHSFGKQ KSLDDQFAEL
210 220
KADDAISEQL AQLKAKMKQD NQ
Length:222
Mass (Da):25,493
Last modified:January 23, 2007 - v2
Checksum:iEAC29290406E5053
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti182 – 1821A → R in CAA40789 (PubMed:1712397).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57560 Genomic DNA. Translation: CAA40789.1.
U00096 Genomic DNA. Translation: AAC74386.1.
AP009048 Genomic DNA. Translation: BAA14873.1.
PIRiC64879.
RefSeqiNP_415820.1. NC_000913.3.
WP_000511025.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74386; AAC74386; b1304.
BAA14873; BAA14873; BAA14873.
GeneIDi945887.
KEGGiecj:JW1297.
eco:b1304.
PATRICi32117880. VBIEscCol129921_1360.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X57560 Genomic DNA. Translation: CAA40789.1.
U00096 Genomic DNA. Translation: AAC74386.1.
AP009048 Genomic DNA. Translation: BAA14873.1.
PIRiC64879.
RefSeqiNP_415820.1. NC_000913.3.
WP_000511025.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4WHEX-ray1.80A1-144[»]
ProteinModelPortaliP0AFM6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262874. 304 interactions.
DIPiDIP-10587N.
IntActiP0AFM6. 4 interactions.
STRINGi511145.b1304.

Proteomic databases

EPDiP0AFM6.
PaxDbiP0AFM6.
PRIDEiP0AFM6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74386; AAC74386; b1304.
BAA14873; BAA14873; BAA14873.
GeneIDi945887.
KEGGiecj:JW1297.
eco:b1304.
PATRICi32117880. VBIEscCol129921_1360.

Organism-specific databases

EchoBASEiEB0769.
EcoGeneiEG10776. pspA.

Phylogenomic databases

eggNOGiENOG41087YS. Bacteria.
COG1842. LUCA.
HOGENOMiHOG000227267.
InParanoidiP0AFM6.
KOiK03969.
OMAiQKTIIMR.
OrthoDBiEOG6H7FJ5.
PhylomeDBiP0AFM6.

Enzyme and pathway databases

BioCyciEcoCyc:EG10776-MONOMER.
ECOL316407:JW1297-MONOMER.

Miscellaneous databases

PROiP0AFM6.

Family and domain databases

InterProiIPR014319. Phageshock_PspA.
IPR007157. PspA_IM30.
[Graphical view]
PfamiPF04012. PspA_IM30. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02977. phageshock_pspA. 1 hit.
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], PARTIAL PROTEIN SEQUENCE, FUNCTION, 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. "Inhibition of lipid biosynthesis induces the expression of the pspA gene."
    Bergler H., Abraham D., Aschauer H., Turnowsky F.
    Microbiology 140:1937-1944(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
  6. "Appearance of a stress-response protein, phage-shock protein A, in Escherichia coli exposed to hydrophobic organic solvents."
    Kobayashi H., Yamamoto M., Aono R.
    Microbiology 144:353-359(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-20.
    Strain: K12 / JA300 / ATCC 33588 / DSM 4776 / NCIMB 12220.
  7. "Involvement of stress protein PspA (phage shock protein A) of Escherichia coli in maintenance of the protonmotive force under stress conditions."
    Kleerebezem M., Crielaard W., Tommassen J.
    EMBO J. 15:162-171(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  9. "The PspA protein of Escherichia coli is a negative regulator of sigma(54)-dependent transcription."
    Dworkin J., Jovanovic G., Model P.
    J. Bacteriol. 182:311-319(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Interactions between phage-shock proteins in Escherichia coli."
    Adams H., Teertstra W., Demmers J., Boesten R., Tommassen J.
    J. Bacteriol. 185:1174-1180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PSPB AND PSPC.
    Strain: K12.
  11. "Organization of the AAA(+) adaptor protein PspA is an oligomeric ring."
    Hankamer B.D., Elderkin S.L., Buck M., Nield J.
    J. Biol. Chem. 279:8862-8866(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  12. "Identification of a new member of the phage shock protein response in Escherichia coli, the phage shock protein G (PspG)."
    Lloyd L.J., Jones S.E., Jovanovic G., Gyaneshwar P., Rolfe M.D., Thompson A., Hinton J.C., Buck M.
    J. Biol. Chem. 279:55707-55714(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: K12 / MG1655 / ATCC 47076.
  13. "Contact-dependent growth inhibition causes reversible metabolic downregulation in Escherichia coli."
    Aoki S.K., Webb J.S., Braaten B.A., Low D.A.
    J. Bacteriol. 191:1777-1786(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY CDI, DISRUPTION PHENOTYPE.
    Strain: K12 / MC1061 / ATCC 53338 / DSM 7140.
  14. "A lower-order oligomer form of phage shock protein A (PspA) stably associates with the hexameric AAA(+) transcription activator protein PspF for negative regulation."
    Joly N., Burrows P.C., Engl C., Jovanovic G., Buck M.
    J. Mol. Biol. 394:764-775(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, INTERACTION WITH PSPF, DOMAIN.
  15. "In vivo localizations of membrane stress controllers PspA and PspG in Escherichia coli."
    Engl C., Jovanovic G., Lloyd L.J., Murray H., Spitaler M., Ying L., Errington J., Buck M.
    Mol. Microbiol. 73:382-396(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
    Strain: K12 / MG1655 / ATCC 47076.

Entry informationi

Entry nameiPSPA_ECOLI
AccessioniPrimary (citable) accession number: P0AFM6
Secondary accession number(s): P23853, P76040, P77363
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 81 of the entry and version 2 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.