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Protein

Antitoxin PrlF

Gene

prlF

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

Functioni

Antitoxin component of a toxin-antitoxin (TA) module. Labile antitoxin that binds to the YhaV toxin and neutralizes its ribonuclease activity. Also acts as a transcription factor. The YhaV/PrlF complex binds the prlF-yhaV operon, probably negatively regulating its expression.1 Publication
Negatively regulates its own expression as well as relieving the export block imposed by high-level synthesis of the LamB-LacZ hybrid protein. Overexpression leads to increased doubling time and also suppresses a htrA (degP) null phenotype.1 Publication

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • enzyme binding Source: EcoCyc
  • identical protein binding Source: EcoCyc
  • toxin-antitoxin pair type II binding Source: EcoCyc
  • transcription factor activity, sequence-specific DNA binding Source: EcoCyc

GO - Biological processi

  • negative regulation of transcription, DNA-templated Source: EcoCyc
  • regulation of cell growth Source: EcoCyc
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10955-MONOMER.
ECOL316407:JW3098-MONOMER.
MetaCyc:EG10955-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Antitoxin PrlF
Alternative name(s):
HtrA suppressor protein SohA
Gene namesi
Name:prlF
Synonyms:sohA
Ordered Locus Names:b3129, JW3098
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10955. prlF.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Not essential.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi91 – 11121QGKKL…IGDDE → HSTRKETCRWHGRQH in prlF1; suppresses overproduction lethality of lamB-lacZ gene fusions, leads to decreased beta-galactosidase activity. Partially alleviates YhaV toxic activity. 1 PublicationAdd
BLAST

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 111111Antitoxin PrlFPRO_0000072033Add
BLAST

Proteomic databases

PaxDbiP15373.

Interactioni

Subunit structurei

Homodimer; forms a complex with YhaV with stoichiometry PrlF(2)-YhaV4, possibly as a YhaV(2)-PrlF(2)-YhaV2 complex like the MazFE complex. This complex is seen to dimerize in solution.1 Publication

GO - Molecular functioni

  • enzyme binding Source: EcoCyc
  • identical protein binding Source: EcoCyc
  • toxin-antitoxin pair type II binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4259492. 399 interactions.
IntActiP15373. 6 interactions.
STRINGi511145.b3129.

Structurei

3D structure databases

ProteinModelPortaliP15373.
SMRiP15373. Positions 12-54.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 5948SpoVT-AbrBPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 SpoVT-AbrB domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105ZEG. Bacteria.
COG2002. LUCA.
HOGENOMiHOG000229555.
InParanoidiP15373.
KOiK19156.
OMAiDKICYTI.
OrthoDBiEOG6GBMFR.
PhylomeDBiP15373.

Family and domain databases

InterProiIPR031848. PrlF_antitoxin.
IPR007159. SpoVT-AbrB_dom.
[Graphical view]
PfamiPF15937. PrlF_antitoxin. 1 hit.
[Graphical view]
PROSITEiPS51740. SPOVT_ABRB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P15373-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPANARSHAV LTTESKVTIR GQTTIPAPVR EALKLKPGQD SIHYEILPGG
60 70 80 90 100
QVFMCRLGDE QEDHTMNAFL RFLDADIQNN PQKTRPFNIQ QGKKLVAGMD
110
VNIDDEIGDD E
Length:111
Mass (Da):12,359
Last modified:April 1, 1990 - v1
Checksum:i5FC0D5FF43F75D8A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30178 Genomic DNA. Translation: AAA24638.1.
M32358 Genomic DNA. Translation: AAA24418.1.
U18997 Genomic DNA. Translation: AAA57932.1.
U00096 Genomic DNA. Translation: AAC76163.1.
AP009048 Genomic DNA. Translation: BAE77176.1.
PIRiA35137.
RefSeqiNP_417598.1. NC_000913.3.
WP_001307405.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76163; AAC76163; b3129.
BAE77176; BAE77176; BAE77176.
GeneIDi947639.
KEGGiecj:JW3098.
eco:b3129.
PATRICi32121674. VBIEscCol129921_3223.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30178 Genomic DNA. Translation: AAA24638.1.
M32358 Genomic DNA. Translation: AAA24418.1.
U18997 Genomic DNA. Translation: AAA57932.1.
U00096 Genomic DNA. Translation: AAC76163.1.
AP009048 Genomic DNA. Translation: BAE77176.1.
PIRiA35137.
RefSeqiNP_417598.1. NC_000913.3.
WP_001307405.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP15373.
SMRiP15373. Positions 12-54.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259492. 399 interactions.
IntActiP15373. 6 interactions.
STRINGi511145.b3129.

Proteomic databases

PaxDbiP15373.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76163; AAC76163; b3129.
BAE77176; BAE77176; BAE77176.
GeneIDi947639.
KEGGiecj:JW3098.
eco:b3129.
PATRICi32121674. VBIEscCol129921_3223.

Organism-specific databases

EchoBASEiEB0948.
EcoGeneiEG10955. prlF.

Phylogenomic databases

eggNOGiENOG4105ZEG. Bacteria.
COG2002. LUCA.
HOGENOMiHOG000229555.
InParanoidiP15373.
KOiK19156.
OMAiDKICYTI.
OrthoDBiEOG6GBMFR.
PhylomeDBiP15373.

Enzyme and pathway databases

BioCyciEcoCyc:EG10955-MONOMER.
ECOL316407:JW3098-MONOMER.
MetaCyc:EG10955-MONOMER.

Miscellaneous databases

PROiP15373.

Family and domain databases

InterProiIPR031848. PrlF_antitoxin.
IPR007159. SpoVT-AbrB_dom.
[Graphical view]
PfamiPF15937. PrlF_antitoxin. 1 hit.
[Graphical view]
PROSITEiPS51740. SPOVT_ABRB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Increased expression of the bifunctional protein PrlF suppresses overproduction lethality associated with exported beta-galactosidase hybrid proteins in Escherichia coli."
    Kiino D.R., Phillips G.J., Silhavy T.J.
    J. Bacteriol. 172:185-192(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUPPRESSION OF JAMMED SECRETION MACHINERY, MUTAGENESIS OF 91-GLN--GLU-111, DISRUPTION PHENOTYPE.
    Strain: K12.
  2. "Identification, cloning, and characterization of the Escherichia coli sohA gene, a suppressor of the htrA (degP) null phenotype."
    Baird L., Georgopoulos C.
    J. Bacteriol. 172:1587-1594(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, SUPPRESSION OF AN HTRA NULL MUTANT.
    Strain: K12.
  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. "prlF and yhaV encode a new toxin-antitoxin system in Escherichia coli."
    Schmidt O., Schuenemann V.J., Hand N.J., Silhavy T.J., Martin J., Lupas A.N., Djuranovic S.
    J. Mol. Biol. 372:894-905(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN ANTITOXIN, SUBUNIT, DNA-BINDING, OPERON STRUCTURE.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "mRNA interferases, sequence-specific endoribonucleases from the toxin-antitoxin systems."
    Yamaguchi Y., Inouye M.
    Prog. Mol. Biol. Transl. Sci. 85:467-500(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiPRLF_ECOLI
AccessioniPrimary (citable) accession number: P15373
Secondary accession number(s): Q2M980
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: May 11, 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. 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.