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Protein

Double-strand break reduction protein

Gene

rcbA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Helps to maintain the integrity of the chromosome by lowering the steady-state level of double strand breaks (PubMed:22343303). This region of DNA acts as an antitoxin to toxin RalR, a DNase, but it seems to be sRNA RalA that has the antitoxin activity and not this putative protein. Therefore the identity of this as a protein-coding gene has been cast into doubt (PubMed:24748661).2 Publications

GO - Biological processi

  • DNA metabolic process Source: EcoCyc
  • response to antibiotic Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Antibiotic resistance

Enzyme and pathway databases

BioCyciEcoCyc:EG11901-MONOMER.
ECOL316407:JW1341-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Double-strand break reduction protein1 Publication
Gene namesi
Name:rcbA1 Publication
Synonyms:ydaC
Ordered Locus Names:b1347, JW1341
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11901. ydaC.

Pathology & Biotechi

Disruption phenotypei

Mutants show increased numbers of double-strand breaks (PubMed:22343303). The single ralR and double ralR-ralA mutant have increased sensitivity to the antibiotic fosfomycin.2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1M → T: No protein should be translated, DNA region still acts as an antitoxin to RalR. 1 Publication1
Mutagenesisi9 – 69Missing : No protein should be translated, DNA region still acts as an antitoxin to RalR. 1 PublicationAdd BLAST61

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001689011 – 69Double-strand break reduction proteinAdd BLAST69

Proteomic databases

PaxDbiP33230.
PRIDEiP33230.

Interactioni

Protein-protein interaction databases

BioGridi4261948. 13 interactors.
DIPiDIP-11619N.
IntActiP33230. 4 interactors.
STRINGi511145.b1347.

Structurei

3D structure databases

ProteinModelPortaliP33230.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiENOG41070YT. Bacteria.
ENOG410YWP5. LUCA.
HOGENOMiHOG000120153.
KOiK19780.
OMAiTRYSKTK.

Family and domain databases

InterProiIPR009572. DUF1187.
[Graphical view]
PfamiPF06688. DUF1187. 1 hit.
[Graphical view]
ProDomiPD055514. DUF1187. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequencei

Sequence statusi: Complete.

P33230-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYKITATIEK EGGTPTNWTR YSKSKLTKSE CEKMLSGKKE AGVSREQKVK
60
LINFNCEKLQ SSRIALYSN
Length:69
Mass (Da):7,863
Last modified:November 1, 1997 - v2
Checksum:iD65D6454A7FBF4A6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74429.1.
AP009048 Genomic DNA. Translation: BAA14947.1.
L23927 Unassigned DNA. Translation: AAA16181.1.
PIRiF64884.
RefSeqiNP_415863.1. NC_000913.3.
WP_000276809.1. NZ_CP014272.1.

Genome annotation databases

EnsemblBacteriaiAAC74429; AAC74429; b1347.
BAA14947; BAA14947; BAA14947.
GeneIDi947504.
KEGGiecj:JW1341.
eco:b1347.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74429.1.
AP009048 Genomic DNA. Translation: BAA14947.1.
L23927 Unassigned DNA. Translation: AAA16181.1.
PIRiF64884.
RefSeqiNP_415863.1. NC_000913.3.
WP_000276809.1. NZ_CP014272.1.

3D structure databases

ProteinModelPortaliP33230.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261948. 13 interactors.
DIPiDIP-11619N.
IntActiP33230. 4 interactors.
STRINGi511145.b1347.

Proteomic databases

PaxDbiP33230.
PRIDEiP33230.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74429; AAC74429; b1347.
BAA14947; BAA14947; BAA14947.
GeneIDi947504.
KEGGiecj:JW1341.
eco:b1347.

Organism-specific databases

EchoBASEiEB1846.
EcoGeneiEG11901. ydaC.

Phylogenomic databases

eggNOGiENOG41070YT. Bacteria.
ENOG410YWP5. LUCA.
HOGENOMiHOG000120153.
KOiK19780.
OMAiTRYSKTK.

Enzyme and pathway databases

BioCyciEcoCyc:EG11901-MONOMER.
ECOL316407:JW1341-MONOMER.

Miscellaneous databases

PROiP33230.

Family and domain databases

InterProiIPR009572. DUF1187.
[Graphical view]
PfamiPF06688. DUF1187. 1 hit.
[Graphical view]
ProDomiPD055514. DUF1187. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetiSearch...

Entry informationi

Entry nameiRCBA_ECOLI
AccessioniPrimary (citable) accession number: P33230
Secondary accession number(s): P77683
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: November 1, 1997
Last modified: November 2, 2016
This is version 103 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

Complete proteome, Reference proteome

Documents

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

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.