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Protein

Co-chaperone protein DjlA

Gene

djlA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Regulatory DnaK co-chaperone. Direct interaction between DnaK and DjlA is needed for the induction of the wcaABCDE operon, involved in the synthesis of a colanic acid polysaccharide capsule, possibly through activation of the RcsB/RcsC phosphotransfer signaling pathway. The colanic acid capsule may help the bacterium survive conditions outside the host.UniRule annotation3 Publications

GO - Molecular functioni

  • chaperone binding Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Enzyme and pathway databases

BioCyciEcoCyc:EG11570-MONOMER.
ECOL316407:JW0054-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Co-chaperone protein DjlAUniRule annotationCurated
Alternative name(s):
DnaJ-like protein DjlACurated
Gene namesi
Name:djlA1 PublicationUniRule annotation
Synonyms:yabH
Ordered Locus Names:b0055, JW0054
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11570. djlA.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66PeriplasmicUniRule annotation2 Publications
Transmembranei7 – 3125HelicalUniRule annotationAdd
BLAST
Topological domaini32 – 271240CytoplasmicUniRule annotation2 PublicationsAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: EcoCyc
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi15 – 151L → R: Loss of activation of rcs. 1 Publication
Mutagenesisi16 – 161M → R: Only partial activation of rcs. 1 Publication
Mutagenesisi233 – 2331H → Q: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 271271Co-chaperone protein DjlAPRO_0000209424Add
BLAST

Proteomic databases

PaxDbiP31680.
PRIDEiP31680.

Interactioni

Subunit structurei

Homodimer.UniRule annotation1 Publication

GO - Molecular functioni

  • chaperone binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4261616. 7 interactions.
IntActiP31680. 7 interactions.
STRINGi511145.b0055.

Structurei

3D structure databases

ProteinModelPortaliP31680.
SMRiP31680. Positions 200-268.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini205 – 27167JUniRule annotationAdd
BLAST

Domaini

The transmembrane domain is a dimerization domain.UniRule annotation1 Publication

Sequence similaritiesi

Contains 1 J domain.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG41066UG. Bacteria.
COG1076. LUCA.
HOGENOMiHOG000272779.
InParanoidiP31680.
KOiK05801.
OMAiMQYWGKL.

Family and domain databases

CDDicd06257. DnaJ. 1 hit.
Gene3Di1.10.287.110. 1 hit.
1.10.3680.10. 1 hit.
HAMAPiMF_01153. DjlA. 1 hit.
InterProiIPR023749. DjlA.
IPR007791. DjlA_N.
IPR001623. DnaJ_domain.
IPR029024. TerB-like.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
PF05099. TerB. 1 hit.
[Graphical view]
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
PROSITEiPS50076. DNAJ_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P31680-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQYWGKIIGV AVALLMGGGF WGVVLGLLIG HMFDKARSRK MAWFANQRER
60 70 80 90 100
QALFFATTFE VMGHLTKSKG RVTEADIHIA SQLMDRMNLH GASRTAAQNA
110 120 130 140 150
FRVGKSDNYP LREKMRQFRS VCFGRFDLIR MFLEIQIQAA FADGSLHPNE
160 170 180 190 200
RAVLYVIAEE LGISRAQFDQ FLRMMQGGAQ FGGGYQQQTG GGNWQQAQRG
210 220 230 240 250
PTLEDACNVL GVKPTDDATT IKRAYRKLMS EHHPDKLVAK GLPPEMMEMA
260 270
KQKAQEIQQA YELIKQQKGF K
Length:271
Mass (Da):30,579
Last modified:July 1, 1993 - v1
Checksum:i80A0FC28F6D470DF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti195 – 1951Q → L in AAT42473 (PubMed:12664169).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC73166.1.
AP009048 Genomic DNA. Translation: BAB96623.1.
AY625119 Genomic DNA. Translation: AAT42473.1.
PIRiG64726.
RefSeqiNP_414597.1. NC_000913.3.
WP_001200579.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73166; AAC73166; b0055.
BAB96623; BAB96623; BAB96623.
GeneIDi948992.
KEGGiecj:JW0054.
eco:b0055.
PATRICi32115209. VBIEscCol129921_0056.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC73166.1.
AP009048 Genomic DNA. Translation: BAB96623.1.
AY625119 Genomic DNA. Translation: AAT42473.1.
PIRiG64726.
RefSeqiNP_414597.1. NC_000913.3.
WP_001200579.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP31680.
SMRiP31680. Positions 200-268.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261616. 7 interactions.
IntActiP31680. 7 interactions.
STRINGi511145.b0055.

Proteomic databases

PaxDbiP31680.
PRIDEiP31680.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73166; AAC73166; b0055.
BAB96623; BAB96623; BAB96623.
GeneIDi948992.
KEGGiecj:JW0054.
eco:b0055.
PATRICi32115209. VBIEscCol129921_0056.

Organism-specific databases

EchoBASEiEB1530.
EcoGeneiEG11570. djlA.

Phylogenomic databases

eggNOGiENOG41066UG. Bacteria.
COG1076. LUCA.
HOGENOMiHOG000272779.
InParanoidiP31680.
KOiK05801.
OMAiMQYWGKL.

Enzyme and pathway databases

BioCyciEcoCyc:EG11570-MONOMER.
ECOL316407:JW0054-MONOMER.

Miscellaneous databases

PROiP31680.

Family and domain databases

CDDicd06257. DnaJ. 1 hit.
Gene3Di1.10.287.110. 1 hit.
1.10.3680.10. 1 hit.
HAMAPiMF_01153. DjlA. 1 hit.
InterProiIPR023749. DjlA.
IPR007791. DjlA_N.
IPR001623. DnaJ_domain.
IPR029024. TerB-like.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
PF05099. TerB. 1 hit.
[Graphical view]
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
PROSITEiPS50076. DNAJ_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDJLA_ECOLI
AccessioniPrimary (citable) accession number: P31680
Secondary accession number(s): Q6IU30
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: September 7, 2016
This is version 133 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.