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D5DKR1 (D5DKR1_BACMD) Unreviewed, UniProtKB/TrEMBL

Last modified June 11, 2014. Version 27. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein attributes

Sequence length205 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair By similarity. HAMAP-Rule MF_00015 SAAS SAAS019759

Catalytic activity

Hydrolysis of Ala-|-Gly bond in repressor LexA. HAMAP-Rule MF_00015 SAAS SAAS019759

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00015 SAAS SAAS019759

Sequence similarities

Belongs to the peptidase S24 family. HAMAP-Rule MF_00015 RuleBase RU003991

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

DNA binding27 – 4721H-T-H motif By similarity HAMAP-Rule MF_00015

Sites

Active site1271For autocatalytic cleavage activity By similarity HAMAP-Rule MF_00015
Active site1651For autocatalytic cleavage activity By similarity HAMAP-Rule MF_00015
Site91 – 922Cleavage; by autolysis By similarity HAMAP-Rule MF_00015

Sequences

Sequence LengthMass (Da)Tools
D5DKR1 [UniParc].

Last modified June 15, 2010. Version 1.
Checksum: 189CA7BF44519873

FASTA20522,847
        10         20         30         40         50         60 
MKLSKRQQDI LDFIKHEVKL KGYPPSVREI GEAVGLASSS TVHGHLARLE SKGLIRRDPT 

        70         80         90        100        110        120 
KPRAIEVLQL DEVNIPKSNV INVPVIGKVT AGLPITAVEN VEEYFPLPDK FVSPDDHVFM 

       130        140        150        160        170        180 
LEIMGESMIE AGILDGDMVI VRQQQTANNG DIVVAMTEDN EATVKRFFKE ENFVRLQPEN 

       190        200 
STMAPIILRH VTILGKVTGV YRTIH 

« Hide

References

[1]"Genome sequences of the industrial vitamin B12-producers B. megaterium QM B1551 and DSM319 reveal new insights into the Bacillus genome evolution and pan-genome structure."
Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K., Riley D.R., Creasy H.H., Koenig S.S.K., Galens K., Orvis J., Creasy T., Biedendieck R., Braun C., Grayburn S., Jahn D., Ravel J., Vary P.S.
Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 319.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001982 Genomic DNA. Translation: ADF40907.1.
RefSeqYP_003599257.1. NC_014103.1.

3D structure databases

ProteinModelPortalD5DKR1.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS24.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADF40907; ADF40907; BMD_4077.
GeneID9119468.
KEGGbmd:BMD_4077.
PATRIC37258317. VBIBacMeg104484_4072.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000232168.
KOK01356.
OMAHVTILGK.

Enzyme and pathway databases

BioCycBMEG592022:GIVX-4077-MONOMER.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
2.10.109.10. 1 hit.
HAMAPMF_00015. LexA.
InterProIPR006200. LexA.
IPR006199. LexA_DNA-bd_dom.
IPR028360. Peptidase_S24/S26_b-rbn.
IPR006197. Peptidase_S24_LexA.
IPR019759. Peptidase_S24_S26.
IPR015927. Peptidase_S24_S26A/B/C.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF01726. LexA_DNA_bind. 1 hit.
PF00717. Peptidase_S24. 1 hit.
[Graphical view]
PRINTSPR00726. LEXASERPTASE.
SUPFAMSSF51306. SSF51306. 1 hit.
TIGRFAMsTIGR00498. lexA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameD5DKR1_BACMD
AccessionPrimary (citable) accession number: D5DKR1
Entry history
Integrated into UniProtKB/TrEMBL: June 15, 2010
Last sequence update: June 15, 2010
Last modified: June 11, 2014
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)