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B7CTM8 (B7CTM8_BURPS) Unreviewed, UniProtKB/TrEMBL

Last modified January 25, 2012. Version 22. 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 length215 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 MF_00015

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. SAAS SAAS006199

Catalytic activity

Hydrolysis of Ala-|-Gly bond in repressor lexA. HAMAP MF_00015 RuleBase RU003992 SAAS SAAS006197

Subunit structure

Homodimer By similarity. HAMAP MF_00015 SAAS SAAS006197

Sequence similarities

Belongs to the peptidase S24 family. HAMAP MF_00015 RuleBase RU003991

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

DNA binding28 – 4821H-T-H motif By similarity HAMAP MF_00015

Sites

Active site1331For autocatalytic cleavage activity By similarity HAMAP MF_00015
Active site1701For autocatalytic cleavage activity By similarity HAMAP MF_00015
Site98 – 992Cleavage; by autolysis By similarity HAMAP MF_00015

Sequences

Sequence LengthMass (Da)Tools
B7CTM8 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 713C9B66594842E5

FASTA21523,199
        10         20         30         40         50         60 
MIKLTARQQQ VFDLIRRAIE RSGFPPTRAE IAAELGFSSP NAAEEHLRAL ARKGVIELAA 

        70         80         90        100        110        120 
GASRGIRLLG IDDAPHQLTL PHAALMQLSL PLVGRVAAGS PILAQEHISQ HYACDPALFS 

       130        140        150        160        170        180 
SKPDYLLKVR GLSMRDAGIL DGDLLAVQKR TEAKDGQIIV ARLGDDVTVK RLKRRPGGVE 

       190        200        210 
LIAENPDYEN IFVKAGSAEF ALEGIAVGLI RPGEF 

« Hide

References

[1]Brinkac L.M., Harkins D.M., Shrivastava S., Durkin A.S., Sutton G.
Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: 576 EMBL EEC33611.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
ACCE01000007 Genomic DNA. Translation: EEC33611.1.

3D structure databases

ProteinModelPortalB7CTM8.
SMRB7CTM8. Positions 1-69, 90-215.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

PATRIC27888186. VBIBurPse132396_4594.

Phylogenomic databases

OMAIAENPDF.

Family and domain databases

HAMAPMF_00015. LexA.
[Tree]
InterProIPR006199. LexA_DNA-bd_dom.
IPR006200. Pept_S24_LexA.
IPR006197. Peptidase_S24_LexA.
IPR019759. Peptidase_S24_S26.
IPR015927. Peptidase_S24_S26A/B/C.
IPR011056. Peptidase_S24_S26A/B/C_b-rbn.
IPR011991. WHTH_trsnscrt_rep_DNA-bd.
[Graphical view]
Gene3DG3DSA:2.10.109.10. Pept_S24_S26_C. 1 hit.
G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
PfamPF01726. LexA_DNA_bind. 1 hit.
PF00717. Peptidase_S24. 1 hit.
[Graphical view]
PRINTSPR00726. LEXASERPTASE.
SUPFAMSSF51306. Pept_S24_S26_C. 1 hit.
TIGRFAMsTIGR00498. LexA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameB7CTM8_BURPS
AccessionPrimary (citable) accession number: B7CTM8
Entry history
Integrated into UniProtKB/TrEMBL: February 10, 2009
Last sequence update: February 10, 2009
Last modified: January 25, 2012
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)