ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q6FZU5


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name LEXA_BARQU
Primary accession number Q6FZU5
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 2005
Sequence was last modified on July 19, 2004 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 28)
Name and origin of the protein
Protein name LexA repressor
Synonym EC 3.4.21.88
Gene name
Name: lexA
OrderedLocusNames: BQ06160
From
Bartonella quintana (Rochalimaea quintana) [TaxID: 803] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Bartonellaceae; Bartonella.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Toulouse;
DOI=10.1073/pnas.0305659101; PubMed=15210978 [NCBI, ExPASy, EBI, Israel, Japan]
Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E.;
"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae.";
Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
BX897700; CAF26107.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq YP_032265.1; -.
3D structure databases
ModBase Q6FZU5.
Protein family/group databases
MEROPS S24.001; -.
Enzyme and pathway databases
BioCyc BQUI283165:BQ06160-MON; -.
Ontologies
GO
GO:0003677; Molecular function: DNA binding (inferred from electronic annotation from HAMAP).
GO:0004252; Molecular function: serine-type endopeptidase activity (inferred from electronic annotation from HAMAP).
GO:0006281; Biological process: DNA repair (inferred from electronic annotation from HAMAP).
GO:0006260; Biological process: DNA replication (inferred from electronic annotation from HAMAP).
GO:0045892; Biological process: negative regulation of transcription, DNA-dependent (inferred from electronic annotation from HAMAP).
GO:0009432; Biological process: SOS response (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00015; -; 1.
PBIL [Tree]
InterPro IPR006199; LexA_DNA_bd.
IPR006200; Pept_S24_LexA.
IPR006197; Pept_S24_SOS.
IPR011056; Peptidase_S24_S26_C.
IPR011991; Wing_hlx_DNA_bd.
Graphical view of domain structure.
Gene3D G3DSA:2.10.109.10; Pept_S24_S26_C; 1.
G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
Pfam PF01726; LexA_DNA_bind; 1.
PF00717; Peptidase_S24; 1.
Pfam graphical view of domain structure.
PRINTS PR00726; LEXASERPTASE.
TIGRFAMs TIGR00498; lexA; 1.
BLOCKS Q6FZU5.
ProtoNet Q6FZU5.
Genome annotation databases
GeneID 2866428; -.
GenomeReviews BX897700_GR; BQ06160.
KEGG bqu:BQ06160; -.
NMPDR fig|283165.1.peg.535; -.
Phylogenomic databases
HOGENOM Q6FZU5; -.
Genome annotation databases
CMR Q6FZU5; BQ06160.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Autocatalytic cleavage; Complete proteome; DNA damage; DNA repair; DNA replication; DNA-binding; Hydrolase; Repressor; SOS response; Transcription; Transcription regulation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   237  237     LexA repressor. PRO_0000170012
DNA_BIND   26    46  21     H-T-H motif (By similarity). 
ACT_SITE   158   158        For autocatalytic cleavage activity (By similarity). 
ACT_SITE   196   196        For autocatalytic cleavage activity (By similarity). 
SITE   123   124  2     Cleavage; by autolysis (By similarity). 
Sequence information
Length: 237 AA [This is the length of the unprocessed precursor] Molecular weight: 26908 Da [This is the MW of the unprocessed precursor] CRC64: 0A152E6FF49A8299 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLTCKQYELL LFIHNHMKEI GVPPSFDEMK IALELTSKSG IHRLITALEE RGFIRRLPNR 

        70         80         90        100        110        120 
ARAVEVVRLP EKITFNLSSA RKISPNVIEN NRRKISKNSK NLNNFDIEDK KNVTVPIMGR 

       130        140        150        160        170        180 
IAAGVPVSAI QQQTNTLCLP ADMISLGEHY ALEVKDDSMI EAGILDKDTI IVRRQNTATP 

       190        200        210        220        230 
GEIIIALIDK EEATLKRYRR NGASIALEAA NPHYETRIYR PERIEIQGKL IGLIRKY 

Q6FZU5 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!