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UniProtKB/Swiss-Prot entry Q8P9X2


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

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Entry information
Entry name LEXA2_XANCP
Primary accession number Q8P9X2
Secondary accession numbers None
Integrated into Swiss-Prot on November 25, 2002
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 46)
Name and origin of the protein
Protein name LexA repressor 2
Synonym EC 3.4.21.88
Gene name
Name: lexA2
OrderedLocusNames: XCC1721
From
Xanthomonas campestris pv. campestris [TaxID: 340] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; Xanthomonadaceae; Xanthomonas.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 33913 / NCPPB 528 / LMG 568;
DOI=10.1038/417459a; PubMed=12024217 [NCBI, ExPASy, EBI, Israel, Japan]
da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B., Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
"Comparison of the genomes of two Xanthomonas pathogens with differing host specificities.";
Nature 417:459-463(2002).
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
AE012273; AAM41015.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_637091.1; -.
3D structure databases
HSSP P03033; 1JHC. [HSSP ENTRY / PDB]
ModBase Q8P9X2.
Protein family/group databases
MEROPS S24.001; -.
Enzyme and pathway databases
BioCyc XCAM190485:XCC1721-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:0006508; Biological process: proteolysis (inferred from electronic annotation from InterPro).
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.
Genome annotation databases
GeneID 998323; -.
GenomeReviews AE008922_GR; XCC1721.
KEGG xcc:XCC1721; -.
Phylogenomic databases
HOGENOM Q8P9X2; -.
Genome annotation databases
CMR Q8P9X2; XCC1721.
Other
ProtoNet Q8P9X2.
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   213  213     LexA repressor 2. PRO_0000170110
DNA_BIND   27    47  21     H-T-H motif (By similarity). 
ACT_SITE   133   133        For autocatalytic cleavage activity (By similarity). 
ACT_SITE   170   170        For autocatalytic cleavage activity (By similarity). 
SITE   98    99  2     Cleavage; by autolysis (By similarity). 
Sequence information
Length: 213 AA [This is the length of the unprocessed precursor] Molecular weight: 23149 Da [This is the MW of the unprocessed precursor] CRC64: C43E270DA737A106 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGLTDTQQAI LALIAERIET DGVPPSQTEI ARAFGFKGVR AAQYHLEALE QAGAIRRVPG 

        70         80         90        100        110        120 
QARGIRLAGA AAHARAAPAE EPVRDDVLRL PVLGRVAAGL PIGADIGSDD FVVLDRVFFS 

       130        140        150        160        170        180 
PSPDYLLKVQ GDSMRDEGIF NGDLIGVHRT RDARSGQIVV ARIDEEITVK LLKIGKDRIR 

       190        200        210 
LLPRNPDYAP IEVLPDQDFA IEGLYCGLLR PNR 

Q8P9X2 in FASTA format

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