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UniProtKB/Swiss-Prot entry Q8PN77


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

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Entry information
Entry name LEXA1_XANAC
Primary accession number Q8PN77
Secondary accession numbers None
Integrated into Swiss-Prot on March 1, 2004
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 41)
Name and origin of the protein
Protein name LexA repressor 1
Synonym EC 3.4.21.88
Gene name
Name: lexA1
OrderedLocusNames: XAC1196
From
Xanthomonas axonopodis pv. citri (Citrus canker) [TaxID: 92829] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; Xanthomonadaceae; Xanthomonas.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=306;
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
AE011749; AAM36068.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_641532.1; -.
3D structure databases
HSSP P03033; 1LEA. [HSSP ENTRY / PDB]
ModBase Q8PN77.
Protein family/group databases
MEROPS S24.001; -.
Enzyme and pathway databases
BioCyc XAXO190486:XAC1196-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 1155267; -.
GenomeReviews AE008923_GR; XAC1196.
KEGG xac:XAC1196; -.
NMPDR fig|190486.1.peg.1176; -.
Phylogenomic databases
HOGENOM Q8PN77; -.
Genome annotation databases
CMR Q8PN77; XAC1196.
Other
ProtoNet Q8PN77.
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   201  201     LexA repressor 1. PRO_0000170105
DNA_BIND   27    47  21     H-T-H motif (By similarity). 
ACT_SITE   122   122        For autocatalytic cleavage activity (By similarity). 
ACT_SITE   159   159        For autocatalytic cleavage activity (By similarity). 
SITE   87    88  2     Cleavage; by autolysis (By similarity). 
Sequence information
Length: 201 AA [This is the length of the unprocessed precursor] Molecular weight: 21442 Da [This is the MW of the unprocessed precursor] CRC64: 9B0FABAFEDFB7082 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPSLPPQRAA VLAFLQEQAQ AGVSPSLAEI AQAFGFASRN AAQKHVQALA DAGLIELLPN 

        70         80         90        100        110        120 
QKRGIRLPGG AGRDALLALP VLGRVAAGLP IGADIGLERQ LWLDRALFSL RPDYLLQVQG 

       130        140        150        160        170        180 
DSMIDDGILD GDLVGVHRSN EARDGQIVVA RVDGEITIKR LERGAERIRL LPRNRAHAPI 

       190        200 
VVAADADFAI EGLYCGLIRQ G 

Q8PN77 in FASTA format

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