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Description:
LexA repressor (EC 3.4.21.88).
Molecular weight: 23395
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 )
Important dates:
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
27-APR-2001, sequence version 2.
07-MAR-2006, entry version 36.
Phylogenetic order:
Bacteria Proteobacteria Gammaproteobacteria Xanthomonadales Xanthomonadaceae Xylella.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein LEXA_XYLFA:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AE003865 | AAF82935.1 | ALT_INIT |
| HSSP | P03033 | 1JHF | |
| MEROPS | S24.001 | -. | |
| GenomeReviews | AE003849_GR | Xf0122.1 | |
| HAMAP | MF_00015 | - | 1. |
| InterPro | IPR006199 | LexA_DNA_bd. | |
| InterPro | IPR006200 | Pept_S24_LexA. | |
| InterPro | IPR006198 | Pept_S24_S26. | |
| InterPro | IPR006197 | Pept_S24_SOS. | |
| InterPro | IPR011991 | Wing_hlx_DNA_bd. | |
| Pfam | PF01726 | LexA_DNA_bind | 1. |
| Pfam | PF00717 | Peptidase_S24 | 1. |
| PRINTS | PR00726 | LEXASERPTASE. | |
| TIGRFAMs | TIGR00498 | lexA | 1. |
Keywords:
Autocatalytic cleavage; Complete proteome; DNA damage; DNA repair; DNA replication; DNA-binding; Hydrolase; Repressor; SOS response; Transcription; Transcription regulation.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9a5c;
RX MEDLINE=20365717; PubMed=10910347; DOI=10.1038/35018003;
RA Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M.,
RA Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S.,
RA Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S.,
RA Bueno M.R.P., Camargo A.A., Camargo L.E.A., Carraro D.M., Carrer H.,
RA Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M.,
RA Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H.,
RA Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A.,
RA Fraga J.S., Franca S.C., Franco M.C., Frohme M., Furlan L.R.,
RA Garnier M., Goldman G.H., Goldman M.H.S., Gomes S.L., Gruber A.,
RA Ho P.L., Hoheisel J.D., Junqueira M.L., Kemper E.L., Kitajima J.P.,
RA Krieger J.E., Kuramae E.E., Laigret F., Lambais M.R., Leite L.C.C.,
RA Lemos E.G.M., Lemos M.V.F., Lopes S.A., Lopes C.R., Machado J.A.,
RA Machado M.A., Madeira A.M.B.N., Madeira H.M.F., Marino C.L.,
RA Marques M.V., Martins E.A.L., Martins E.M.F., Matsukuma A.Y.,
RA Menck C.F.M., Miracca E.C., Miyaki C.Y., Monteiro-Vitorello C.B.,
RA Moon D.H., Nagai M.A., Nascimento A.L.T.O., Netto L.E.S.,
RA Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A.,
RA de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A.,
RA Peixoto B.R., Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B.,
RA Quaggio R.B., Roberto P.G., Rodrigues V., de Rosa A.J.M.,
RA de Rosa V.E. Jr., de Sa R.G., Santelli R.V., Sawasaki H.E.,
RA da Silva A.C.R., da Silva A.M., da Silva F.R., Silva W.A. Jr.,
RA da Silveira J.F., Silvestri M.L.Z., Siqueira W.J., de Souza A.A.,
RA de Souza A.P., Terenzi M.F., Truffi D., Tsai S.M., Tsuhako M.H.,
RA Vallada H., Van Sluys M.A., Verjovski-Almeida S., Vettore A.L.,
RA Zago M.A., Zatz M., Meidanis J., Setubal J.C.;
RT "The genome sequence of the plant pathogen Xylella fastidiosa.";
RL Nature 406:151-159(2000).
Feature:
CHAIN 1 211 LexA repressor.
/FTId=PRO_0000170113.
DNA_BIND 27 47 H-T-H motif (By similarity).
ACT_SITE 131 131 Involved in auto-cleavage (By
similarity).
ACT_SITE 168 168 Involved in auto-cleavage (By
similarity).
SITE 96 97 Cleavage (auto-) (By similarity).
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).
-!- CATALYTIC ACTIVITY: Hydrolysis of Ala-|-Gly bond in repressor
lexA.
-!- SUBUNIT: Homodimer (By similarity).
-!- SIMILARITY: Belongs to the peptidase S24 family.
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Sequence length: 211
MSLSDIQQAI LSLITNHINA DGVSPSQTEI ARAFGFKGVR AVQHHLDVLE QQGMIRRVPR
QARGIRLKHL TEVDETALAL QSEDVLRLPV LGRVAAGQPI GADIGEGRVV LLDRVFFSPA
PDYLLRVQGD SMRDEGIFDG DLIGVHRTQD AHSGQIVVAR IDDEITVKLL KISKDRIRLL
PRNPDFAPIE VRSDQDFAIE GLYCGLLRPN R