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Description:
LexA repressor (EC 3.4.21.88) (SOS regulatory protein dinR).
Molecular weight: 22849
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:
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-JUL-1993, sequence version 1.
07-MAR-2006, entry version 54.
Phylogenetic order:
Bacteria Firmicutes Bacillales Bacillaceae Bacillus.
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_BACSU:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | M64684 | AAA22573.1 | - |
| EMBL | Z99113 | CAB13669.1 | - |
| PIR | A41315 | A41315. | |
| HSSP | P03033 | 1JHF | |
| GenomeReviews | AL009126_GR | BSU17850.1 | |
| SubtiList | BG10678 | lexA. | |
| BioCyc | BSUB1423:BSU1786-MONOMER | -.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 [GENOMIC DNA].
RC STRAIN=168;
RX MEDLINE=92041604; PubMed=1657879;
RA Raymond-Denise A., Guillen N.;
RT "Identification of dinR, a DNA damage-inducible regulator gene of
RT Bacillus subtilis.";
RL J. Bacteriol. 173:7084-7091(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=168 / YB886;
RX MEDLINE=97125992; PubMed=8969214; DOI=10.1074/jbc.271.52.33176;
RA Miller M.C., Resnick J.B., Smith B.T., Lovett C.M. Jr.;
RT "The Bacillus subtilis dinR gene codes for the analogue of Escherichia
RT coli LexA. Purification and characterization of the DinR protein.";
RL J. Biol. Chem. 271:33502-33508(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP DNA-BINDING SPECIFICITY, AND POSSIBLE DIMERIZATION.
RC STRAIN=YB886A;
RX MEDLINE=98215190; PubMed=9555905;
RA Winterling K.W., Chafin D., Hayes J.J., Sun J., Levine A.S.,
RA Yasbin R.E., Woodgate R.;
RT "The Bacillus subtilis DinR binding site: redefinition of the
RT consensus sequence.";
RL J. Bacteriol. 180:2201-2211(1998).
Feature:
CHAIN 1 205 LexA repressor.
/FTId=PRO_0000170010.
DNA_BIND 28 48 H-T-H motif (By similarity).
ACT_SITE 127 127 Involved in auto-cleavage (By
similarity).
ACT_SITE 165 165 Involved in auto-cleavage (By
similarity).
SITE 91 92 Cleavage (auto-).
Comments:
-!- FUNCTION: Represses dinA, dinB, dinC, recA genes and itself by
binding to the 14 bp palindromic sequence 5'-CGAACNNNNGTTCG-3'. 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.
-!- CATALYTIC ACTIVITY: Hydrolysis of Ala-|-Gly bond in repressor
lexA.
-!- SUBUNIT: Homodimer (By similarity).
-!- DEVELOPMENTAL STAGE: Expressed during the entire cell cycle with
at least a threefold increase when cells develop competence.
-!- INDUCTION: An SOS-independent induction of dinR occurs during
competence.
-!- SIMILARITY: Belongs to the peptidase S24 family.
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Sequence length: 205
MTKLSKRQLD ILRFIKAEVK SKGYPPSVRE IGEAVGLASS STVHGHLARL ETKGLIRRDP
TKPRAIEILD EEVDIPQSQV VNVPVIGKVT AGSPITAVEN IEEYFPLPDR MVPPDEHVFM
LEIMGDSMID AGILDKDYVI VKQQNTANNG EIVVAMTEDD EATVKRFYKE DTHIRLQPEN
PTMEPIILQN VSILGKVIGV FRTVH