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Description:
Exodeoxyribonuclease (EC 3.1.11.2).
Molecular weight: 29252
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-OCT-1994, integrated into UniProtKB/Swiss-Prot.
01-OCT-1994, sequence version 1.
07-MAR-2006, entry version 53.
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 EXOA_BACSU:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | D26185 | BAA05218.1 | - |
| EMBL | Z99124 | CAB16125.1 | - |
| PIR | S66012 | S66012. | |
| HSSP | P27695 | 1HD7 | |
| GenomeReviews | AL009126_GR | BSU40880.1 | |
| SubtiList | BG10046 | exoA. | |
| BioCyc | BSUB1423:BSU4085-MONOMER | -.1 | |
| InterPro | IPR000097 | APendonclse1. | |
| InterPro | IPR005135 | Exo_endo_phos. | |
| InterPro | IPR004808 | ExoIII_xth. | |
| Pfam | PF03372 | Exo_endo_phos | 1. |
| TIGRFAMs | TIGR00195 | exoDNase_III | 1. |
| TIGRFAMs | TIGR00633 | xth | 1. |
| PROSITE | PS00726 | AP_NUCLEASE_F1_1 | 1. |
| PROSITE | PS00727 | AP_NUCLEASE_F1_2 | 1. |
| PROSITE | PS00728 | AP_NUCLEASE_F1_3 | 1. |
Keywords:
Complete proteome; Exonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX MEDLINE=96051385; PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA Ogasawara N., Nakai S., Yoshikawa H.;
RT "Systematic sequencing of the 180 kilobase region of the Bacillus
RT subtilis chromosome containing the replication origin.";
RL DNA Res. 1:1-14(1994).
RN [2]
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 [3]
RP CHARACTERIZATION.
RA Shida T., Ogawa T., Ogasawara N., Sekiguchi J.;
RT "Characterization of Bacillus subtilis ExoA protein: a multifunctional
RT DNA-repair enzyme similar to the Escherichia coli exonuclease III.";
RL Biosci. Biotechnol. Biochem. 63:1528-1534(1999).
Feature:
CHAIN 1 252 Exodeoxyribonuclease.
/FTId=PRO_0000200025.
ACT_SITE 243 243 Proton acceptor (By similarity).
METAL 36 36 Magnesium or manganese (By similarity).
Comments:
-!- CATALYTIC ACTIVITY: Exonucleolytic cleavage in the 3'- to 5'-
direction to yield nucleoside 5'-phosphates.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- SIMILARITY: Belongs to the DNA repair enzymes AP/exoA family.
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Sequence length: 252
MKLISWNVNG LRAVMRKMDF LSYLKEEDAD IICLQETKIQ DGQVDLQPED YHVYWNYAVK
KGYSGTAVFS KQEPLQVIYG IGVEEHDQEG RVITLEFENV FVMTVYTPNS RRGLERIDYR
MQWEEALLSY ILELDQKKPV ILCGDLNVAH QEIDLKNPKA NRNNAGFSDQ EREAFTRFLE
AGFVDSFRHV YPDLEGAYSW WSYRAGARDR NIGWRIDYFV VSESLKEQIE DASISADVMG
SDHCPVELII NI