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Protein data for RECA_LISIN:

Description:
Protein recA (Recombinase A).

Molecular weight: 38021

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:
23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
07-MAR-2006, entry version 30.

Phylogenetic order:
Bacteria Firmicutes Bacillales Listeriaceae Listeria.

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 RECA_LISIN:

DatabasePointerAdd. info#1Add. info#2
EMBLAL596168CAC96666.1-
PIRAB1612AB1612.
HSSPQ595601UBC
GenomeReviewsAL592022_GRlin1435.1
ListiListLIN01435-.1
BioCycLINN1642:LIN1435-MONOMER-.1
HAMAPMF_00268-1.
InterProIPR003593AAA_ATPase.
InterProIPR001553RecA_bac.
PfamPF00154RecA1.
PRINTSPR00142RECA.
ProDomPD000229RecA1.
SMARTSM00382AAA1.
TIGRFAMsTIGR02012tigrfam_recA1.
PROSITEPS00321RECA_11.
PROSITEPS50162RECA_21.
PROSITEPS50163RECA_31.

General information about the databases mentioned above

Keywords:
ATP-binding; Complete proteome; DNA damage; DNA recombination; DNA repair; DNA-binding; Nucleotide-binding; SOS response.

References:
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIP 11262 / Serovar 6a;
RX MEDLINE=21537279; PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A.,
RA Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T.,
RA Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P.,
RA Domann E., Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O.,
RA Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P.,
RA Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D.,
RA Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G.,
RA Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H.,
RA Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R.,
RA Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A.,
RA Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).

Feature:
CHAIN 1 348 Protein recA.
/FTId=PRO_0000122746.
NP_BIND 64 71 ATP (By similarity).

Comments:
-!- FUNCTION: Can catalyze the hydrolysis of ATP in the presence of
single-stranded DNA, the ATP-dependent uptake of single-stranded
DNA by duplex DNA, and the ATP-dependent hybridization of
homologous single-stranded DNAs. It interacts with lexA causing
its activation and leading to its autocatalytic cleavage (By
similarity).
-!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
-!- SIMILARITY: Belongs to the recA family.
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Sequence length: 348

     MNDRQAALDQ ALKQIEKQFG KGSIMKLGEH SDQNISTISS GSLALDIALG VGGYPRGRII
     EVYGPESSGK TTVALHAIAE VQAQGGTAAF IDAEHALDPA YAKNLGVNID ELLLSQPDTG
     EQALEIAEAL VRSGAVDMLV IDSVAALVPR AEIEGEMGDA HVGLQARLMS QALRKLSGVI
     NKSKTIAIFI NQIREKVGVM FGNPEITPGG RALKFYSTVR LEVRRAEQLK QGTDVMGNKT
     KIKVVKNKVA PPFRIAEVDI MYGEGISREG ELVDMAAEVD VINKSGSWYS YKEERIGQGR
     ENAKQYLKEH TDIRDEISKR VREEYEIDGT NKEPLDENEE TLSLLDDE

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