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RECR_STAAS
ID   RECR_STAAS              Reviewed;         198 AA.
AC   Q6GC08;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Recombination protein RecR {ECO:0000255|HAMAP-Rule:MF_00017};
GN   Name=recR {ECO:0000255|HAMAP-Rule:MF_00017}; OrderedLocusNames=SAS0437;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: May play a role in DNA repair. It seems to be involved in an
CC       RecBC-independent recombinational process of DNA repair. It may act
CC       with RecF and RecO. {ECO:0000255|HAMAP-Rule:MF_00017}.
CC   -!- SIMILARITY: Belongs to the RecR family. {ECO:0000255|HAMAP-
CC       Rule:MF_00017}.
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DR   EMBL; BX571857; CAG42212.1; -; Genomic_DNA.
DR   RefSeq; WP_000559156.1; NC_002953.3.
DR   AlphaFoldDB; Q6GC08; -.
DR   SMR; Q6GC08; -.
DR   KEGG; sas:SAS0437; -.
DR   HOGENOM; CLU_060739_1_0_9; -.
DR   OMA; DVMAIEN; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   CDD; cd01025; TOPRIM_recR; 1.
DR   HAMAP; MF_00017; RecR; 1.
DR   InterPro; IPR000093; DNA_Rcmb_RecR.
DR   InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR   InterPro; IPR023627; Rcmb_RecR.
DR   InterPro; IPR023628; Rcmb_RecR_C4-type_Zn.
DR   InterPro; IPR015967; Rcmb_RecR_CS.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR034137; TOPRIM_RecR.
DR   PANTHER; PTHR30446; PTHR30446; 1.
DR   Pfam; PF02132; RecR; 1.
DR   Pfam; PF13662; Toprim_4; 1.
DR   SMART; SM00278; HhH1; 1.
DR   SMART; SM00493; TOPRIM; 1.
DR   SUPFAM; SSF111304; SSF111304; 1.
DR   TIGRFAMs; TIGR00615; recR; 1.
DR   PROSITE; PS01300; RECR; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA recombination; DNA repair; Metal-binding; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..198
FT                   /note="Recombination protein RecR"
FT                   /id="PRO_0000190389"
FT   DOMAIN          80..175
FT                   /note="Toprim"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00017"
FT   ZN_FING         57..72
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00017"
SQ   SEQUENCE   198 AA;  22100 MW;  DCC2FA88971D3EB7 CRC64;
     MHYPEPISKL IDSFMKLPGI GPKTAQRLAF HTLDMKEDDV VQFAKALVDV KRELTYCSVC
     GHITENDPCY ICEDKQRDRS VICVVEDDKD VIAMEKMREY KGLYHVLHGS ISPMDGIGPE
     DINIPSLIER LKNDEVSELI LAMNPNLEGE STAMYISRLV KPIGIKVTRL AQGLSVGGDL
     EYADEVTLSK AIAGRTEM
 
 
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