RECR_CAMJR
ID RECR_CAMJR Reviewed; 190 AA.
AC Q5HTK0;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Recombination protein RecR {ECO:0000255|HAMAP-Rule:MF_00017};
GN Name=recR {ECO:0000255|HAMAP-Rule:MF_00017}; OrderedLocusNames=CJE1399;
OS Campylobacter jejuni (strain RM1221).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=195099;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM1221;
RX PubMed=15660156; DOI=10.1371/journal.pbio.0030015;
RA Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A.,
RA Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C.,
RA Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U.,
RA Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M.,
RA Nelson K.E.;
RT "Major structural differences and novel potential virulence mechanisms from
RT the genomes of multiple Campylobacter species.";
RL PLoS Biol. 3:72-85(2005).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000025; AAW35718.1; -; Genomic_DNA.
DR RefSeq; WP_011049920.1; NC_003912.7.
DR AlphaFoldDB; Q5HTK0; -.
DR SMR; Q5HTK0; -.
DR KEGG; cjr:CJE1399; -.
DR HOGENOM; CLU_060739_1_1_7; -.
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; 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 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..190
FT /note="Recombination protein RecR"
FT /id="PRO_0000190299"
FT DOMAIN 81..167
FT /note="Toprim"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00017"
FT ZN_FING 58..73
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00017"
SQ SEQUENCE 190 AA; 21525 MW; A69D62F302B9B1C2 CRC64;
MVKGLEKFNE LVESFANLPT IGKKTAIRLA YHLCINNQID GMKLAHNIEN AIRFIKPCEQ
CGALSENELC EICSDEERNK NILCIVESPK DILTLEESQS YNGLYFVLDE LNEEKLEKLK
QIILKLNISE LIFALTHSIN SDATIFFIED KFKGLNLTFS KIAQGIPSGI NLENVDLISL
NKAMNFRTKI