RECF_DEIDV
ID RECF_DEIDV Reviewed; 360 AA.
AC C1CW06;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2015, sequence version 2.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=DNA replication and repair protein RecF {ECO:0000255|HAMAP-Rule:MF_00365};
GN Name=recF {ECO:0000255|HAMAP-Rule:MF_00365}; OrderedLocusNames=Deide_14250;
OS Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=546414;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115;
RX PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT bacterium Deinococcus deserti.";
RL PLoS Genet. 5:E1000434-E1000434(2009).
CC -!- FUNCTION: The RecF protein is involved in DNA metabolism; it is
CC required for DNA replication and normal SOS inducibility. RecF binds
CC preferentially to single-stranded, linear DNA. It also seems to bind
CC ATP. {ECO:0000255|HAMAP-Rule:MF_00365}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00365}.
CC -!- SIMILARITY: Belongs to the RecF family. {ECO:0000255|HAMAP-
CC Rule:MF_00365}.
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DR EMBL; CP001114; ACO46373.2; -; Genomic_DNA.
DR AlphaFoldDB; C1CW06; -.
DR SMR; C1CW06; -.
DR STRING; 546414.Deide_14250; -.
DR PaxDb; C1CW06; -.
DR EnsemblBacteria; ACO46373; ACO46373; Deide_14250.
DR KEGG; ddr:Deide_14250; -.
DR eggNOG; COG1195; Bacteria.
DR HOGENOM; CLU_040267_0_1_0; -.
DR Proteomes; UP000002208; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.1050.90; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00365; RecF; 1.
DR InterPro; IPR001238; DNA-binding_RecF.
DR InterPro; IPR018078; DNA-binding_RecF_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038729; Rad50/SbcC_AAA.
DR InterPro; IPR042174; RecF_2.
DR PANTHER; PTHR32182:SF0; PTHR32182:SF0; 2.
DR Pfam; PF13476; AAA_23; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00611; recf; 1.
DR PROSITE; PS00617; RECF_1; 1.
DR PROSITE; PS00618; RECF_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; DNA damage; DNA repair; DNA replication;
KW DNA-binding; Nucleotide-binding; Reference proteome; SOS response.
FT CHAIN 1..360
FT /note="DNA replication and repair protein RecF"
FT /id="PRO_1000205479"
FT BINDING 30..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00365"
SQ SEQUENCE 360 AA; 38925 MW; 472C600099DB1517 CRC64;
MQLESLSTLN YRNLAPCTLS FPAGVTGVFG ENGAGKTNLL EAAYLALTGL TDVTRLEQLV
QSGEGEAYVR ADLESGGSLS IQEVGLGRGR RQLKVDGVRV RAGDLPRGSA VWIRPEDSEL
VFGSPSGRRN FLDALLSRLS ARYAQQLARY DRTVSQRNAA LRSGEEWAMH VWDDALVKLG
SDIMLFRRRA LTRLSELAAE ANEALGSRKP LVLGLSESTT PETYAHDLRS RRAEELARGS
TATGPHRDDL TMTLGDFPAT EYASRGEGRT IALALRRAEL ELLAERFGEK PVLLIDDFSA
ELDPTRRAFL LDLAASVPQA IVTGTEQAPG AALTLRAHAG RFTPEPEPVS AQVAVDEVGA
