ID RECF_LACH4 Reviewed; 375 AA.
AC A8YW44;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 92.
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=lhv_0004;
OS Lactobacillus helveticus (strain DPC 4571).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=405566;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DPC 4571;
RX PubMed=17993529; DOI=10.1128/jb.01295-07;
RA Callanan M., Kaleta P., O'Callaghan J., O'Sullivan O., Jordan K.,
RA McAuliffe O., Sangrador-Vegas A., Slattery L., Fitzgerald G.F.,
RA Beresford T., Ross R.P.;
RT "Genome sequence of Lactobacillus helveticus: an organism distinguished by
RT selective gene loss and IS element expansion.";
RL J. Bacteriol. 190:727-735(2008).
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; CP000517; ABX26301.1; -; Genomic_DNA.
DR RefSeq; WP_012211196.1; NC_010080.1.
DR AlphaFoldDB; A8YW44; -.
DR SMR; A8YW44; -.
DR KEGG; lhe:lhv_0004; -.
DR eggNOG; COG1195; Bacteria.
DR HOGENOM; CLU_040267_0_1_9; -.
DR Proteomes; UP000000790; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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 CDD; cd03242; ABC_RecF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.1050.90; RecF/RecN/SMC, N-terminal domain; 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; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR042174; RecF_2.
DR NCBIfam; TIGR00611; recf; 1.
DR PANTHER; PTHR32182; DNA REPLICATION AND REPAIR PROTEIN RECF; 1.
DR PANTHER; PTHR32182:SF0; DNA REPLICATION AND REPAIR PROTEIN RECF; 1.
DR Pfam; PF02463; SMC_N; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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; SOS response.
FT CHAIN 1..375
FT /note="DNA replication and repair protein RecF"
FT /id="PRO_1000072099"
FT BINDING 30..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00365"
SQ SEQUENCE 375 AA; 43094 MW; DD818162488CD587 CRC64;
MYLDHFVVQN FRNLKKLDID FDPNVNIFIG KNAQGKTNLL EAIYFLALTR SHRTNSDKEL
IGFGGEYTNL LGHVRKSQVD LTLRVLITQK GKKVWINRVE QAKLSKYVGQ LNAILFSPED
LELIKSAPAL RRRFMDQEFG QINAEYLYFA SKYRQVLLQK NNYLKQLAKG KTKDQVFLDV
LSDQLAGIAA EVIFRRFKFL RYLSHYASDV YAHISLGGEK LAIAYHPSVS TIEADDTVEE
IYQKILANFE RNKAVEMRKG TTTSGPHRDD IEFKLDGKNA HLYASQGQQR SIALSVKLAE
IQLVHQLTDE YPLLLLDDVM SELDHTRQSA LLNYIHGKTQ TFITTTDLEG ISWEIIKKPR
VYHMQSGKIS FEKEN
//
