ID   RECF_CLOBB              Reviewed;         361 AA.
AC   B2THB7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=CLL_A0004;
OS   Clostridium botulinum (strain Eklund 17B / Type B).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=935198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Eklund 17B / Type B;
RA   Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.S.;
RT   "Complete sequence of Clostridium botulinum strain Eklund.";
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001056; ACD22044.1; -; Genomic_DNA.
DR   RefSeq; WP_012422929.1; NC_018648.1.
DR   AlphaFoldDB; B2THB7; -.
DR   SMR; B2THB7; -.
DR   EnsemblBacteria; ACD22044; ACD22044; CLL_A0004.
DR   KEGG; cbk:CLL_A0004; -.
DR   PATRIC; fig|935198.13.peg.4; -.
DR   HOGENOM; CLU_040267_0_1_9; -.
DR   OMA; GESWSYA; -.
DR   OrthoDB; 891841at2; -.
DR   Proteomes; UP000001195; 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   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; IPR003395; RecF/RecN/SMC_N.
DR   InterPro; IPR042174; RecF_2.
DR   PANTHER; PTHR32182:SF0; PTHR32182:SF0; 1.
DR   Pfam; PF02463; SMC_N; 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; SOS response.
FT   CHAIN           1..361
FT                   /note="DNA replication and repair protein RecF"
FT                   /id="PRO_1000121098"
FT   BINDING         30..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00365"
SQ   SEQUENCE   361 AA;  42185 MW;  AB61EF608DBDB741 CRC64;
     MYIKAIMLAN YRNYNNLELN LSEGVNVFIG DNAQGKTNVL ESIYYCAFAK SHRTSRDKDL
     INWKENEAYI SLLVGKKRLD KRIDIKILRD GKKAIKVNSI KINKIGELFG TFNVVMFSPE
     DLKIIKESPG IRRKFLDMEL CQISKKYYFN LVQYNKILNE RNVILRSRDF NKDILEVYDL
     QLVECADYIV KERLEYIDKI NYYGKFIHNE ITSGKEDIVF KYDSGIKFKD DFKYAFLEKL
     KNNLLRDREQ GITSIGPHRD DFNVLINNID VKKFGSQGQQ RTAVLTMKFS SLKIIKEITK
     EYPILLLDDV LSELDINRKR YVLSTLNDIQ TIITCTGIND LEDYLDDKSK VFKVCNGEIV
     N