ID   RECF_LEPBJ              Reviewed;         365 AA.
AC   Q04WF5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=LBJ_0006;
OS   Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=355277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JB197;
RX   PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA   Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A.,
RA   Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L.,
RA   Rood J.I., Davies J.K., Adler B.;
RT   "Genome reduction in Leptospira borgpetersenii reflects limited
RT   transmission potential.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006).
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; CP000350; ABJ74765.1; -; Genomic_DNA.
DR   RefSeq; WP_011669139.1; NC_008510.1.
DR   AlphaFoldDB; Q04WF5; -.
DR   SMR; Q04WF5; -.
DR   PRIDE; Q04WF5; -.
DR   EnsemblBacteria; ABJ74765; ABJ74765; LBJ_0006.
DR   KEGG; lbj:LBJ_0006; -.
DR   HOGENOM; CLU_040267_0_1_12; -.
DR   OMA; GESWSYA; -.
DR   Proteomes; UP000000656; Chromosome 1.
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..365
FT                   /note="DNA replication and repair protein RecF"
FT                   /id="PRO_1000048537"
FT   BINDING         30..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00365"
SQ   SEQUENCE   365 AA;  42084 MW;  79F5413E8772A56D CRC64;
     MFLKHLTLQN FRSYEELSLD FNSRLIFFVG DNGEGKTNLL EAICMLSWLK SFRESEDSNL
     IRWGSENYFL RGKIKGDQKE SVLEVGFTAK PTVKRKLKFN QEEVKKRTDL IGKFITVLLT
     PMDLKIIEGG PAERRKFIDA FISSFDPFYL ECLLEYNKIL KHRNALLKTG ISDASHLSIW
     DRKLIEKGVL ILNKRKEIVF GLNSFYQPNL NKLSGGKDEL EMIYGPNVKD KDEFVEKLGR
     NLGKDLRLGY TSVGIHRDDL FIGADKRDIT EFGSQGQKRS TVIALKAATF NYYRNVLDTM
     PVLLIDDVIR ELDVKRREYF VDLVINAGQA FFTTTDLEGI QDYVGKLKDQ KQIFLIQQGN
     IQFAK