ID   RECF_THEFY              Reviewed;         377 AA.
AC   Q47U20;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 117.
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=Tfu_0004;
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX;
RX   PubMed=17209016; DOI=10.1128/jb.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G.,
RA   Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B.,
RA   Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
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; CP000088; AAZ54044.1; -; Genomic_DNA.
DR   RefSeq; WP_011290453.1; NC_007333.1.
DR   AlphaFoldDB; Q47U20; -.
DR   SMR; Q47U20; -.
DR   STRING; 269800.Tfu_0004; -.
DR   PRIDE; Q47U20; -.
DR   EnsemblBacteria; AAZ54044; AAZ54044; Tfu_0004.
DR   KEGG; tfu:Tfu_0004; -.
DR   eggNOG; COG1195; Bacteria.
DR   HOGENOM; CLU_040267_1_1_11; -.
DR   OMA; GESWSYA; -.
DR   OrthoDB; 891841at2; -.
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..377
FT                   /note="DNA replication and repair protein RecF"
FT                   /id="PRO_0000236159"
FT   BINDING         30..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00365"
SQ   SEQUENCE   377 AA;  41783 MW;  728F5D0050FFDD1A CRC64;
     MHVSHLQLAD YRSYEAAYLE LEPGVSTFIG PNGQGKTNLV EAIGYVATHS SHRVAHDAPL
     VRRGAQRAVI RAAVVRHGQT ALIELEINPG RANRARLNRS PNTRMRDVLG ILHTVLFAPE
     DLALVKGDPG ERRRFLDELL TARAPRYAGV RSDYERVLKQ RNALLKSAAA QNLHHRGGRD
     LPTLDVWDEH LAQIGAELLA ARLALVAELQ PLAAKAYGEL TATQDPISLR YRCSATDEEL
     DTTNRPQLVE ILRAALLRAR PDELRRGVSL VGPHRDDLQL WLNDLPAKGY ASQGESWSYA
     LALRLAGFEL LRADGDDPVL LLDDVFAELD AERRRRLASY VRTAEQVLVT AAVPDDVPQE
     LSGARFRVTG GSVERER