ID   RECF_RHOJR              Reviewed;         410 AA.
AC   Q0SAG4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=DNA replication and repair protein RecF {ECO:0000255|HAMAP-Rule:MF_00365};
GN   Name=recF {ECO:0000255|HAMAP-Rule:MF_00365};
GN   OrderedLocusNames=RHA1_ro03669;
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=101510;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1;
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA   Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA   Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA   Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA   Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA   Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(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; CP000431; ABG95472.1; -; Genomic_DNA.
DR   RefSeq; WP_009476747.1; NC_008268.1.
DR   AlphaFoldDB; Q0SAG4; -.
DR   SMR; Q0SAG4; -.
DR   STRING; 101510.RHA1_ro03669; -.
DR   EnsemblBacteria; ABG95472; ABG95472; RHA1_ro03669.
DR   KEGG; rha:RHA1_ro03669; -.
DR   eggNOG; COG1195; Bacteria.
DR   HOGENOM; CLU_040267_1_1_11; -.
DR   OMA; GESWSYA; -.
DR   Proteomes; UP000008710; 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; Reference proteome; SOS response.
FT   CHAIN           1..410
FT                   /note="DNA replication and repair protein RecF"
FT                   /id="PRO_1000048564"
FT   BINDING         30..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00365"
SQ   SEQUENCE   410 AA;  44817 MW;  B55CFAEA4C513750 CRC64;
     MFVRALSLRD FRSWDALGLT LRPGCTVFVG PNGHGKTNVL EALGYLSTLS SHRVSSDAPL
     IRTGTGQAFA GATVVNAGRE LTVDLELNEG KSNRARINQS PTRRPREILG ILQTVLFAPE
     DLSLVRGDPG DRRRYLDELL TSRIPRMAAV RADYDRVLRQ RSALLKTAGG ALRRVSRGSG
     RPSEDGASAL ATLEVWDGHL AAHGAQLLAG RLHLVHDLAP HLAESYQSLA PESRPASIRY
     RSSLGSSLPP EFTEPARVPE AGDIAFLEER FLQELSVMRS KEIERGVCLV GPHRDDLELH
     LGDTPAKGFA SHGESWSFAL SLRLAGFALL RSDGSDPVLM LDDVFAELDR RRRRALAKVA
     LDAEQVLITA AVPEDVPEEL DAVRFGVEAR DTDRGRISHI VEEPEDRSDG