ID   RECF_STRMU              Reviewed;         363 AA.
AC   Q8DRR3;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=SMU_2156;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; AE014133; AAN59745.1; -; Genomic_DNA.
DR   RefSeq; NP_722439.1; NC_004350.2.
DR   RefSeq; WP_002262456.1; NC_004350.2.
DR   AlphaFoldDB; Q8DRR3; -.
DR   SMR; Q8DRR3; -.
DR   STRING; 210007.SMU_2156; -.
DR   DNASU; 1029328; -.
DR   EnsemblBacteria; AAN59745; AAN59745; SMU_2156.
DR   GeneID; 66818507; -.
DR   KEGG; smu:SMU_2156; -.
DR   PATRIC; fig|210007.7.peg.1918; -.
DR   eggNOG; COG1195; Bacteria.
DR   HOGENOM; CLU_040267_0_1_9; -.
DR   OMA; GESWSYA; -.
DR   PhylomeDB; Q8DRR3; -.
DR   Proteomes; UP000002512; 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..363
FT                   /note="DNA replication and repair protein RecF"
FT                   /id="PRO_0000196471"
FT   BINDING         30..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00365"
SQ   SEQUENCE   363 AA;  42003 MW;  A2632C2AB9027AF0 CRC64;
     MWIEKINLKH YRNYTAIESE FSQSLNVFVG QNAQGKTNFL EAIYFLSLTR SHRTRSDKEL
     IQFGQKELNV SGLLNRVNGK IPLEINLSNK GRTTKINYLK QPKLSDYIGT MTVVLFAPED
     LQLIKGSPSL RRKFIDIDLG QIKPIYLSDL SNYNHVLKQR NAYLKSEKKV DTDFLFVLDE
     QLVDYGSKVI EHRLDFIQNL TKEADKYHFS ISNQQEHLKI SYLSSVKFDH KKNIRDNFLN
     LLQKNRQGDI FKKNTSVGPH RDDLAFFINQ MNASFGSQGQ HRSLILSLKL AEIELTKTVT
     GDYPILLLDD VMSELDNYRQ IKLLEGIKDN VQTFITTTSL EHLQQLPKKL KLFTINQGKV
     LSE