RECF_FRATT
ID RECF_FRATT Reviewed; 349 AA.
AC Q5NGS0;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
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=FTT_0762c;
OS Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=177416;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCHU S4 / Schu 4;
RX PubMed=15640799; DOI=10.1038/ng1499;
RA Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H.,
RA Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D.,
RA Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S.,
RA Sjoestedt A., Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W.,
RA Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W.;
RT "The complete genome sequence of Francisella tularensis, the causative
RT agent of tularemia.";
RL Nat. Genet. 37:153-159(2005).
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; AJ749949; CAG45395.1; -; Genomic_DNA.
DR RefSeq; WP_003020619.1; NZ_CP010290.1.
DR RefSeq; YP_169772.1; NC_006570.2.
DR AlphaFoldDB; Q5NGS0; -.
DR SMR; Q5NGS0; -.
DR STRING; 177416.FTT_0762c; -.
DR DNASU; 3191639; -.
DR EnsemblBacteria; CAG45395; CAG45395; FTT_0762c.
DR KEGG; ftu:FTT_0762c; -.
DR eggNOG; COG1195; Bacteria.
DR OMA; GESWSYA; -.
DR Proteomes; UP000001174; 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; 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..349
FT /note="DNA replication and repair protein RecF"
FT /id="PRO_1000205492"
FT BINDING 30..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00365"
SQ SEQUENCE 349 AA; 40843 MW; 8B80DFBF2F3B12B9 CRC64;
MYISNLRLQN FRNIPAKSFD FKNSINFIVG KNGSGKTSIL ESIYFLSHSR SFRSSQLNRI
INHNADEFII YTKAYNPDEI TISLSRKKNS NNISKLNLEI QKNHTEITRN LPIQLINPES
FNIINSGAQQ RCKVLDWGAF YLDKTFLKIW QQTKFLVKQR NSALKQNYPY SYILSIDKKL
CEFAEILDYK RQAYFTKLKP KIYEILSHFN PNLQLDIDYF RGWNLHKSLA QVLEESFNYD
NKYKVTNHGP HKADIVLSVS HKPIQDIFSR GQQKLLICAL KLAQGEIHNS ENDNKCIYLI
DDITSELDSI HTLTLFNYLK QLKSQVFITT TEKNKINEFI DTNSYILEI
