RECF_CLOBJ
ID RECF_CLOBJ Reviewed; 364 AA.
AC C1FPH6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=CLM_0004;
OS Clostridium botulinum (strain Kyoto / Type A2).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=536232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kyoto / Type A2;
RA Shrivastava S., Brinkac L.M., Brown J.L., Bruce D., Detter C.C.,
RA Johnson E.A., Munk C.A., Smith L.A., Smith T.J., Sutton G., Brettin T.S.;
RT "Genome sequence of Clostridium botulinum A2 Kyoto.";
RL Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001581; ACO84993.1; -; Genomic_DNA.
DR RefSeq; WP_003359456.1; NC_012563.1.
DR AlphaFoldDB; C1FPH6; -.
DR SMR; C1FPH6; -.
DR STRING; 536232.CLM_0004; -.
DR EnsemblBacteria; ACO84993; ACO84993; CLM_0004.
DR GeneID; 5184259; -.
DR KEGG; cby:CLM_0004; -.
DR eggNOG; COG1195; Bacteria.
DR HOGENOM; CLU_040267_0_1_9; -.
DR OMA; GESWSYA; -.
DR Proteomes; UP000001374; 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; SOS response.
FT CHAIN 1..364
FT /note="DNA replication and repair protein RecF"
FT /id="PRO_1000133680"
FT BINDING 30..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00365"
SQ SEQUENCE 364 AA; 42641 MW; E3E9E2E11B980716 CRC64;
MYIKNVHLIN FRNYDDMYLE LSPNTNIFVG NNAQGKTNIL ESIYYSSIGK SHRTNKDKDL
IKWDKNNTYL RTYVSRERLD KTIDINIFKN GKKAITVNKI KIKKISELMG NLNVVMFSPE
DLRIIKDSPG NRRKFLDIEL CKINNVYYHD LVQYNKILSE RNTALKNWNN KINDIIDIYD
EQLSKYGAFI IKERNKYLDK LNIIGKNIHK KITNDLEDIN FRYLTNIKDF DNAEKELLIV
LKKNRKKDLE RNSTSIGPHR DDFEVSINNI DTRIFGSQGQ QRTAVLTLKF ASLEIIKNII
GEYPVLLLDD VLSELDSNRQ KFVLNSIDKI QTIITCTGIE EIDKYLDKKQ SQLYLVNNGK
IKRV