RECF_COREF
ID RECF_COREF Reviewed; 398 AA.
AC Q8FUL4;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=CE0004;
OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS / NBRC 100395).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX PubMed=12840036; DOI=10.1101/gr.1285603;
RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT "Comparative complete genome sequence analysis of the amino acid
RT replacements responsible for the thermostability of Corynebacterium
RT efficiens.";
RL Genome Res. 13:1572-1579(2003).
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; BA000035; BAC16814.1; -; Genomic_DNA.
DR RefSeq; WP_006768690.1; NZ_GG700684.1.
DR AlphaFoldDB; Q8FUL4; -.
DR SMR; Q8FUL4; -.
DR STRING; 196164.23491839; -.
DR EnsemblBacteria; BAC16814; BAC16814; BAC16814.
DR KEGG; cef:CE0004; -.
DR eggNOG; COG1195; Bacteria.
DR HOGENOM; CLU_040267_1_1_11; -.
DR OMA; GESWSYA; -.
DR OrthoDB; 891841at2; -.
DR Proteomes; UP000001409; 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; IPR003593; AAA+_ATPase.
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 SMART; SM00382; AAA; 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..398
FT /note="DNA replication and repair protein RecF"
FT /id="PRO_0000196410"
FT BINDING 30..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00365"
SQ SEQUENCE 398 AA; 43591 MW; 835F113B6977D718 CRC64;
MYIRSLELRD FRSWPELKVE LKPGITIFIG RNGFGKTNIV EAIGYLAHLS SHRVSTDAPL
VRANAGDARI SAVAVNQGRE LAAHLLIKPH AANQGQINRT RVKSPRELLG VIKTVLFAPE
DLALVRGEPA ERRRYLDDII ATRRPRMAGV KADYDKVLKQ RNALLKTATI ALRRGYGTEE
GAAALATLDT WDGQLARLGA EVMAARFALV QDLSSQIRDA YQTIAPESRP AAVNYKTTID
QGLAQFGEFD AGIIEATLLT ELAAKRQREI ERGMSLVGPH RDDLELHLGG QPAKGFASHG
ETWSFALSMR IAEFNLLRSD GTDPILILDD VFSELDAGRR EKLVGIARDA EQVIITAAVS
DDLPANLADA ITARHTVTVR DTDAGRISLL DEQPDTQP
