RECF_CORDI
ID RECF_CORDI Reviewed; 397 AA.
AC Q6NKL5;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, 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=DIP0003;
OS Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype
OS gravis).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=257309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis;
RX PubMed=14602910; DOI=10.1093/nar/gkg874;
RA Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G.,
RA Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D.,
RA De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N.,
RA Holroyd S., Jagels K., Moule S., Quail M.A., Rabbinowitsch E.,
RA Rutherford K.M., Thomson N.R., Unwin L., Whitehead S., Barrell B.G.,
RA Parkhill J.;
RT "The complete genome sequence and analysis of Corynebacterium diphtheriae
RT NCTC13129.";
RL Nucleic Acids Res. 31:6516-6523(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; BX248354; CAE48514.1; -; Genomic_DNA.
DR RefSeq; WP_010933937.1; NC_002935.2.
DR AlphaFoldDB; Q6NKL5; -.
DR SMR; Q6NKL5; -.
DR STRING; 257309.DIP0003; -.
DR EnsemblBacteria; CAE48514; CAE48514; DIP0003.
DR KEGG; cdi:DIP0003; -.
DR HOGENOM; CLU_040267_1_1_11; -.
DR OMA; GESWSYA; -.
DR OrthoDB; 891841at2; -.
DR Proteomes; UP000002198; 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..397
FT /note="DNA replication and repair protein RecF"
FT /id="PRO_0000196409"
FT BINDING 30..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00365"
SQ SEQUENCE 397 AA; 43590 MW; 3C654ABDD1C5BB20 CRC64;
MYIRELSLRD FRSWPECTVT LEPGVTLFVG RNGFGKTNIV EAIGYVAHLG SHRVFHDSAL
VRQGKESARV SVTAVNHGRE LTAHLLIKAK GANQAQINRT RLKSPRELLG VVKTVLFSPE
DLSLVRGDPA ERRRYLDHVI ATRKPRLGGV KADYDKVLRQ RNSLLKTAGA ALRRGYGADD
GALSTLDVWD SQLARLGGQL IHARHSVVRE LGPLVHDAYA RIAPESRPAH IRYVSTVPFA
DVVELPSPEE FEAAMLAELG QCRDKEIDRG VSLVGPHRDD LDVVLGDYPA KGFASHGETW
SMCLSLRLAE FHLLRNDGTD PVLILDDVFA ELDTQRREKL VSVTAEAEQV LITAAVGDDL
PDTLTESAVH RHFVSVADTP EGRISLLDAA TGVPHDG
