RECF_LACE2
ID RECF_LACE2 Reviewed; 363 AA.
AC C4Z176;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-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};
GN OrderedLocusNames=EUBELI_00004;
OS Lachnospira eligens (strain ATCC 27750 / DSM 3376 / VPI C15-48 / C15-B4)
OS (Eubacterium eligens).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae;
OC Lachnospira.
OX NCBI_TaxID=515620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27750 / DSM 3376 / VPI C15-48 / C15-B4;
RX PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA Hettich R.L., Gordon J.I.;
RT "Characterizing a model human gut microbiota composed of members of its two
RT dominant bacterial phyla.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009).
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; CP001104; ACR71050.1; -; Genomic_DNA.
DR RefSeq; WP_012738288.1; NC_012778.1.
DR AlphaFoldDB; C4Z176; -.
DR SMR; C4Z176; -.
DR STRING; 515620.EUBELI_00004; -.
DR EnsemblBacteria; ACR71050; ACR71050; EUBELI_00004.
DR GeneID; 41354803; -.
DR KEGG; eel:EUBELI_00004; -.
DR eggNOG; COG1195; Bacteria.
DR HOGENOM; CLU_040267_0_1_9; -.
DR OMA; GESWSYA; -.
DR OrthoDB; 891841at2; -.
DR Proteomes; UP000001476; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
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; IPR038729; Rad50/SbcC_AAA.
DR InterPro; IPR042174; RecF_2.
DR PANTHER; PTHR32182:SF0; PTHR32182:SF0; 1.
DR Pfam; PF13476; AAA_23; 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..363
FT /note="DNA replication and repair protein RecF"
FT /id="PRO_1000205482"
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; 41773 MW; 5EC0E528F203F8B1 CRC64;
MIVESVELKD FRNYEFLDMN FNEHVNIIYG DNAQGKTNIL ESIYMCSTSK SHRGSKDREI
VRFGEDESHI KLNVLKHGMK YRIDMHLKKN KTKGIAVNGI PIKKAVELFG IINIVFFSPE
DLNIIKNGPS ERRRFMDMEL SQLDKIYLSN LVNYNKVLNQ RNKLLKDIAF SPSEQLMQTL
DIWDMQLVKY GSLIIKGRKS FIEKINTIIS DIHSRLTGGI ENIKVCYVPD VDVNDFEEEV
RNSRQKDIKY KVTGKGPHKD DLIFLINDND VRKYGSQGQQ RTAALSLKLS EIELVKLVIK
DTPVLLLDDV LSELDSNRQN FLINSIGDIQ TIVTCTGLEE FINNRMNINK IFKVTDGHVV
NEN
