RECF_SALAI
ID RECF_SALAI Reviewed; 376 AA.
AC A8LVH1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=Sare_0004;
OS Salinispora arenicola (strain CNS-205).
OC Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC Salinispora.
OX NCBI_TaxID=391037;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNS-205;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Foster B., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Jensen P.R., Moore B.S., Penn K., Jenkins C.,
RA Udwary D., Xiang L., Gontang E., Richardson P.;
RT "Complete sequence of Salinispora arenicola CNS-205.";
RL Submitted (OCT-2007) 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; CP000850; ABV95940.1; -; Genomic_DNA.
DR RefSeq; WP_012180253.1; NC_009953.1.
DR AlphaFoldDB; A8LVH1; -.
DR SMR; A8LVH1; -.
DR STRING; 391037.Sare_0004; -.
DR EnsemblBacteria; ABV95940; ABV95940; Sare_0004.
DR GeneID; 5707577; -.
DR KEGG; saq:Sare_0004; -.
DR PATRIC; fig|391037.6.peg.4; -.
DR eggNOG; COG1195; Bacteria.
DR HOGENOM; CLU_040267_1_1_11; -.
DR OMA; GESWSYA; -.
DR OrthoDB; 891841at2; -.
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..376
FT /note="DNA replication and repair protein RecF"
FT /id="PRO_1000079600"
FT BINDING 30..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00365"
SQ SEQUENCE 376 AA; 40525 MW; 3A0CD5AC31E9B493 CRC64;
MYVRRLELVD FRSYERVGVD LEPGANVLVG HNGVGKTNLI EALGYVATLD SHRVATDAPL
VRMGAGAAVI RCAVVHEGRE LLIELEIVPG RANRARLGRS PARRARDVLG ALRLVLFAPE
DLELVRGDPA ERRRYLDDLL VLRQPRYAGV RADYERVVRQ RNALLRTAYL ARKTGGTRGG
DLSTLAVWDD HLARHGAELL AGRLDLVAAL APHVTRAYDA VAAGTGAAGI AYRPSVELPT
PTTDRADLTA ALSAALAAGR SAEIERGTTL VGPHRDDLTL TLGPLPAKGY ASHGESWSLA
LALRLAGYDL LRVDGIEPVL VLDDVFAELD TGRRDRLAQL VGDASQLLVT CAVEEDVPAR
LRGARFVVRG GEVHRA
