ID   RECF_SALRD              Reviewed;         412 AA.
AC   Q2S6G1;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=SRU_0067;
OS   Salinibacter ruber (strain DSM 13855 / M31).
OC   Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis;
OC   Rhodothermaceae; Salinibacter.
OX   NCBI_TaxID=309807;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13855 / CECT 5946 / M31;
RX   PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA   Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J., Khouri H.,
RA   Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA   Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA   Legault B., Rodriguez-Valera F.;
RT   "The genome of Salinibacter ruber: convergence and gene exchange among
RT   hyperhalophilic bacteria and archaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
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; CP000159; ABC44337.1; -; Genomic_DNA.
DR   RefSeq; WP_011402853.1; NC_007677.1.
DR   RefSeq; YP_444220.1; NC_007677.1.
DR   AlphaFoldDB; Q2S6G1; -.
DR   SMR; Q2S6G1; -.
DR   STRING; 309807.SRU_0067; -.
DR   EnsemblBacteria; ABC44337; ABC44337; SRU_0067.
DR   KEGG; sru:SRU_0067; -.
DR   PATRIC; fig|309807.25.peg.71; -.
DR   eggNOG; COG1195; Bacteria.
DR   HOGENOM; CLU_040267_0_1_10; -.
DR   OMA; GESWSYA; -.
DR   Proteomes; UP000008674; 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; 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.
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..412
FT                   /note="DNA replication and repair protein RecF"
FT                   /id="PRO_0000236140"
FT   REGION          369..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         30..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00365"
SQ   SEQUENCE   412 AA;  45827 MW;  D1732E13668BE3E4 CRC64;
     MILHTLRLRS FRAHAESEFD LAPSINLLYG ANGAGKTNVL EAVHYLCLTK SFTASRDRYA
     VRKDAPYFEI EGRIGQVREE PMTVRLAYVP GEGKSIFVNG AELDRLADIV GTLPVVVFSP
     EDYDLTAGGP SERRRFVNNI LSQARSVYME TLMKYRRARR QRNEVLRSYK KRSAPPPDEL
     LAPWTEKLVG LGSRIVHRRQ QFLQAFADDL EEAYRRIDAV AERPTIEYDT IADLAPDATP
     DAIEDEFRAA LARKQGQERD RGTTLVGPQR DELVFRLDDL EVRRYGSQGQ HRTFAMALKL
     AQYFYLQQRN DTEPLLLLDD AFGKLDAERT GVFLDLLRSD AVGQSLVTAT RRGPFEPALN
     AEPASHRALQ VRPGGGTAAV TPDPEYARGE ATAANGAASA PTGADAASTS RD