ID   RECF_ACIAD              Reviewed;         358 AA.
AC   Q6FG19;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 120.
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=ACIAD0003;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
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; CR543861; CAG66988.1; -; Genomic_DNA.
DR   RefSeq; WP_004930061.1; NC_005966.1.
DR   AlphaFoldDB; Q6FG19; -.
DR   SMR; Q6FG19; -.
DR   STRING; 62977.ACIAD0003; -.
DR   EnsemblBacteria; CAG66988; CAG66988; ACIAD0003.
DR   GeneID; 45232535; -.
DR   KEGG; aci:ACIAD0003; -.
DR   eggNOG; COG1195; Bacteria.
DR   HOGENOM; CLU_040267_0_0_6; -.
DR   OMA; GESWSYA; -.
DR   OrthoDB; 891841at2; -.
DR   BioCyc; ASP62977:ACIAD_RS00015-MON; -.
DR   Proteomes; UP000000430; 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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003395; RecF/RecN/SMC_N.
DR   InterPro; IPR042174; RecF_2.
DR   PANTHER; PTHR32182:SF0; PTHR32182:SF0; 2.
DR   Pfam; PF02463; SMC_N; 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..358
FT                   /note="DNA replication and repair protein RecF"
FT                   /id="PRO_1000048497"
FT   BINDING         30..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00365"
SQ   SEQUENCE   358 AA;  41077 MW;  162E43142F66E417 CRC64;
     MQITRLNIER VRNLKAVALS GLQPFNIFYG ANGSGKTSIL EAVHLLATGR SFRTHMPKHY
     IQQNAQDAII FAQSLSEKIG MQKLLSGEQL IKVNGDTVAT QGQLAKLLPL QHLDPQSTDI
     IDHGAKPRRQ LLDWLMFHVE PEFYFAWQYY SRALKQRNML LKTKRQLSLA ELEPWNKMLS
     EYGEMLHSQR LVTVERWKDF FQQDLAQLLP DLQIELEYSP GFHSEVGLWQ DLLNYHNKDV
     ERRYTEYGPH RADLRLKTAL GDADDVLSRG QKKLLMMALK LSQIAMLHAS NKETVVLLDD
     LTAELDSNAQ RRLIERLSQL GSQVFITTLD HQAVTQHLDG LSISYQLYNV DHGQVHAV