ID   RECF_ACIBY              Reviewed;         360 AA.
AC   B0VAF5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=ABAYE0003;
OS   Acinetobacter baumannii (strain AYE).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=509173;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AYE;
RX   PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA   Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA   Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA   Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA   Weissenbach J., Cruveiller S.;
RT   "Comparative analysis of Acinetobacters: three genomes for three
RT   lifestyles.";
RL   PLoS ONE 3:E1805-E1805(2008).
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; CU459141; CAM84995.1; -; Genomic_DNA.
DR   RefSeq; WP_000550807.1; NC_010410.1.
DR   AlphaFoldDB; B0VAF5; -.
DR   SMR; B0VAF5; -.
DR   EnsemblBacteria; CAM84995; CAM84995; ABAYE0003.
DR   GeneID; 66395339; -.
DR   KEGG; aby:ABAYE0003; -.
DR   HOGENOM; CLU_040267_0_0_6; -.
DR   OMA; GESWSYA; -.
DR   Proteomes; UP000002446; 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; 1.
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; SOS response.
FT   CHAIN           1..360
FT                   /note="DNA replication and repair protein RecF"
FT                   /id="PRO_1000205468"
FT   BINDING         30..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00365"
SQ   SEQUENCE   360 AA;  41144 MW;  2E0A7B32568E082F CRC64;
     MHLTRLNIER VRNLKTVALH GLQPFNVFYG ANGSGKTSIL EAIHLLATGR SFRTHIPKNY
     IQYEADDAIV FAQSATEKIG MQKLASGEQL MKVNGDTVAT QGQLAKLLPL QHIDPQSTDI
     IDHGAKPRRQ LLDWLMFHVE PEFYFAWQYY SRALKQRNTL LKTRRNLSLA DLEPWNKMLS
     DYGEILHSQR LSIVEQWNVY FQNDLSQLLP DLEIELEYSP GFHTEQGLMQ DLLNQHQKDI
     ERRYTEYGPH RADLRLKTPF GHADDVLSRG QKKLLIIALK LSQIAMLHAS NKETVVLLDD
     LTAELDLTAQ QRLIERLSQL GSQVFMTTLD HASVKKHLHD LSISYQLFSV ESGQVSLAAP