ID   RECF_ACTPL              Reviewed;         360 AA.
AC   P24718; Q59132;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=DNA replication and repair protein RecF;
GN   Name=recF;
OS   Actinobacillus pleuropneumoniae (Haemophilus pleuropneumoniae).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=715;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Serotype III / Isolate 1421 (Nielsen);
RX   PubMed=1741300; DOI=10.1093/nar/20.3.615;
RA   Loynds B.M., Langford P.R., Kroll J.S.;
RT   "recF in Actinobacillus pleuropneumoniae.";
RL   Nucleic Acids Res. 20:615-615(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 347-360.
RC   STRAIN=Serotype III / Isolate 1421 (Nielsen);
RA   Langford P.R., Loynds B.M., Kroll J.S.;
RL   Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 249-360.
RC   STRAIN=ATCC 27088 / DSM 13472 / CCM 5869 / S4074 / Serotype 1;
RA   Helie M.C., Sirois M., Ouellet C., Boissinot M.;
RT   "Cloning, sequencing and overproduction of Mn-SOD and Cu,Zn-SOD of
RT   Actinobacillus pleuropneumoniae.";
RL   Submitted (MAR-1996) 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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RecF family. {ECO:0000305}.
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DR   EMBL; X63626; CAA45173.1; -; Genomic_DNA.
DR   EMBL; X99396; CAA67772.1; -; Genomic_DNA.
DR   EMBL; U51440; AAB02817.1; -; Genomic_DNA.
DR   PIR; S22814; S22814.
DR   AlphaFoldDB; P24718; -.
DR   SMR; P24718; -.
DR   STRING; 228399.appser1_180; -.
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..360
FT                   /note="DNA replication and repair protein RecF"
FT                   /id="PRO_0000196390"
FT   BINDING         30..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        249
FT                   /note="I -> M (in Ref. 3)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   360 AA;  41243 MW;  1F9EBCAF2AB0D95D CRC64;
     MPLSRLIINN FRNLQSLDLE LSPNFNFIVG HNGSGKTSLL EAIFYLGHGR SFKSHISNRI
     IHYQAEDFVL HARIDEGQHQ WSVGIQKKRS GDTLLKINGE DGNKISDLAH LLPMQVITPE
     GLTLLNGGPT FRRAFLDWGL FHQYTEFYSC WANLKRLLKQ RNAALHQVRS YAELKPWDIE
     LAKLAEIVSQ MRASYAEGLR PEIEKTCQFF LPELEIGVSF HQGWEKGTDY AEILAQGFER
     DKAMGYTMIG PQKADFRFRA NGLPVEDVLS RGQLKLLMCA LRLAQGEYLV AQKERQCLFL
     IDDFASELDP IKRELLAHRL RESGSQVFVT AITKDQLNQM QWQESEQDSL FQVQQGMLTK