ID   RECF_PECCP              Reviewed;         361 AA.
AC   C6DGH9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=PC1_0003;
OS   Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=561230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL   Submitted (JUL-2009) 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; CP001657; ACT11066.1; -; Genomic_DNA.
DR   RefSeq; WP_010281217.1; NC_012917.1.
DR   AlphaFoldDB; C6DGH9; -.
DR   SMR; C6DGH9; -.
DR   STRING; 561230.PC1_0003; -.
DR   EnsemblBacteria; ACT11066; ACT11066; PC1_0003.
DR   GeneID; 57242314; -.
DR   GeneID; 61410201; -.
DR   KEGG; pct:PC1_0003; -.
DR   eggNOG; COG1195; Bacteria.
DR   HOGENOM; CLU_040267_0_0_6; -.
DR   OMA; GESWSYA; -.
DR   OrthoDB; 891841at2; -.
DR   Proteomes; UP000002736; 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; 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..361
FT                   /note="DNA replication and repair protein RecF"
FT                   /id="PRO_1000205500"
FT   BINDING         30..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00365"
SQ   SEQUENCE   361 AA;  40707 MW;  EFC91E77ABF9BF2C CRC64;
     MALTRLLIKD FRNIEAADLA LVPGFNFLVG ANGSGKTSVL EAIYTLGHGR AFRSIQAGRV
     IRHDQPEFVL HGRIDGTETE RSVGLSKNRQ GDSKVRIDGS DGHKVAELAQ LLPIQLITPE
     GFTLLNGGPK FRRAFLDWGC FHNEPGFFAA WSNMKRLLRQ RNAALRQVSH YGQLRAWDQE
     LVPLAERISE WRAQYSAAIA NDIATTCTQF LPEFSLSFSF QRGWDKESEY AELLERQFER
     DRMLGYTALG PHKADFRIRA SGVAVEDMLS RGQLKLLMCA LRLAQGEFLT RQNGLRCLYL
     IDDFASELDS TRRRLLAERL KATHAQVFVS AVSAEQIEDM VGEKGKMFRV EQGKITVQSQ
     D