ID   RECF_PORGI              Reviewed;         364 AA.
AC   Q7MX24;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 111.
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=PG_0398;
OS   Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=242619;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-308 / W83;
RX   PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA   Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA   Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA   Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA   Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA   Fraser C.M.;
RT   "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT   gingivalis strain W83.";
RL   J. Bacteriol. 185:5591-5601(2003).
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; AE015924; AAQ65603.1; -; Genomic_DNA.
DR   RefSeq; WP_005873835.1; NC_002950.2.
DR   AlphaFoldDB; Q7MX24; -.
DR   SMR; Q7MX24; -.
DR   STRING; 242619.PG_0398; -.
DR   DNASU; 2551893; -.
DR   EnsemblBacteria; AAQ65603; AAQ65603; PG_0398.
DR   KEGG; pgi:PG_0398; -.
DR   PATRIC; fig|242619.8.peg.365; -.
DR   eggNOG; COG1195; Bacteria.
DR   HOGENOM; CLU_040267_0_1_10; -.
DR   OMA; GESWSYA; -.
DR   OrthoDB; 891841at2; -.
DR   BioCyc; PGIN242619:G1G02-373-MON; -.
DR   Proteomes; UP000000588; 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; IPR041685; AAA_15.
DR   InterPro; IPR001238; DNA-binding_RecF.
DR   InterPro; IPR018078; DNA-binding_RecF_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR042174; RecF_2.
DR   PANTHER; PTHR32182:SF0; PTHR32182:SF0; 1.
DR   Pfam; PF13175; AAA_15; 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; Reference proteome; SOS response.
FT   CHAIN           1..364
FT                   /note="DNA replication and repair protein RecF"
FT                   /id="PRO_0000196440"
FT   BINDING         30..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00365"
SQ   SEQUENCE   364 AA;  41811 MW;  99BE2EE5434A2476 CRC64;
     MIIEELHIVN FKSIAAADCR FSPKVNCLVG NNGMGKTNLL DALHFLSFCR SHLSVPDNMV
     VRHGEEMALL QGLYRDESGD GIELLLSIRP GKHKVLRRNK KEYERLSDHI GRFPLVIVSP
     QDYQLILGGS DERRRFMDQQ LCQQDPRYLS ALIQYNRHLQ QRNTMLKQDR HDDALMDVLE
     LQMGSYAAEI CNKRSRFIED FLPVFNDLYS DISGSAEKVS LSYRSHLADG IPLEELLRRS
     RPKDYLLGFS SCGVHKDELE MLLGGVLIRK IGSEGQNKTF LISMKLAQFR HQQLHGDETP
     ILLLDDIFDK LDATRVERII RLVGGNGFGQ IFITDTNRKN LDEIIASWSE DYRLFKIENG
     QIFQ