ID   RECF_PARUW              Reviewed;         359 AA.
AC   Q6MAG9;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=DNA replication and repair protein RecF {ECO:0000255|HAMAP-Rule:MF_00365};
GN   Name=recF {ECO:0000255|HAMAP-Rule:MF_00365}; Synonyms=uvrF;
GN   OrderedLocusNames=pc1706;
OS   Protochlamydia amoebophila (strain UWE25).
OC   Bacteria; Chlamydiae; Parachlamydiales; Parachlamydiaceae;
OC   Candidatus Protochlamydia.
OX   NCBI_TaxID=264201;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UWE25;
RX   PubMed=15073324; DOI=10.1126/science.1096330;
RA   Horn M., Collingro A., Schmitz-Esser S., Beier C.L., Purkhold U.,
RA   Fartmann B., Brandt P., Nyakatura G.J., Droege M., Frishman D., Rattei T.,
RA   Mewes H.-W., Wagner M.;
RT   "Illuminating the evolutionary history of chlamydiae.";
RL   Science 304:728-730(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; BX908798; CAF24430.1; -; Genomic_DNA.
DR   RefSeq; WP_011176251.1; NC_005861.1.
DR   AlphaFoldDB; Q6MAG9; -.
DR   SMR; Q6MAG9; -.
DR   STRING; 264201.pc1706; -.
DR   EnsemblBacteria; CAF24430; CAF24430; PC_RS08170.
DR   KEGG; pcu:PC_RS08170; -.
DR   eggNOG; COG1195; Bacteria.
DR   HOGENOM; CLU_040267_0_1_0; -.
DR   OMA; GESWSYA; -.
DR   OrthoDB; 891841at2; -.
DR   Proteomes; UP000000529; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
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; IPR038729; Rad50/SbcC_AAA.
DR   InterPro; IPR042174; RecF_2.
DR   PANTHER; PTHR32182:SF0; PTHR32182:SF0; 2.
DR   Pfam; PF13476; AAA_23; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00611; recf; 1.
DR   PROSITE; PS00617; RECF_1; 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..359
FT                   /note="DNA replication and repair protein RecF"
FT                   /id="PRO_0000196437"
FT   BINDING         30..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00365"
SQ   SEQUENCE   359 AA;  41803 MW;  97E6D31361F5EC17 CRC64;
     MTLRSLYLQH FRNYEEAYLE FSPQFNLICG PNAKGKTTLL EAIHCLMIGR SFRTSHYPDL
     IQQQFESFFL EAQFYKHGIE QTLKFGFHTT DRKIIYNSTP LATLSNLLGL IPGVIITPDD
     VQLVKGSPQL RRQFLDIQIA QVDPLYVHHL NRYGRALKQR NHLLKMKQQI SIDSWEQEMT
     HSAAYLIQQR YQTITHLQNL AQKYYHLLSG ENDLLTLEYR SIANSNLSID EIKKLLVKQL
     CKNRQREMQI GYTLSGPHKD DLFVAIGGRD IRYFASEGQQ RSCVNALHFA EWNRLHQRGD
     GDFPLFMIDD IGMSLDSNRK DRLVEQLQSV GQVFLTTTDP KFLDHIDADK KIFTLPFYN