ID   RECF_CHLMU              Reviewed;         365 AA.
AC   Q9PKW5;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=DNA replication and repair protein RecF;
GN   Name=recF; OrderedLocusNames=TC_0346;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RecF family. {ECO:0000305}.
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DR   EMBL; AE002160; AAF39207.1; -; Genomic_DNA.
DR   PIR; B81713; B81713.
DR   RefSeq; WP_010230223.1; NZ_CP027217.1.
DR   AlphaFoldDB; Q9PKW5; -.
DR   SMR; Q9PKW5; -.
DR   STRING; 243161.TC_0346; -.
DR   EnsemblBacteria; AAF39207; AAF39207; TC_0346.
DR   GeneID; 1246389; -.
DR   KEGG; cmu:TC_0346; -.
DR   eggNOG; COG1195; Bacteria.
DR   HOGENOM; CLU_040267_0_1_0; -.
DR   OMA; GESWSYA; -.
DR   OrthoDB; 891841at2; -.
DR   Proteomes; UP000000800; 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..365
FT                   /note="DNA replication and repair protein RecF"
FT                   /id="PRO_0000196404"
FT   BINDING         30..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   365 AA;  41321 MW;  FD97CE97B10C8958 CRC64;
     MRVHSLFLKD FRNYSELRLE LGPEMNSIFG LNAQGKTNIL EALYILSLGR SFRTSRLTEA
     IRFGSSHFFI EAVFSQNQVF HTLSIQVDKR GKKILFDGAP ITKLSALVGL FPVILFSVKD
     TTIIEGSPAE RRRFLDLLLA QASEKYTGQI ALYHKALDQR NAAIKTQDYK TIAAWNSPLI
     AYGSLVALLR YECAKKLHKI FQNLWDNTLK ETLSLRYESS LITTESPTLN DIASNYYEQL
     RLANTKDFEL GYTTVGPHRD ELIITLNDLP VSKFSSEGQK HSLLAVLRFA ECVYLQEEFL
     IHPLLCMDDI HACLDQNRLD QLFQLSTSLG QTVTTSTICP NHLDSNSSIF HVTQAQVSLV
     TSNFL