RECF_COXBU
ID RECF_COXBU Reviewed; 357 AA.
AC Q83FD6;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 104.
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=CBU_0003;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(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; AE016828; AAO89573.2; -; Genomic_DNA.
DR RefSeq; NP_819059.2; NC_002971.3.
DR RefSeq; WP_010957316.1; NC_002971.4.
DR AlphaFoldDB; Q83FD6; -.
DR SMR; Q83FD6; -.
DR STRING; 227377.CBU_0003; -.
DR EnsemblBacteria; AAO89573; AAO89573; CBU_0003.
DR GeneID; 1207923; -.
DR KEGG; cbu:CBU_0003; -.
DR PATRIC; fig|227377.7.peg.4; -.
DR eggNOG; COG1195; Bacteria.
DR HOGENOM; CLU_040267_0_0_6; -.
DR OMA; GESWSYA; -.
DR Proteomes; UP000002671; 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:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0000731; P:DNA synthesis involved in DNA repair; IBA:GO_Central.
DR GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
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; Reference proteome; SOS response.
FT CHAIN 1..357
FT /note="DNA replication and repair protein RecF"
FT /id="PRO_0000196412"
FT BINDING 31..38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00365"
SQ SEQUENCE 357 AA; 41039 MW; 55560EBA41080DC7 CRC64;
MPYIGSLKVN QFRNLADVDI TPHSQFNFFF GQNGAGKTSI LESIYYLSVG RSFRTHLPQR
LIQDNTDRFL IFITLYNGTQ FIPLGVERDC HGDRCLRING ETASSWSLAA KRLPLCSLSA
MSHRFLLDGP RVRRQFLDWL MFHVEPSFFS IWQRLQRSLK QRNAALKAKL PLGEITHWDK
MLVEDGERLH QLRQNVVTEF KPLFTQMLQQ FLPAYPLIGH YFRGWSEKYS LMEQLQINLK
QDLQRGYTQA GPQRADFRLT LGDLPAQDIL SQGQQKLVTY ALHFAQGLLL KEKTGISPIY
LIDDLPAELD ANKRDCVIDL VNCLESQVFI SGIDPNEIRL PPHSTLFHVK HGKVAAL