ID   RECF_MYCTO              Reviewed;         385 AA.
AC   P9WHI8; L0T293; P77896; Q59586;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=DNA replication and repair protein RecF;
GN   Name=recF; OrderedLocusNames=MT0003;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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; AE000516; AAK44226.1; -; Genomic_DNA.
DR   PIR; S70984; S70984.
DR   RefSeq; WP_003899768.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WHI8; -.
DR   SMR; P9WHI8; -.
DR   EnsemblBacteria; AAK44226; AAK44226; MT0003.
DR   KEGG; mtc:MT0003; -.
DR   PATRIC; fig|83331.31.peg.3; -.
DR   HOGENOM; CLU_040267_1_1_11; -.
DR   Proteomes; UP000001020; 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..385
FT                   /note="DNA replication and repair protein RecF"
FT                   /id="PRO_0000428179"
FT   BINDING         30..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   385 AA;  42200 MW;  461D715A7C79F1FE CRC64;
     MYVRHLGLRD FRSWACVDLE LHPGRTVFVG PNGYGKTNLI EALWYSTTLG SHRVSADLPL
     IRVGTDRAVI STIVVNDGRE CAVDLEIATG RVNKARLNRS SVRSTRDVVG VLRAVLFAPE
     DLGLVRGDPA DRRRYLDDLA IVRRPAIAAV RAEYERVLRQ RTALLKSVPG ARYRGDRGVF
     DTLEVWDSRL AEHGAELVAA RIDLVNQLAP EVKKAYQLLA PESRSASIGY RASMDVTGPS
     EQSDTDRQLL AARLLAALAA RRDAELERGV CLVGPHRDDL ILRLGDQPAK GFASHGEAWS
     LAVALRLAAY QLLRVDGGEP VLLLDDVFAE LDVMRRRALA TAAESAEQVL VTAAVLEDIP
     AGWDARRVHI DVRADDTGSM SVVLP