ID   RECF_YERPS              Reviewed;         361 AA.
AC   Q663T4;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 2.
DT   03-AUG-2022, entry version 100.
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=YPTB3941;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAH23179.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BX936398; CAH23179.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_002209643.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q663T4; -.
DR   SMR; Q663T4; -.
DR   EnsemblBacteria; CAH23179; CAH23179; YPTB3941.
DR   GeneID; 66843641; -.
DR   KEGG; ypo:BZ17_2635; -.
DR   KEGG; yps:YPTB3941; -.
DR   PATRIC; fig|273123.14.peg.2763; -.
DR   OMA; GESWSYA; -.
DR   Proteomes; UP000001011; 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..361
FT                   /note="DNA replication and repair protein RecF"
FT                   /id="PRO_0000236164"
FT   BINDING         30..37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00365"
SQ   SEQUENCE   361 AA;  40468 MW;  6F389434F29FDEDA CRC64;
     MALTRLLIKD FRNIESADLA LAAGFNFLVG PNGSGKTSVL EAVYTLGHGR AFRSLQAGRV
     IRHECAEFVL HGRVDANERE ASVGLSKSRQ GDTKVRIDGT DGHKVAELAQ MLPMQLITPE
     GFTLLNGGPK FRRAFLDWGC FHNEPGFFTA WSNLKRLLKQ RNAALRQVSR YTQIRAWDQE
     IIPLAERISE WRAAYSDAIA ADISATCALF LPEFALSFSF QRGWDKESDY GELLARQFER
     DRALTYTAVG PHKADFRIRA DGTPVEDLLS RGQLKLLMCA LRLAQGEFLT RQSGRRCLYL
     LDDFASELDT GRRRLLAERL KATQAQVFVS AVSAEQVADM VGEKGKMFRV EHGKIEVQPQ
     D