RECF_STRM5
ID RECF_STRM5 Reviewed; 364 AA.
AC B4SR07;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=Smal_0003;
OS Stenotrophomonas maltophilia (strain R551-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=391008;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R551-3;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Taghavi S.,
RA Monchy S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.;
RT "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001111; ACF49708.1; -; Genomic_DNA.
DR RefSeq; WP_012509600.1; NC_011071.1.
DR AlphaFoldDB; B4SR07; -.
DR SMR; B4SR07; -.
DR STRING; 391008.Smal_0003; -.
DR EnsemblBacteria; ACF49708; ACF49708; Smal_0003.
DR KEGG; smt:Smal_0003; -.
DR eggNOG; COG1195; Bacteria.
DR HOGENOM; CLU_040267_0_0_6; -.
DR OMA; GESWSYA; -.
DR OrthoDB; 891841at2; -.
DR BioCyc; SMAL391008:SMAL_RS00015-MON; -.
DR Proteomes; UP000001867; 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..364
FT /note="DNA replication and repair protein RecF"
FT /id="PRO_1000121159"
FT BINDING 30..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00365"
SQ SEQUENCE 364 AA; 40738 MW; 1B29ED4E9AA2E596 CRC64;
MQIRRLALHQ LRRFNAVELS PQPGLNLLTG DNGAGKTSIL EALHLMAYGR SFRGRVRDGL
VRQGQEALEI FVEWDEQRAS HPPHRRKAGL RHSGQDWKGR LDGEDVAQLG NLCAALAVVT
FEPGSHALVS GGGEPRRRFL DWGLFHVEPD FLSLWRRYSR ALKQRNALLK QGGPSRMLDT
WDHELAEAGE PLTSRRQHYL ERLQQRTVAL AAELAPQLGI QAMELSPGWR RHELPLADAL
LLARERDRQA GYTSVGPHRA DWSVDFHNIP GRDALSRGQA KLTALACLLA QAEDYAEQRG
EWPVIALDDL ASELDRTHQA RVLERLLGGP AQIFVTATET PAALQELTHI ARFHVEHAQI
VAVP