ID F6ABW1_PSEF1 Unreviewed; 378 AA.
AC F6ABW1;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=DNA replication and repair protein RecF {ECO:0000256|ARBA:ARBA00020170, ECO:0000256|HAMAP-Rule:MF_00365};
GN Name=recF {ECO:0000256|HAMAP-Rule:MF_00365};
GN OrderedLocusNames=Psefu_0003 {ECO:0000313|EMBL:AEF19990.1};
OS Pseudomonas fulva (strain 12-X).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=743720 {ECO:0000313|EMBL:AEF19990.1, ECO:0000313|Proteomes:UP000000686};
RN [1] {ECO:0000313|EMBL:AEF19990.1, ECO:0000313|Proteomes:UP000000686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12-X {ECO:0000313|Proteomes:UP000000686};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Pagani I., Davenport K., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Lcollab F.I.,
RA Woyke T.;
RT "Complete sequence of Pseudomonas fulva 12-X.";
RL Submitted (APR-2011) 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:0000256|HAMAP-Rule:MF_00365, ECO:0000256|RuleBase:RU000578}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00365,
CC ECO:0000256|RuleBase:RU000578}.
CC -!- SIMILARITY: Belongs to the RecF family. {ECO:0000256|ARBA:ARBA00008016,
CC ECO:0000256|HAMAP-Rule:MF_00365, ECO:0000256|RuleBase:RU000578}.
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DR EMBL; CP002727; AEF19990.1; -; Genomic_DNA.
DR AlphaFoldDB; F6ABW1; -.
DR STRING; 743720.Psefu_0003; -.
DR KEGG; pfv:Psefu_0003; -.
DR eggNOG; COG1195; Bacteria.
DR HOGENOM; CLU_040267_0_0_6; -.
DR Proteomes; UP000000686; 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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.1050.90; RecF/RecN/SMC, N-terminal domain; 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 NCBIfam; TIGR00611; recf; 1.
DR PANTHER; PTHR32182; DNA REPLICATION AND REPAIR PROTEIN RECF; 1.
DR PANTHER; PTHR32182:SF0; DNA REPLICATION AND REPAIR PROTEIN RECF; 1.
DR Pfam; PF02463; SMC_N; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00617; RECF_1; 1.
DR PROSITE; PS00618; RECF_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00365};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00365};
KW DNA damage {ECO:0000256|HAMAP-Rule:MF_00365,
KW ECO:0000256|RuleBase:RU000578};
KW DNA repair {ECO:0000256|HAMAP-Rule:MF_00365,
KW ECO:0000256|RuleBase:RU000578};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW Rule:MF_00365};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_00365};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00365}; Reference proteome {ECO:0000313|Proteomes:UP000000686};
KW SOS response {ECO:0000256|HAMAP-Rule:MF_00365,
KW ECO:0000256|RuleBase:RU000578}.
FT DOMAIN 14..369
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT BINDING 41..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00365"
SQ SEQUENCE 378 AA; 43143 MW; E0DD5F0B037C5C19 CRC64;
MLSPPFSLGL FMSLTRINFT AVRNLEPSTL LPSPRINILY GDNGSGKTSV LEGIHLLGLA
RSFRSARLLP VIQYEQQVCT LFGQVQLSDG RLSNLGVSRD RQGEFQIRID GQNARSAAQL
AETLPLQLIN PDSFRLLEGS PKIRRQFLDW GVFHVEHRFL PAWQRLQKAL KQRNSWLRRG
TLDPVSQAAW DRELCLASDE IDSYRRSYIQ QLKPVFERTL SELVELQGLT LSYYRGWDKE
RPLSEVLTSS LLRDQQIGHT QSGPQRADLR LRLGAHNAAD ILSRGQQKLV VCALRIAQGH
LVDQAKRGQC IYLVDDLPSE LDEQHRRALC RLLEDLNCQV FITCVDHELL SDGWQTDTPV
SMFHVEHGRI TQTHDHRE
//
