ID M1M798_9CLOT Unreviewed; 360 AA.
AC M1M798;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
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 ECO:0000313|EMBL:AGF53849.1};
GN ORFNames=Cspa_c00040 {ECO:0000313|EMBL:AGF53849.1};
OS Clostridium saccharoperbutylacetonicum N1-4(HMT).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=931276 {ECO:0000313|EMBL:AGF53849.1, ECO:0000313|Proteomes:UP000011728};
RN [1] {ECO:0000313|EMBL:AGF53849.1, ECO:0000313|Proteomes:UP000011728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N1-4(HMT) {ECO:0000313|Proteomes:UP000011728};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium saccharoperbutylacetonicum N1-4(HMT).";
RL Submitted (FEB-2013) 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; CP004121; AGF53849.1; -; Genomic_DNA.
DR RefSeq; WP_015390185.1; NZ_AOIF01000160.1.
DR AlphaFoldDB; M1M798; -.
DR STRING; 36745.CLSAP_00040; -.
DR KEGG; csr:Cspa_c00040; -.
DR PATRIC; fig|931276.5.peg.4; -.
DR eggNOG; COG1195; Bacteria.
DR HOGENOM; CLU_040267_0_1_9; -.
DR OrthoDB; 9803889at2; -.
DR Proteomes; UP000011728; 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 CDD; cd03242; ABC_RecF; 1.
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; 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|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_00365};
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:UP000011728};
KW SOS response {ECO:0000256|ARBA:ARBA00023236, ECO:0000256|HAMAP-
KW Rule:MF_00365}.
FT DOMAIN 2..356
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT BINDING 30..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00365"
SQ SEQUENCE 360 AA; 41888 MW; 4E31A6DE5ACC34E0 CRC64;
MYVKNISLLN YRNYENLNIQ LIKNVNVFVG DNAQGKTNIL EAIYYSAFAK SHRTSKDKEL
INWKKDNAYI SLLVGKNRLD KKIDINILRD GKKAIKVNNI KVNKIGELFG TFNVVMFSPE
DLKVIKESPT IRRRMLDMEL SQINPKYYFN LVQYNKVLNE RNIILKSKIF NQDILEVYDM
QLIEYADYIV SKRLEYIDKI NFFGDEIHKE ITSSKEKIEF KYNCTVNLEN FKDNYLQKLK
ANVLKDRERG LTSVGPHRDD FSVFINSIDT KIFGSQGQQR TSILTMKFSS LKIIKQITGE
YPVLLLDDVL SELDSSRKRY ILSSINDIQT VITCTGVEDL NDYLDEKVKI FTVSNGKVLN
//
