ID A0A317DW10_9PROT Unreviewed; 376 AA.
AC A0A317DW10;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=DNA replication and repair protein RecF {ECO:0000256|HAMAP-Rule:MF_00365};
GN Name=recF {ECO:0000256|HAMAP-Rule:MF_00365};
GN ORFNames=DKG74_19945 {ECO:0000313|EMBL:PWR18150.1};
OS Zavarzinia aquatilis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Zavarziniaceae; Zavarzinia.
OX NCBI_TaxID=2211142 {ECO:0000313|EMBL:PWR18150.1, ECO:0000313|Proteomes:UP000245461};
RN [1] {ECO:0000313|EMBL:PWR18150.1, ECO:0000313|Proteomes:UP000245461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HR-AS {ECO:0000313|EMBL:PWR18150.1,
RC ECO:0000313|Proteomes:UP000245461};
RA Lee Y., Jeon C.O.;
RT "Zavarzinia sp. HR-AS.";
RL Submitted (MAY-2018) 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}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00365}.
CC -!- SIMILARITY: Belongs to the RecF family. {ECO:0000256|HAMAP-
CC Rule:MF_00365}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWR18150.1}.
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DR EMBL; QGLE01000017; PWR18150.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317DW10; -.
DR OrthoDB; 9803889at2; -.
DR Proteomes; UP000245461; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; IPR003593; AAA+_ATPase.
DR InterPro; IPR001238; DNA-binding_RecF.
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 SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 DNA repair {ECO:0000256|HAMAP-Rule:MF_00365};
KW DNA replication {ECO:0000256|HAMAP-Rule:MF_00365};
KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00365};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00365}; Reference proteome {ECO:0000313|Proteomes:UP000245461};
KW SOS response {ECO:0000256|HAMAP-Rule:MF_00365}.
FT DOMAIN 29..368
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 37..44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00365"
SQ SEQUENCE 376 AA; 39815 MW; 9AB3BEBF644B9E71 CRC64;
MAVEVAHRHV SRLMLTDFRC YERVVLALRP GPVVLSGPNG AGKTNILEAV SLLSPGRGLR
HARAADMARM GGGGGFAVAA TIEGADLVAP LDLGTATAGE GDRRIVKRAG AMATQASLAR
DLSILWLTPT MDRIWTEGAA GRRRFLDRLV LARRPSHAEA HIAYDKARDE RMRLLLNGPR
DATWLAAIEE RAAKAGAAIA VARRGAVAEL NAEMAAAETP FPAAELTLTG EVEGWAETEE
AGLAARLKAA LAATRARDAE AGVQVTGPHR GDLTARHVAK DLPASHCSTG EQKALLIAIV
LAQAALVARA EGRAPILLLD EVAAHIDPGR RQMLYDLLSG RGLQAFLTGT ERSLFHGLED
RGQFFDVRDG QVAAAS
//
