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Database: UniProt
Entry: A0A0G0IQ55_9BACT
LinkDB: A0A0G0IQ55_9BACT
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ID   A0A0G0IQ55_9BACT        Unreviewed;       376 AA.
AC   A0A0G0IQ55;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
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   ORFNames=US72_C0003G0034 {ECO:0000313|EMBL:KKQ53095.1};
OS   Microgenomates group bacterium GW2011_GWC1_38_12.
OC   Bacteria.
OX   NCBI_TaxID=1618512 {ECO:0000313|EMBL:KKQ53095.1, ECO:0000313|Proteomes:UP000034948};
RN   [1] {ECO:0000313|EMBL:KKQ53095.1, ECO:0000313|Proteomes:UP000034948}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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|ARBA:ARBA00008016,
CC       ECO:0000256|HAMAP-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:KKQ53095.1}.
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DR   EMBL; LBUB01000003; KKQ53095.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0IQ55; -.
DR   PATRIC; fig|1618512.3.peg.221; -.
DR   Proteomes; UP000034948; 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: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.
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|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}; SOS response {ECO:0000256|HAMAP-Rule:MF_00365}.
FT   DOMAIN          3..373
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   376 AA;  43199 MW;  7B37C212E1570370 CRC64;
     MLIRKIHLTN FRSFKDKILE FSPKTTVIVG PNASGKTNII EAIFLLSTGK SFRARIEEEM
     INYDEEIARV KGAIIDRGDK ERSGTNLEVV LTRGEITIGK SPEKVERVAR KKLLINGVGK
     RLIDFAGTFK TVLFGPWDMG LVTESPSVRR KFLDTVISQV DREYRRASMS YEKGLRQRNR
     LLWRIREEGL SRSQLLFWDK LLIRNGDYLS QKREEFIEFI NNFPFSLPAQ AGVFHFPFNI
     EYDKSAISEA RLEQYAEEEV ASATTLVGPH RDDFIMKSTT GIKGTKSIKG RELARYGSRG
     EQRMGVLWLK LAELAFIEKV TEEKPTLLLD DIFSELDHEH RDIVFEAAKA QQTVITTAEP
     HYMEGFEKIE RISLQV
//
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