ID A0A1I0RC56_9BACT Unreviewed; 358 AA.
AC A0A1I0RC56;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=SAMN05428988_4815 {ECO:0000313|EMBL:SEW38360.1};
OS Chitinophaga sp. YR573.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=1881040 {ECO:0000313|EMBL:SEW38360.1, ECO:0000313|Proteomes:UP000198758};
RN [1] {ECO:0000313|EMBL:SEW38360.1, ECO:0000313|Proteomes:UP000198758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YR573 {ECO:0000313|EMBL:SEW38360.1,
RC ECO:0000313|Proteomes:UP000198758};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOJF01000002; SEW38360.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0RC56; -.
DR STRING; 1881040.SAMN05428988_4815; -.
DR Proteomes; UP000198758; 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.
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};
KW SOS response {ECO:0000256|HAMAP-Rule:MF_00365,
KW ECO:0000256|RuleBase:RU000578}.
FT DOMAIN 1..334
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT BINDING 29..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00365"
SQ SEQUENCE 358 AA; 41379 MW; 981550F04D65D86E CRC64;
MLRKISLVQF KNYTGETFGF NKRIVGITGR NGSGKTNLLD AIYYLCFTKS YFTSSEAQNT
QYLTNGFRLE GILDKDDHEN RIVCTLKDGK KDIALNDEHY ERFSQHIGKF PAVMIAPDDA
EIILGGSEER RKWLDALLCQ LHPGYLEHLI TYQKILLQRN SLLKTIASQG RSQDALLDVF
DEQLVQHGTP VFEWRRSFLP AFIQQVQKLY DYLAGHHEVV SIQYQCGLHE QSFAQLLKAN
RYKDHMMQRT TGGIHRDDLL FLLDDHAMKS SASQGQRKSF LFALKLAQYE VIKEYKKFPP
LLLLDDVFEK LDQDRVSRLI NLVSGPVYGQ VFITDTHAVR LLDAFKENQE SFQLVEMR
//