ID D6DAZ4_BIFLN Unreviewed; 412 AA.
AC D6DAZ4;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 24-JAN-2024, entry version 70.
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=BIL_19520 {ECO:0000313|EMBL:CBK71347.1};
OS Bifidobacterium longum subsp. longum F8.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=722911 {ECO:0000313|EMBL:CBK71347.1, ECO:0000313|Proteomes:UP000007063};
RN [1] {ECO:0000313|EMBL:CBK71347.1, ECO:0000313|Proteomes:UP000007063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F8 {ECO:0000313|EMBL:CBK71347.1,
RC ECO:0000313|Proteomes:UP000007063};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Bifidobacterium longum longum F8.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBK71347.1, ECO:0000313|Proteomes:UP000007063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F8 {ECO:0000313|EMBL:CBK71347.1,
RC ECO:0000313|Proteomes:UP000007063};
RA Pajon A.;
RL Submitted (MAR-2010) 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|ARBA:ARBA00025401, 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}.
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DR EMBL; FP929034; CBK71347.1; -; Genomic_DNA.
DR RefSeq; WP_015512556.1; NC_021008.1.
DR AlphaFoldDB; D6DAZ4; -.
DR KEGG; blg:BIL_19520; -.
DR PATRIC; fig|722911.3.peg.1493; -.
DR HOGENOM; CLU_040267_1_1_11; -.
DR Proteomes; UP000007063; 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; 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.
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}; SOS response {ECO:0000256|HAMAP-Rule:MF_00365}.
FT DOMAIN 3..356
FT /note="RecF/RecN/SMC N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02463"
FT REGION 381..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 30..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00365"
SQ SEQUENCE 412 AA; 44941 MW; 6B654692820C2C81 CRC64;
MHISRLALDH YRSWSQVVVD FVPGVNILFG KNGLGKTNLV EAVEVLSTGS SHRTSSTLPL
IERGQTTATI RANVADDAGQ TTTYEASIHA RGANRARINS GSSLYLRDII GKIPSVSFTP
EDQRLVSGDP GARRTMMNQA AALLEPGYMQ TLQQFTRIAK QRATLLKQLN ANVNNGQPMD
AVLSGLEIWT GQFIEAGVAL TRMRAHVIGL LAEPFAAIYA DLAGAGEQVT LTYAPSFDEV
LMFDDPHPQI SEHFQRIYPG EVARGVNLIG PQRDDMNLEL AGIPAREFAS NGEMWTMALA
LKMALFEIVR DRLGLQPIVI LDDVFAQLDD SRRTQILDFA RKQDQVLITV AAEGDVPDYE
SAHRIDVAAL DEPASVILPT LGNLSNSREN ESLGGYDEKT AVDSASVERK VS
//