ID L0E0T7_THIND Unreviewed; 366 AA.
AC L0E0T7;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=DNA replication and repair protein RecF {ECO:0000256|HAMAP-Rule:MF_00365};
GN Name=recF [H] {ECO:0000313|EMBL:AGA35439.1};
GN Synonyms=recF {ECO:0000256|HAMAP-Rule:MF_00365};
GN OrderedLocusNames=TVNIR_3813 {ECO:0000313|EMBL:AGA35439.1};
OS Thioalkalivibrio nitratireducens (strain DSM 14787 / UNIQEM 213 / ALEN2).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thioalkalivibrio.
OX NCBI_TaxID=1255043 {ECO:0000313|EMBL:AGA35439.1, ECO:0000313|Proteomes:UP000010809};
RN [1] {ECO:0000313|Proteomes:UP000010809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14787 / UNIQEM 213 / ALEN2
RC {ECO:0000313|Proteomes:UP000010809};
RA Tikhonova T.V., Pavlov A.R., Beletsky A.V., Mardanov A.V., Sorokin D.Y.,
RA Ravin N.V., Popov V.O.;
RT "Complete sequence of Thioalkalivibrio nitratireducens.";
RL Submitted (DEC-2012) 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}.
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DR EMBL; CP003989; AGA35439.1; -; Genomic_DNA.
DR RefSeq; WP_015260531.1; NC_019902.2.
DR AlphaFoldDB; L0E0T7; -.
DR STRING; 1255043.TVNIR_3813; -.
DR KEGG; tni:TVNIR_3813; -.
DR PATRIC; fig|1255043.3.peg.3848; -.
DR eggNOG; COG1195; Bacteria.
DR HOGENOM; CLU_040267_0_0_6; -.
DR OrthoDB; 9803889at2; -.
DR Proteomes; UP000010809; Chromosome.
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:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0006302; P:double-strand break repair; IEA:InterPro.
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; IPR038729; Rad50/SbcC_AAA.
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; PF13476; AAA_23; 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 10..48
FT /note="Rad50/SbcC-type AAA"
FT /evidence="ECO:0000259|Pfam:PF13476"
FT BINDING 29..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00365"
SQ SEQUENCE 366 AA; 40563 MW; A28CDABC3C3602FE CRC64;
MLVELWTRDV RNLQETRIRF GNELNLIVGA NGSGKTSLLE ACHVLALGRS FRTHRLARVA
RSGFGAFSVA GELWDSIHGR SWAGVEWKGQ RRSRLNGQWL EGHWEIARRM PLLSVHAGSF
ELLAGAPEER RRLLDWGSFY LHADFVQQWM TWRRAHEQRN AALRQQDTRT AARFEAIAAD
AGTRLTEMRA AVVAQLRHHL ADAASCGLRQ GLAGAIELTF RQGWPENETL SDAYARSRSS
DLERGFGQSG PQKADLEIRV GGRLIREASR GEQKRVLNVL VIAQGLLLVG IGPGGAAPLL
LLDDAVAEMD EAGLGGLMDA IAVLQWQCLA TTVDLKWALR TASRYRGAEM FHVKQGTLLR
SHVPGD
//
