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Database: UniProt
Entry: A0A1X6X3X5_9MICO
LinkDB: A0A1X6X3X5_9MICO
Original site: A0A1X6X3X5_9MICO 
ID   A0A1X6X3X5_9MICO        Unreviewed;       429 AA.
AC   A0A1X6X3X5;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
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=FM110_10045 {ECO:0000313|EMBL:SLM93533.1};
OS   Brachybacterium nesterenkovii.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC   Brachybacterium.
OX   NCBI_TaxID=47847 {ECO:0000313|EMBL:SLM93533.1, ECO:0000313|Proteomes:UP000195981};
RN   [1] {ECO:0000313|EMBL:SLM93533.1, ECO:0000313|Proteomes:UP000195981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP104813 {ECO:0000313|EMBL:SLM93533.1,
RC   ECO:0000313|Proteomes:UP000195981};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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       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; FWFG01000089; SLM93533.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X6X3X5; -.
DR   OrthoDB; 9803889at2; -.
DR   Proteomes; UP000195981; 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   CDD; cd03242; ABC_RecF; 1.
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}; Reference proteome {ECO:0000313|Proteomes:UP000195981};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578}.
FT   DOMAIN          3..390
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   429 AA;  46708 MW;  47370D75A229EE67 CRC64;
     MELTALHLTD YRSYPRLELA LKPGVTVFVG PNGQGKTNIV EAVWYLATLS SHRVPHDAAL
     VARGQQTAIV RASFLRAGRP LQVDLQITPG RSNTARVQGA ALSRLRDLLG EVRAVLFAPE
     DLSLVKGDPD GRRRFLDELL FEIAPRFASV KADYDRVLKQ RSHLLKQMRS MKRGGSGRSV
     GGLDPAETAA STLEVWDTQL AGLGAELTRA RIHLVNRLRP HLGYSYLRVA TDEGAEAALD
     LSPEDRGTVD SPADIGYRGA VVDALGAPDG TLPSTLELRD ALLAIIAERR EDEIDRGVSL
     VGPHRDDLEI RLNDFPAKGY ASHGESWSLA LALRLASYDL LRLEEGDLGD GEPILMLDDV
     FSELDAHRRE RLGRIITGAR QVLITTANDS DIPDSLEGEI QVVDVTRGSA VVREGGFRRG
     IADTGSAAW
//
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