GenomeNet

Database: UniProt
Entry: A0A060QEP0_9PROT
LinkDB: A0A060QEP0_9PROT
Original site: A0A060QEP0_9PROT 
ID   A0A060QEP0_9PROT        Unreviewed;       368 AA.
AC   A0A060QEP0;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
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=ASAP_1360 {ECO:0000313|EMBL:CDG39405.1};
OS   Asaia bogorensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Asaia.
OX   NCBI_TaxID=91915 {ECO:0000313|EMBL:CDG39405.1, ECO:0000313|Proteomes:UP000027583};
RN   [1] {ECO:0000313|EMBL:CDG39405.1, ECO:0000313|Proteomes:UP000027583}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SF2.1 {ECO:0000313|EMBL:CDG39405.1,
RC   ECO:0000313|Proteomes:UP000027583};
RX   PubMed=24682158; DOI=10.1093/gbe/evu062;
RA   Chouaia B., Gaiarsa S., Crotti E., Comandatore F., Degli Esposti M.,
RA   Ricci I., Alma A., Favia G., Bandi C., Daffonchio D.;
RT   "Acetic acid bacteria genomes reveal functional traits for adaptation to
RT   life in insect guts.";
RL   Genome Biol. Evol. 6:912-920(2014).
RN   [2] {ECO:0000313|EMBL:CDG39405.1, ECO:0000313|Proteomes:UP000027583}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SF2.1 {ECO:0000313|EMBL:CDG39405.1,
RC   ECO:0000313|Proteomes:UP000027583};
RX   PubMed=24804722; DOI=10.1371/journal.pone.0096566;
RA   Degli Esposti M., Chouaia B., Comandatore F., Crotti E., Sassera D.,
RA   Lievens P.M., Daffonchio D., Bandi C.;
RT   "Evolution of mitochondria reconstructed from the energy metabolism of
RT   living bacteria.";
RL   PLoS ONE 9:e96566-e96566(2014).
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:CDG39405.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CBLX010000009; CDG39405.1; -; Genomic_DNA.
DR   RefSeq; WP_023977399.1; NZ_CBLX010000009.1.
DR   AlphaFoldDB; A0A060QEP0; -.
DR   eggNOG; COG1195; Bacteria.
DR   Proteomes; UP000027583; 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   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..349
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   368 AA;  40190 MW;  1D4C0E96B10958D5 CRC64;
     MRINRLVLTN FRNYERLVWT PQSRLVVLTG ENGAGKTNLL EALSLLAPGR GLRAASNAQI
     QRQDGGPWGV VARLNDVAGE GMDLATGTDP ANPVRRVFRL NNEVIRNQGQ IAPYCAVTWL
     TPQMDRLFSD PASGRRRFFD RLVLALDPNH ARESAAHERA VTQRNRLLAT RPDQKSWLDA
     LEDSIARHAV ALTASRMALV DAMNATALTD DTGFPIARVA LECEIAAELH RRPALLVEDG
     LRGKLAAARS EDAQRSTTSV GAHRTDFGLQ DAASGRSAAL SSSGQQKAML VHVILNHAGL
     TASRTGRAPF ILLDEPLVHL DSRRREGLLG YLRDQAFEVF LTGTDREQFA ALGDGVDYRC
     VTAGRFSA
//
DBGET integrated database retrieval system