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Database: UniProt
Entry: S9S8P8_9RHOB
LinkDB: S9S8P8_9RHOB
Original site: S9S8P8_9RHOB 
ID   S9S8P8_9RHOB            Unreviewed;       367 AA.
AC   S9S8P8;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 51.
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=Salmuc_00913 {ECO:0000313|EMBL:EPX82594.1};
OS   Salipiger mucosus DSM 16094.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Salipiger.
OX   NCBI_TaxID=1123237 {ECO:0000313|EMBL:EPX82594.1, ECO:0000313|Proteomes:UP000015347};
RN   [1] {ECO:0000313|Proteomes:UP000015347}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16094 {ECO:0000313|Proteomes:UP000015347};
RX   PubMed=25197501; DOI=10.4056/sigs.4909790;
RA   Riedel T., Spring S., Fiebig A., Petersen J., Kyrpides N.C., Goker M.,
RA   Klenk H.P.;
RT   "Genome sequence of the exopolysaccharide-producing Salipiger mucosus type
RT   strain (DSM 16094(T)), a moderately halophilic member of the Roseobacter
RT   clade.";
RL   Stand. Genomic Sci. 9:1331-1343(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:EPX82594.1}.
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DR   EMBL; APVH01000020; EPX82594.1; -; Genomic_DNA.
DR   RefSeq; WP_020041996.1; NZ_KE557275.1.
DR   AlphaFoldDB; S9S8P8; -.
DR   STRING; 1123237.Salmuc_00913; -.
DR   eggNOG; COG1195; Bacteria.
DR   HOGENOM; CLU_040267_2_0_5; -.
DR   OrthoDB; 9803889at2; -.
DR   Proteomes; UP000015347; 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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; IPR003593; AAA+_ATPase.
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   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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   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}; Reference proteome {ECO:0000313|Proteomes:UP000015347};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00365}.
FT   DOMAIN          24..362
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   BINDING         32..39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00365"
SQ   SEQUENCE   367 AA;  39646 MW;  80C20ABB349E055D CRC64;
     MSLHLSRLSL SHFRSHKRAV VEVDARPVAI FGPNGAGKTN LIEAVSLFSP GRGLRRAAAP
     DMARRPEDLG WTVLGLLQTP GGLHEIDFRS EGGSARQVQI DGKPAPQTAL GRLSRVLWLV
     PSMDRLWIEG PEGRRRFLDR MALSFFPDHA EAALAYEKAM RERNRLLKDQ VRDPHWYAAL
     EAQMAQGGAV LTANRRAALE RLSEAQAGAE TSFPAAELEL VSTEAEIPGT EADLAAALAE
     SRFRDLAAGR ALVGPHRADL RGVYAAKGVP AADCSTGEQK ALLISLILAN ARALATDIGA
     PPILLLDEVS AHLDSDRRAA LYDEICALGA QAWMTGTGPE LFDDLGARAQ RLHVTEEAGQ
     SLVEKRE
//
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