GenomeNet

Database: UniProt
Entry: A0A151BW24_9MICO
LinkDB: A0A151BW24_9MICO
Original site: A0A151BW24_9MICO 
ID   A0A151BW24_9MICO        Unreviewed;       387 AA.
AC   A0A151BW24;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
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=AZH51_15450 {ECO:0000313|EMBL:KYH44169.1};
OS   Branchiibius sp. NY16-3462-2.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC   Branchiibius.
OX   NCBI_TaxID=1807500 {ECO:0000313|EMBL:KYH44169.1, ECO:0000313|Proteomes:UP000075667};
RN   [1] {ECO:0000313|EMBL:KYH44169.1, ECO:0000313|Proteomes:UP000075667}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NY16-3462-2 {ECO:0000313|EMBL:KYH44169.1};
RA   Lapierre P., Halse T.A., Shea J., Musser K.A., Escuyer V.E.;
RT   "Draft genome assembly of Branchiibius sp. 15-3462-2 from a clinical sputum
RT   sample.";
RL   Submitted (MAR-2016) 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}.
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:KYH44169.1}.
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; LVCF01000037; KYH44169.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151BW24; -.
DR   STRING; 1807500.AZH51_15450; -.
DR   Proteomes; UP000075667; 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   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:UP000075667};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578}.
FT   DOMAIN          2..354
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   387 AA;  42076 MW;  EE9D4804818339EF CRC64;
     MYVAHLVLTD FRSYDRVDLP LRPGPSLFVG LNGQGKTNLV EAIGYVASLG SHRVATDGPL
     IRAGCEQAII STAVVRDGRT QQVELEINPG RANRARLGGH PTRPRETLGT LRTVLFAPED
     LALVKGDPEQ RRRFLDDLLV ARQPRWSAAR SDYDKILKQR NALLKTARNS ADRAGVLASL
     PAWNDHLATA GAHLLYARLR LLRDLAPHVA QAYEQVSAGA GGAHATYRSS LDPEVAQRIA
     AGQVPEVQEL TEATHERFAQ VAQAEVERGL TLVGPHRDDV ELELGDLPAK GYASHGESWS
     FALALRLAAY QLLRHDLGTD PVLVLDDVFA ELDTGRRERL AALIEDCEQV LVTAAVPADI
     PASLVGPRFE VTRAAVSAIT VPQETPR
//
DBGET integrated database retrieval system