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Database: UniProt
Entry: A0A0K0Y0Z5_9RHOB
LinkDB: A0A0K0Y0Z5_9RHOB
Original site: A0A0K0Y0Z5_9RHOB 
ID   A0A0K0Y0Z5_9RHOB        Unreviewed;       369 AA.
AC   A0A0K0Y0Z5;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 37.
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   ECO:0000313|EMBL:AKS44572.1};
GN   ORFNames=OSB_00030 {ECO:0000313|EMBL:AKS44572.1};
OS   Octadecabacter temperatus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Octadecabacter.
OX   NCBI_TaxID=1458307 {ECO:0000313|EMBL:AKS44572.1, ECO:0000313|Proteomes:UP000067444};
RN   [1] {ECO:0000313|EMBL:AKS44572.1, ECO:0000313|Proteomes:UP000067444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB1 {ECO:0000313|EMBL:AKS44572.1,
RC   ECO:0000313|Proteomes:UP000067444};
RX   PubMed=26358607;
RA   Voget S., Billerbeck S., Simon M., Daniel R.;
RT   "Closed Genome Sequence of Octadecabacter temperatus SB1, the First
RT   Mesophilic Species of the Genus Octadecabacter.";
RL   Genome Announc. 3:e01051-15(2015).
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, 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; CP012160; AKS44572.1; -; Genomic_DNA.
DR   RefSeq; WP_049833055.1; NZ_FSRP01000002.1.
DR   AlphaFoldDB; A0A0K0Y0Z5; -.
DR   STRING; 1458307.OSB_00030; -.
DR   KEGG; otm:OSB_00030; -.
DR   PATRIC; fig|1458307.3.peg.3; -.
DR   OrthoDB; 9803889at2; -.
DR   Proteomes; UP000067444; 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: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   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   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   ECO:0000256|RuleBase:RU000578};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00365}; Reference proteome {ECO:0000313|Proteomes:UP000067444};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00365,
KW   ECO:0000256|RuleBase:RU000578}.
FT   DOMAIN          25..359
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   BINDING         33..40
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00365"
SQ   SEQUENCE   369 AA;  39997 MW;  998E5F7128998F14 CRC64;
     MSALFLSRLT LSHFRSHKRA SLDLDGRPVA IYGPNGAGKT NILEAVSILS PGRGLRRSSS
     EDMTRRPEAL GWKVTADLTS LSQNHEIEAW SENGASRQTK IDGKAAAQVA LGRIGRVLWL
     IPAMDRLWIE GAEGRRRFLD RATLSFEPLH AEAVLSYEKA MRERNRLLKD MVRDAHWYAA
     LERQMAESGA QIHRNRTHAL DLLSTAQDAA ETAFPTATLS LTHSDPACDA PKDPDALLSA
     FAGNRSRDMA AGRTLIGPHR ADLGAIFAAK DVPAKDCSTG EQKALLISLI LANARALADD
     FGAPPILLLD EVAAHLDADR RAALYSEITT LGAQAFMTGT GPELFAELGE SAQYVHVTDE
     NSVSQTTQA
//
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