(data stored in ACNUC7421 zone)

SWISSPROT: RECF_SALTO

ID   RECF_SALTO              Reviewed;         377 AA.
AC   A4X0U0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   11-DEC-2019, entry version 80.
DE   RecName: Full=DNA replication and repair protein RecF {ECO:0000255|HAMAP-Rule:MF_00365};
GN   Name=recF {ECO:0000255|HAMAP-Rule:MF_00365}; OrderedLocusNames=Strop_0005;
OS   Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440).
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Salinispora.
OX   NCBI_TaxID=369723;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440;
RX   PubMed=17563368; DOI=10.1073/pnas.0700962104;
RA   Udwary D.W., Zeigler L., Asolkar R.N., Singan V., Lapidus A., Fenical W.,
RA   Jensen P.R., Moore B.S.;
RT   "Genome sequencing reveals complex secondary metabolome in the marine
RT   actinomycete Salinispora tropica.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10376-10381(2007).
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:0000255|HAMAP-Rule:MF_00365}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00365}.
CC   -!- SIMILARITY: Belongs to the RecF family. {ECO:0000255|HAMAP-
CC       Rule:MF_00365}.
DR   EMBL; CP000667; ABP52490.1; -; Genomic_DNA.
DR   RefSeq; WP_011903927.1; NC_009380.1.
DR   STRING; 369723.Strop_0005; -.
DR   EnsemblBacteria; ABP52490; ABP52490; Strop_0005.
DR   GeneID; 5056434; -.
DR   KEGG; stp:Strop_0005; -.
DR   PATRIC; fig|369723.5.peg.5; -.
DR   eggNOG; ENOG4105C3X; Bacteria.
DR   eggNOG; COG1195; LUCA.
DR   HOGENOM; HOG000269561; -.
DR   KO; K03629; -.
DR   OMA; GESWSYA; -.
DR   Proteomes; UP000000235; Chromosome.
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; 1.20.1050.90; -; 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:SF0; PTHR32182:SF0; 1.
DR   Pfam; PF02463; SMC_N; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00611; recf; 1.
DR   PROSITE; PS00617; RECF_1; 1.
DR   PROSITE; PS00618; RECF_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4X0U0.
DR   SWISS-2DPAGE; A4X0U0.
KW   ATP-binding; Cytoplasm; DNA damage; DNA repair; DNA replication;
KW   DNA-binding; Nucleotide-binding; Reference proteome; SOS response.
FT   CHAIN           1..377
FT                   /note="DNA replication and repair protein RecF"
FT                   /id="PRO_1000079603"
FT   NP_BIND         30..37
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00365"
SQ   SEQUENCE   377 AA;  40648 MW;  D8C8F90C2273DBA3 CRC64;
     MYVRRLELVD FRSYERVGVD LEPGANVLVG PNGVGKTNLI EALGYVATLD SHRVATDAPL
     VRMGAAAGII RCAVVHEGRE LLVELEIVPG RANRARLGRS PARRARDVLG ALRLVLFAPE
     DLELVRGDPA QRRRYLDDLL VLRQPRYAGV RTDYERVVRQ RNALLRTAYL ARKTGGTRGG
     DLSTLAVWDD HLARHGAELL AGRLDLVAAL APHVNRAYDA VAAGAGAAGI AYRSSVELAS
     STADRADLTA ALSDALAAGR TAEIERGTTL VGPHRDELTL TLGPLPAKGY ASHGESWSFA
     LALRLAGYDL LRADGIEPVL VLDDVFAELD TGRRDRLAEL VGDASQLLVT CAVEEDLPAR
     LRGARFVVRE GEVQRVG
//

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