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RECN_BACSU
ID   RECN_BACSU              Reviewed;         576 AA.
AC   P17894; P19671; P71027;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=DNA repair protein RecN;
DE   AltName: Full=Recombination protein N;
GN   Name=recN; OrderedLocusNames=BSU24240;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / PY79;
RX   PubMed=2106508; DOI=10.1128/jb.172.3.1306-1311.1990;
RA   van Hoy B.E., Hoch J.A.;
RT   "Characterization of the spoIVB and recN loci of Bacillus subtilis.";
RL   J. Bacteriol. 172:1306-1311(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   SEQUENCE REVISION TO 189 AND 546-548.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-111.
RC   STRAIN=168 / EMG50;
RX   PubMed=2507400; DOI=10.1016/0378-1119(89)90247-3;
RA   North A.K., Smith M.C.M., Baumberg S.;
RT   "Nucleotide sequence of a Bacillus subtilis arginine regulatory gene and
RT   homology of its product to the Escherichia coli arginine repressor.";
RL   Gene 80:29-38(1989).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 346-576.
RC   STRAIN=168 / JH642;
RX   PubMed=9044256; DOI=10.1046/j.1365-2958.1997.2091573.x;
RA   Oke V., Shchepetov M., Cutting S.;
RT   "SpoIVB has two distinct functions during spore formation in Bacillus
RT   subtilis.";
RL   Mol. Microbiol. 23:223-230(1997).
RN   [7]
RP   SUBCELLULAR LOCATION, AND TEMPORAL ORDER OF DNA DOUBLE-STRAND BREAK
RP   RECRUITMENT.
RC   STRAIN=168 / YB886 / BG214;
RX   PubMed=15186413; DOI=10.1111/j.1365-2958.2004.04102.x;
RA   Kidane D., Sanchez H., Alonso J.C., Graumann P.L.;
RT   "Visualization of DNA double-strand break repair in live bacteria reveals
RT   dynamic recruitment of Bacillus subtilis RecF, RecO and RecN proteins to
RT   distinct sites on the nucleoids.";
RL   Mol. Microbiol. 52:1627-1639(2004).
RN   [8]
RP   RECRUITMENT OF RECA.
RC   STRAIN=168 / YB886 / BG214;
RX   PubMed=16061691; DOI=10.1083/jcb.200412090;
RA   Kidane D., Graumann P.L.;
RT   "Dynamic formation of RecA filaments at DNA double strand break repair
RT   centers in live cells.";
RL   J. Cell Biol. 170:357-366(2005).
RN   [9]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=168 / YB886 / BG214;
RX   PubMed=16385024; DOI=10.1128/jb.188.2.353-360.2006;
RA   Sanchez H., Kidane D., Castillo Cozar M., Graumann P.L., Alonso J.C.;
RT   "Recruitment of Bacillus subtilis RecN to DNA double-strand breaks in the
RT   absence of DNA end processing.";
RL   J. Bacteriol. 188:353-360(2006).
CC   -!- FUNCTION: Involved in recombinational repair of damaged DNA. Seems to
CC       be the first protein recruited to repair centers, foci that are the
CC       site of double-strand DNA break(s), followed by RecO and then RecF.
CC   -!- SUBUNIT: Forms multimers, possibly octamers; these become larger
CC       following DNA damage. Recruited to foci following DNA damage; probably
CC       interacts with RecF and RecO.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000269|PubMed:15186413,
CC       ECO:0000269|PubMed:16385024}. Note=Cytoplasmically located in untreated
CC       cells. Recruited to foci following treatment with DNA damaging agents;
CC       these foci are presumably the breaks themselves. They are almost always
CC       located within nucleoids.
CC   -!- SIMILARITY: Belongs to the RecN family. {ECO:0000305}.
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DR   EMBL; M30297; AAA22691.1; -; Genomic_DNA.
DR   EMBL; D84432; BAA12579.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14355.2; -; Genomic_DNA.
DR   EMBL; M27869; AAA22209.1; -; Genomic_DNA.
DR   EMBL; U68235; AAC44870.1; -; Genomic_DNA.
DR   PIR; B35128; B35128.
DR   RefSeq; NP_390304.2; NC_000964.3.
DR   RefSeq; WP_003230267.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P17894; -.
DR   SMR; P17894; -.
DR   STRING; 224308.BSU24240; -.
DR   jPOST; P17894; -.
DR   PaxDb; P17894; -.
DR   PRIDE; P17894; -.
DR   EnsemblBacteria; CAB14355; CAB14355; BSU_24240.
DR   GeneID; 938656; -.
DR   KEGG; bsu:BSU24240; -.
DR   PATRIC; fig|224308.179.peg.2642; -.
DR   eggNOG; COG0497; Bacteria.
DR   InParanoid; P17894; -.
DR   OMA; QVICVTH; -.
DR   PhylomeDB; P17894; -.
DR   BioCyc; BSUB:BSU24240-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0043590; C:bacterial nucleoid; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR   GO; GO:0006302; P:double-strand break repair; IMP:UniProtKB.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR   GO; GO:0009314; P:response to radiation; IBA:GO_Central.
DR   GO; GO:0009432; P:SOS response; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR004604; DNA_recomb/repair_RecN.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038729; Rad50/SbcC_AAA.
DR   PANTHER; PTHR11059; PTHR11059; 1.
DR   Pfam; PF13476; AAA_23; 1.
DR   PIRSF; PIRSF003128; RecN; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   TIGRFAMs; TIGR00634; recN; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; DNA damage; DNA repair; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..576
FT                   /note="DNA repair protein RecN"
FT                   /id="PRO_0000188014"
FT   BINDING         29..36
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        74
FT                   /note="H -> L (in Ref. 5; AAA22209)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        104..111
FT                   /note="SVCRVNGK -> AFAVSMAS (in Ref. 5; AAA22209)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        189
FT                   /note="R -> L (in Ref. 1; AAA22691 and 2; BAA12579)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        546..548
FT                   /note="GRM -> ERS (in Ref. 1; AAA22691, 2; BAA12579 and 6;
FT                   AAC44870)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   576 AA;  64508 MW;  235BED4E4A2EB17D CRC64;
     MLAELSIKNF AIIEELTVSF ERGLTVLTGE TGAGKSIIID AISLLVGGRG SSEFVRYGEA
     KAELEGLFLL ESGHPVLGVC AEQGIDVSDE MIVMRRDIST SGKSVCRVNG KLVTIASLRE
     IGRLLLDIHG QHDNQLLMED ENHLQLLDKF AGAEVESALK TYQEGYQRYV KLLKKLKQLS
     ESEQEMAHRL DLIQFQLEEI ESAKLELNED EQLQEERQQI SNFEKIYESL QNAYNALRSE
     QGGLDWVGMA SAQLEDISDI NEPLKKMSES VSNSYYLLED ATFQMRNMLD ELEFDPERLN
     YIETRLNEIK QLKRKYGATV EDILEYASKI EEEIDQIENR DSHLQSLKKE LDSVGKDVAV
     EAANVSQIRK TWAKKLADEI HRELKSLYME KSTFDTEFKV RTASRNEEAP LVNGQPVQLT
     EQGIDLVKFL ISTNTGEPLK SLSKVASGGE LSRVMLAIKS IFSSQQDVTS IIFDEVDTGV
     SGRVAQAIAE KIHKVSIGSQ VLCITHLPQV AAMADTHLYI AKELKDGRTT TRVKPLSKQE
     KVAEIGRMIA GVEVTDLTKR HAKELLKQAD QVKTTG
 
 
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