RECN_ECOLI
ID RECN_ECOLI Reviewed; 553 AA.
AC P05824; P76602;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=DNA repair protein RecN;
DE AltName: Full=Recombination protein N;
GN Name=recN; Synonyms=radB; OrderedLocusNames=b2616, JW5416;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3037486; DOI=10.1093/nar/15.13.5041;
RA Rostas K., Morton S.J., Picksley S.M., Lloyd R.G.;
RT "Nucleotide sequence and LexA regulation of the Escherichia coli recN
RT gene.";
RL Nucleic Acids Res. 15:5041-5049(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP SEQUENCE REVISION TO 426.
RX PubMed=16397293; DOI=10.1093/nar/gkj405;
RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA Thomson N.R., Wishart D., Wanner B.L.;
RT "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT -- 2005.";
RL Nucleic Acids Res. 34:1-9(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP INDUCTION BY HYDROXYUREA.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=20005847; DOI=10.1016/j.molcel.2009.11.024;
RA Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J.,
RA Walker G.C.;
RT "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia
RT coli.";
RL Mol. Cell 36:845-860(2009).
RN [7]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12;
RX PubMed=21219465; DOI=10.1111/j.1365-2958.2010.07465.x;
RA Babu M., Beloglazova N., Flick R., Graham C., Skarina T., Nocek B.,
RA Gagarinova A., Pogoutse O., Brown G., Binkowski A., Phanse S.,
RA Joachimiak A., Koonin E.V., Savchenko A., Emili A., Greenblatt J.,
RA Edwards A.M., Yakunin A.F.;
RT "A dual function of the CRISPR-Cas system in bacterial antivirus immunity
RT and DNA repair.";
RL Mol. Microbiol. 79:484-502(2011).
CC -!- FUNCTION: May be involved in recombinational repair of damaged DNA.
CC -!- INTERACTION:
CC P05824; P76104: rlhA; NbExp=3; IntAct=EBI-548098, EBI-556974;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21219465}. Note=In
CC 70% of cell localizes to discrete nucleoid foci (probable DNA damage
CC sites) upon treatment with mitomycin C (MMC) for 2 hours.
CC -!- INDUCTION: Induced by hydroxyurea. {ECO:0000269|PubMed:20005847}.
CC -!- SIMILARITY: Belongs to the RecN family. {ECO:0000305}.
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DR EMBL; Y00357; CAA68435.1; -; Genomic_DNA.
DR EMBL; U36840; AAA79786.1; -; Genomic_DNA.
DR EMBL; U00096; AAT48145.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16501.1; -; Genomic_DNA.
DR PIR; C65040; RQECN.
DR RefSeq; WP_000880910.1; NZ_SSTT01000038.1.
DR RefSeq; YP_026172.1; NC_000913.3.
DR AlphaFoldDB; P05824; -.
DR SMR; P05824; -.
DR BioGRID; 4263399; 117.
DR BioGRID; 851440; 1.
DR DIP; DIP-10655N; -.
DR IntAct; P05824; 2.
DR STRING; 511145.b2616; -.
DR ChEMBL; CHEMBL4630870; -.
DR PaxDb; P05824; -.
DR PRIDE; P05824; -.
DR EnsemblBacteria; AAT48145; AAT48145; b2616.
DR EnsemblBacteria; BAA16501; BAA16501; BAA16501.
DR GeneID; 66673496; -.
DR GeneID; 947105; -.
DR KEGG; ecj:JW5416; -.
DR KEGG; eco:b2616; -.
DR PATRIC; fig|1411691.4.peg.4123; -.
DR EchoBASE; EB0824; -.
DR eggNOG; COG0497; Bacteria.
DR HOGENOM; CLU_018297_3_1_6; -.
DR InParanoid; P05824; -.
DR OMA; QVICVTH; -.
DR PhylomeDB; P05824; -.
DR BioCyc; EcoCyc:EG10831-MON; -.
DR PRO; PR:P05824; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0043590; C:bacterial nucleoid; IDA:EcoCyc.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; ISM:EcoCyc.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:EcoCyc.
DR GO; GO:0006302; P:double-strand break repair; IDA:EcoCyc.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0036298; P:recombinational interstrand cross-link repair; IMP:EcoCyc.
DR GO; GO:0000725; P:recombinational repair; IDA:EcoCyc.
DR GO; GO:0010212; P:response to ionizing radiation; IMP:EcoCyc.
DR GO; GO:0009314; P:response to radiation; IMP:EcoCyc.
DR GO; GO:0009411; P:response to UV; IMP:EcoCyc.
DR GO; GO:0010165; P:response to X-ray; IMP:EcoCyc.
DR GO; GO:0009432; P:SOS response; IEP:EcoCyc.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR004604; DNA_recomb/repair_RecN.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR PANTHER; PTHR11059; PTHR11059; 1.
DR Pfam; PF02463; SMC_N; 1.
DR PIRSF; PIRSF003128; RecN; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00634; recN; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; DNA damage; DNA repair; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..553
FT /note="DNA repair protein RecN"
FT /id="PRO_0000188017"
FT BINDING 29..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 59..60
FT /note="AA -> C (in Ref. 1; CAA68435)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="A -> R (in Ref. 1; CAA68435)"
FT /evidence="ECO:0000305"
FT CONFLICT 535..553
FT /note="GGSEVTRNTLANAKELLAA -> VAVKSHVIHWRMRKNCLQRKLFSCFTVRV
FT NSKTP (in Ref. 1; CAA68435)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 553 AA; 61396 MW; 0048034F3515EDDB CRC64;
MLAQLTISNF AIVRELEIDF HSGMTVITGE TGAGKSIAID ALGLCLGGRA EADMVRTGAA
RADLCARFSL KDTPAALRWL EENQLEDGHE CLLRRVISSD GRSRGFINGT AVPLSQLREL
GQLLIQIHGQ HAHQLLTKPE HQKFLLDGYA NETSLLQEMT ARYQLWHQSC RDLAHHQQLS
QERAARAELL QYQLKELNEF NPQPGEFEQI DEEYKRLANS GQLLTTSQNA LALMADGEDA
NLQSQLYTAK QLVSELIGMD SKLSGVLDML EEATIQIAEA SDELRHYCDR LDLDPNRLFE
LEQRISKQIS LARKHHVSPE ALPQYYQSLL EEQQQLDDQA DSQETLALAV TKHHQQALEI
ARALHQQRQQ YAEELAQLIT DSMHALSMPH GQFTIDVKFD EHHLGADGAD RIEFRVTTNP
GQPMQPIAKV ASGGELSRIA LAIQVITARK METPALIFDE VDVGISGPTA AVVGKLLRQL
GESTQVMCVT HLPQVAGCGH QHYFVSKETD GAMTETHMQS LNKKARLQEL ARLLGGSEVT
RNTLANAKEL LAA
