MCRA_ECOLI
ID MCRA_ECOLI Reviewed; 277 AA.
AC P24200;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Type IV methyl-directed restriction enzyme EcoKMcrA {ECO:0000303|PubMed:12654995};
DE Short=EcoKMcrA {ECO:0000303|PubMed:12654995};
DE EC=3.1.21.-;
DE AltName: Full=5-methylcytosine-specific restriction enzyme A;
GN Name=mcrA {ECO:0000303|PubMed:1938927}; Synonyms=rglA;
GN OrderedLocusNames=b1159, JW1145;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1938927; DOI=10.1128/jb.173.22.7368-7373.1991;
RA Hiom K.J., Sedgwick S.G.;
RT "Cloning and structural characterization of the mcrA locus of Escherichia
RT coli.";
RL J. Bacteriol. 173:7368-7373(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX DOI=10.1007/BF02703150;
RA Ramalingam R., Prasad R., Shivapriya R., Dharmalingam K.;
RT "Molecular cloning and sequencing of mcrA locus and identification of McrA
RT protein in Escherichia coli.";
RL J. Biosci. 17:217-232(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [4]
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 [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 NOMENCLATURE.
RX PubMed=12654995; DOI=10.1093/nar/gkg274;
RA Roberts R.J., Belfort M., Bestor T., Bhagwat A.S., Bickle T.A.,
RA Bitinaite J., Blumenthal R.M., Degtyarev S.K., Dryden D.T., Dybvig K.,
RA Firman K., Gromova E.S., Gumport R.I., Halford S.E., Hattman S.,
RA Heitman J., Hornby D.P., Janulaitis A., Jeltsch A., Josephsen J., Kiss A.,
RA Klaenhammer T.R., Kobayashi I., Kong H., Krueger D.H., Lacks S.,
RA Marinus M.G., Miyahara M., Morgan R.D., Murray N.E., Nagaraja V.,
RA Piekarowicz A., Pingoud A., Raleigh E., Rao D.N., Reich N., Repin V.E.,
RA Selker E.U., Shaw P.C., Stein D.C., Stoddard B.L., Szybalski W.,
RA Trautner T.A., Van Etten J.L., Vitor J.M., Wilson G.G., Xu S.Y.;
RT "A nomenclature for restriction enzymes, DNA methyltransferases, homing
RT endonucleases and their genes.";
RL Nucleic Acids Res. 31:1805-1812(2003).
CC -!- FUNCTION: Restriction of 5-methyl and 5-hydroxymethylcytosines at the
CC specific DNA sequence 5'-C(me)CGG-3'.
CC -!- MISCELLANEOUS: Encoded by the SOS-inducible cryptic lambdoid prophage
CC e14 (PubMed:1938927, Ref.2, PubMed:9278503, PubMed:16738553). UV
CC treatment leads to prophage excision and reduced levels of McrA
CC (PubMed:1938927, Ref.2). {ECO:0000269|PubMed:16738553,
CC ECO:0000269|PubMed:1938927, ECO:0000269|PubMed:9278503,
CC ECO:0000269|Ref.2}.
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; M76667; AAA68481.1; -; Genomic_DNA.
DR EMBL; Z19104; CAA79520.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74243.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35995.1; -; Genomic_DNA.
DR PIR; A41424; A41424.
DR RefSeq; NP_415677.1; NC_000913.3.
DR RefSeq; WP_000557907.1; NZ_CP047127.1.
DR PDB; 6GHC; X-ray; 2.85 A; A/B=1-277.
DR PDB; 6R64; X-ray; 2.64 A; A/B=1-143.
DR PDB; 6T21; X-ray; 2.07 A; A/B=1-143.
DR PDB; 6T22; X-ray; 2.21 A; A/B=1-143.
DR PDBsum; 6GHC; -.
DR PDBsum; 6R64; -.
DR PDBsum; 6T21; -.
DR PDBsum; 6T22; -.
DR AlphaFoldDB; P24200; -.
DR SASBDB; P24200; -.
DR SMR; P24200; -.
DR BioGRID; 4262863; 146.
DR IntAct; P24200; 3.
DR STRING; 511145.b1159; -.
DR REBASE; 13372; EcoW3110McrAP.
DR REBASE; 155511; VscVS05ORF515P.
DR REBASE; 2832; EcoKMcrA.
DR PaxDb; P24200; -.
DR PRIDE; P24200; -.
DR EnsemblBacteria; AAC74243; AAC74243; b1159.
DR EnsemblBacteria; BAA35995; BAA35995; BAA35995.
DR GeneID; 66675027; -.
DR GeneID; 945727; -.
DR KEGG; ecj:JW1145; -.
DR KEGG; eco:b1159; -.
DR PATRIC; fig|511145.12.peg.1200; -.
DR EchoBASE; EB0568; -.
DR eggNOG; COG1403; Bacteria.
DR HOGENOM; CLU_1003791_0_0_6; -.
DR BioCyc; EcoCyc:EG10573-MON; -.
DR BioCyc; MetaCyc:EG10573-MON; -.
DR PRO; PR:P24200; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0008327; F:methyl-CpG binding; IDA:EcoliWiki.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR CDD; cd00085; HNHc; 1.
DR InterPro; IPR002711; HNH.
DR InterPro; IPR003615; HNH_nuc.
DR Pfam; PF01844; HNH; 1.
DR SMART; SM00507; HNHc; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endonuclease; Hydrolase; Nuclease; Reference proteome;
KW Restriction system.
FT CHAIN 1..277
FT /note="Type IV methyl-directed restriction enzyme EcoKMcrA"
FT /id="PRO_0000077380"
FT DOMAIN 207..257
FT /note="HNH"
FT STRAND 1..4
FT /evidence="ECO:0007829|PDB:6T21"
FT STRAND 10..20
FT /evidence="ECO:0007829|PDB:6T21"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:6T21"
FT TURN 34..39
FT /evidence="ECO:0007829|PDB:6T21"
FT HELIX 40..53
FT /evidence="ECO:0007829|PDB:6T21"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:6T21"
FT HELIX 66..71
FT /evidence="ECO:0007829|PDB:6T21"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:6T21"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:6T21"
FT HELIX 93..102
FT /evidence="ECO:0007829|PDB:6T21"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:6T21"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:6T21"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:6T21"
FT HELIX 134..142
FT /evidence="ECO:0007829|PDB:6T21"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:6GHC"
FT HELIX 155..167
FT /evidence="ECO:0007829|PDB:6GHC"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:6GHC"
FT STRAND 181..189
FT /evidence="ECO:0007829|PDB:6GHC"
FT HELIX 193..203
FT /evidence="ECO:0007829|PDB:6GHC"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:6GHC"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:6GHC"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:6GHC"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:6GHC"
FT TURN 233..236
FT /evidence="ECO:0007829|PDB:6GHC"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:6GHC"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:6GHC"
FT HELIX 249..257
FT /evidence="ECO:0007829|PDB:6GHC"
FT HELIX 261..271
FT /evidence="ECO:0007829|PDB:6GHC"
SQ SEQUENCE 277 AA; 31390 MW; E5F2627DFFDEC402 CRC64;
MHVFDNNGIE LKAECSIGEE DGVYGLILES WGPGDRNKDY NIALDYIIER LVDSGVSQVV
VYLASSSVRK HMHSLDERKI HPGEYFTLIG NSPRDIRLKM CGYQAYFSRT GRKEIPSGNR
TKRILINVPG IYSDSFWASI IRGELSELSQ PTDDESLLNM RVSKLIKKTL SQPEGSRKPV
EVERLQKVYV RDPMVKAWIL QQSKGICENC GKNAPFYLND GNPYLEVHHV IPLSSGGADT
TDNCVALCPN CHRELHYSKN AKELIEMLYV NINRLQK