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MCRC_ECOLI
ID   MCRC_ECOLI              Reviewed;         348 AA.
AC   P15006; Q2M5X1;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 3.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Type IV methyl-directed restriction enzyme EcoKMcrBC {ECO:0000303|PubMed:12654995};
DE            Short=EcoKMcrBC {ECO:0000303|PubMed:12654995};
DE   AltName: Full=Protein McrC;
GN   Name=mcrC; OrderedLocusNames=b4345, JW5789;
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=2203735; DOI=10.1128/jb.172.9.4888-4900.1990;
RA   Dila D., Sutherland E., Moran L., Slatko B., Raleigh E.A.;
RT   "Genetic and sequence organization of the mcrBC locus of Escherichia coli
RT   K-12.";
RL   J. Bacteriol. 172:4888-4900(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=2649480; DOI=10.1128/jb.171.4.1974-1981.1989;
RA   Ross T.K., Achberger E.C., Braymer H.D.;
RT   "Nucleotide sequence of the McrB region of Escherichia coli K-12 and
RT   evidence for two independent translational initiation sites at the mcrB
RT   locus.";
RL   J. Bacteriol. 171:1974-1981(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA   Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT   "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT   from 92.8 through 100 minutes.";
RL   Nucleic Acids Res. 23:2105-2119(1995).
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   PROTEIN SEQUENCE OF 1-10.
RC   STRAIN=K12;
RX   PubMed=2050643; DOI=10.1128/jb.173.12.3918-3920.1991;
RA   Zheng L., Braymer H.D.;
RT   "Overproduction and purification of McrC protein from Escherichia coli K-
RT   12.";
RL   J. Bacteriol. 173:3918-3920(1991).
RN   [7]
RP   ERRATUM OF PUBMED:2050643.
RA   Zheng L., Braymer H.D.;
RL   J. Bacteriol. 173:5933-5933(1991).
RN   [8]
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: Modifies the specificity of McrB restriction by expanding the
CC       range of modified sequences restricted. Does not bind to DNA.
CC   -!- INTERACTION:
CC       P15006; P15005: mcrB; NbExp=2; IntAct=EBI-25407271, EBI-552513;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA24146.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M58752; AAA24146.1; ALT_INIT; Genomic_DNA.
DR   EMBL; M24927; AAA24144.1; -; Genomic_DNA.
DR   EMBL; U14003; AAA97242.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC77301.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE78335.1; -; Genomic_DNA.
DR   PIR; JS0121; BVECMB.
DR   RefSeq; NP_418765.1; NC_000913.3.
DR   RefSeq; WP_000437621.1; NZ_LN832404.1.
DR   PDB; 6HZ4; EM; 3.60 A; M/N=1-348.
DR   PDB; 6HZ5; EM; 4.20 A; M/N=1-348.
DR   PDB; 6HZ6; EM; 4.30 A; M/N=1-348.
DR   PDB; 6HZ7; EM; 4.30 A; M/N=1-348.
DR   PDB; 6HZ8; EM; 4.30 A; M/N=1-348.
DR   PDB; 6HZ9; EM; 4.80 A; M/N=1-348.
DR   PDB; 6UT6; EM; 3.28 A; G=1-348.
DR   PDBsum; 6HZ4; -.
DR   PDBsum; 6HZ5; -.
DR   PDBsum; 6HZ6; -.
DR   PDBsum; 6HZ7; -.
DR   PDBsum; 6HZ8; -.
DR   PDBsum; 6HZ9; -.
DR   PDBsum; 6UT6; -.
DR   AlphaFoldDB; P15006; -.
DR   SMR; P15006; -.
DR   BioGRID; 4262764; 181.
DR   ComplexPortal; CPX-5285; McrBC 5-methylcytosine-specific restriction endonuclease complex.
DR   IntAct; P15006; 1.
DR   STRING; 511145.b4345; -.
DR   REBASE; 13377; EcoW3110McrBCP.
DR   REBASE; 2865; EcoKMcrBC.
DR   REBASE; 441251; EcoBL21FMcrBCP.
DR   PaxDb; P15006; -.
DR   PRIDE; P15006; -.
DR   EnsemblBacteria; AAC77301; AAC77301; b4345.
DR   EnsemblBacteria; BAE78335; BAE78335; BAE78335.
DR   GeneID; 948880; -.
DR   KEGG; ecj:JW5789; -.
DR   KEGG; eco:b4345; -.
DR   PATRIC; fig|1411691.4.peg.2341; -.
DR   EchoBASE; EB0570; -.
DR   eggNOG; COG4268; Bacteria.
DR   HOGENOM; CLU_065564_0_0_6; -.
DR   InParanoid; P15006; -.
DR   OMA; IPIRNLW; -.
DR   BioCyc; EcoCyc:EG10575-MON; -.
DR   BioCyc; MetaCyc:EG10575-MON; -.
DR   PRO; PR:P15006; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:1905348; C:endonuclease complex; IPI:ComplexPortal.
DR   GO; GO:0032067; F:type IV site-specific deoxyribonuclease activity; IDA:EcoCyc.
DR   GO; GO:0009307; P:DNA restriction-modification system; IC:ComplexPortal.
DR   InterPro; IPR019292; McrC.
DR   InterPro; IPR014407; McrC_bac.
DR   PANTHER; PTHR38733; PTHR38733; 1.
DR   Pfam; PF10117; McrBC; 1.
DR   PIRSF; PIRSF003109; McrC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Reference proteome;
KW   Restriction system.
FT   CHAIN           1..348
FT                   /note="Type IV methyl-directed restriction enzyme
FT                   EcoKMcrBC"
FT                   /id="PRO_0000077381"
FT   HELIX           8..18
FT                   /evidence="ECO:0007829|PDB:6UT6"
FT   HELIX           29..32
FT                   /evidence="ECO:0007829|PDB:6UT6"
FT   HELIX           38..53
FT                   /evidence="ECO:0007829|PDB:6UT6"
FT   TURN            54..56
FT                   /evidence="ECO:0007829|PDB:6UT6"
FT   STRAND          61..71
FT                   /evidence="ECO:0007829|PDB:6UT6"
FT   STRAND          74..76
FT                   /evidence="ECO:0007829|PDB:6UT6"
FT   HELIX           80..83
FT                   /evidence="ECO:0007829|PDB:6UT6"
FT   TURN            84..88
FT                   /evidence="ECO:0007829|PDB:6UT6"
FT   STRAND          92..101
FT                   /evidence="ECO:0007829|PDB:6UT6"
FT   HELIX           104..117
FT                   /evidence="ECO:0007829|PDB:6UT6"
FT   STRAND          118..122
FT                   /evidence="ECO:0007829|PDB:6UT6"
FT   HELIX           124..135
FT                   /evidence="ECO:0007829|PDB:6UT6"
FT   HELIX           147..150
FT                   /evidence="ECO:0007829|PDB:6UT6"
FT   TURN            151..153
FT                   /evidence="ECO:0007829|PDB:6UT6"
FT   STRAND          154..157
FT                   /evidence="ECO:0007829|PDB:6UT6"
FT   HELIX           162..174
FT                   /evidence="ECO:0007829|PDB:6UT6"
FT   STRAND          175..177
FT                   /evidence="ECO:0007829|PDB:6UT6"
FT   STRAND          185..187
FT                   /evidence="ECO:0007829|PDB:6UT6"
FT   HELIX           194..204
FT                   /evidence="ECO:0007829|PDB:6UT6"
FT   HELIX           206..210
FT                   /evidence="ECO:0007829|PDB:6UT6"
FT   TURN            211..213
FT                   /evidence="ECO:0007829|PDB:6UT6"
FT   STRAND          244..249
FT                   /evidence="ECO:0007829|PDB:6UT6"
FT   STRAND          252..258
FT                   /evidence="ECO:0007829|PDB:6UT6"
FT   HELIX           263..266
FT                   /evidence="ECO:0007829|PDB:6UT6"
FT   HELIX           279..288
FT                   /evidence="ECO:0007829|PDB:6UT6"
FT   STRAND          297..302
FT                   /evidence="ECO:0007829|PDB:6UT6"
FT   STRAND          306..308
FT                   /evidence="ECO:0007829|PDB:6UT6"
FT   STRAND          312..315
FT                   /evidence="ECO:0007829|PDB:6UT6"
FT   STRAND          317..319
FT                   /evidence="ECO:0007829|PDB:6UT6"
FT   STRAND          321..324
FT                   /evidence="ECO:0007829|PDB:6UT6"
FT   HELIX           332..344
FT                   /evidence="ECO:0007829|PDB:6UT6"
SQ   SEQUENCE   348 AA;  40590 MW;  9B65FAD20E5C6E64 CRC64;
     MEQPVIPVRN IYYMLTYAWG YLQEIKQANL EAIPGNNLLD ILGYVLNKGV LQLSRRGLEL
     DYNPNTEIIP GIKGRIEFAK TIRGFHLNHG KTVSTFDMLN EDTLANRIIK STLAILIKHE
     KLNSTIRDEA RSLYRKLPGI STLHLTPQHF SYLNGGKNTR YYKFVISVCK FIVNNSIPGQ
     NKGHYRFYDF ERNEKEMSLL YQKFLYEFCR RELTSANTTR SYLKWDASSI SDQSLNLLPR
     METDITIRSS EKILIVDAKY YKSIFSRRMG TEKFHSQNLY QLMNYLWSLK PENGENIGGL
     LIYPHVDTAV KHRYKINGFD IGLCTVNLGQ EWPCIHQELL DIFDEYLK
 
 
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