MCRB_ECOLI
ID MCRB_ECOLI Reviewed; 459 AA.
AC P15005; Q2M5X0;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 3.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Type IV methyl-directed restriction enzyme EcoKMcrB subunit {ECO:0000303|PubMed:12654995};
DE Short=EcoKMcrBC {ECO:0000303|PubMed:1312983};
DE AltName: Full=5-methylcytosine-specific restriction enzyme B;
DE EC=3.1.21.-;
GN Name=mcrB; Synonyms=rglB; OrderedLocusNames=b4346, JW5871;
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], ISOFORMS 33 KDA AND 51 KDA, FUNCTION,
RP AND DISRUPTION PHENOTYPE.
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 AND 163-175, AND ISOFORMS 33 KDA AND 51 KDA.
RC STRAIN=K12;
RX PubMed=1312983; DOI=10.1016/0378-1119(92)90308-c;
RA Zheng L., Wang X., Braymer H.D.;
RT "Purification and N-terminal amino acid sequences of two polypeptides
RT encoded by the mcrB gene from Escherichia coli K-12.";
RL Gene 112:97-100(1992).
RN [7]
RP CHARACTERIZATION.
RX PubMed=7781618; DOI=10.1002/j.1460-2075.1995.tb07264.x;
RA Krueger T., Wild C., Noyer-Weidner M.;
RT "McrB: a prokaryotic protein specifically recognizing DNA containing
RT modified cytosine residues.";
RL EMBO J. 14:2661-2669(1995).
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: Recognizes N4- and C5-methylcytosine (and 5-hydroxy-
CC methylcytosines) produced by a broad range of DNA methylases and
CC appears to act against 5-methylcytosine preceded by a purine residue.
CC Binds to DNA containing methylated cytosines; also binds to GTP.
CC Isoform 33 kDa is less active than isoform 51 kDa and may play a role
CC in regulating the activity of isoform 51 kDa by competing with it in
CC DNA and protein binding abilities. {ECO:0000305|PubMed:2649480}.
CC -!- INTERACTION:
CC P15005; P15005: mcrB; NbExp=2; IntAct=EBI-552513, EBI-552513;
CC P15005; P15006: mcrC; NbExp=2; IntAct=EBI-552513, EBI-25407271;
CC P15005; P31806: nnr; NbExp=3; IntAct=EBI-552513, EBI-554188;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Comment=Both isoforms are expressed at the same level. A frameshift
CC mutation within the codon for residue 58 prevents formation of the 51
CC kDa but not 33 kDa isoform. {ECO:0000269|PubMed:2649480};
CC Name=51 kDa {ECO:0000269|PubMed:1312983};
CC IsoId=P15005-1; Sequence=Displayed;
CC Name=33 kDa {ECO:0000269|PubMed:1312983};
CC IsoId=P15005-2; Sequence=VSP_018868;
CC -!- DISRUPTION PHENOTYPE: 7.2-fold drop in transformation efficiency with
CC M.AluI-methylated DNA. {ECO:0000269|PubMed:2649480}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA24145.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA97243.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M58752; AAA24145.1; ALT_INIT; Genomic_DNA.
DR EMBL; M24927; AAA24142.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97243.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC77302.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE78336.1; -; Genomic_DNA.
DR PIR; A36708; XYECMB.
DR RefSeq; NP_418766.4; NC_000913.3.
DR RefSeq; WP_000443951.1; NZ_LN832404.1.
DR PDB; 3SSC; X-ray; 2.10 A; A/B=1-161.
DR PDB; 3SSD; X-ray; 2.20 A; A/B=1-161.
DR PDB; 3SSE; X-ray; 2.70 A; A/B=1-161.
DR PDB; 6GCD; X-ray; 1.80 A; A/B=1-161.
DR PDB; 6GCE; X-ray; 1.60 A; A/B=1-161.
DR PDB; 6GCF; X-ray; 1.55 A; A/B=1-161.
DR PDB; 6HZ4; EM; 3.60 A; A/B/C/D/E/F=162-459.
DR PDB; 6HZ5; EM; 4.20 A; A/B/C/D/E/F/G/H/I/J/K/L=162-459.
DR PDB; 6HZ6; EM; 4.30 A; A/B/C/D/E/F/G/H/I/J/K/L=162-459.
DR PDB; 6HZ7; EM; 4.30 A; A/B/C/D/E/F/G/H/I/J/K/L=162-459.
DR PDB; 6HZ8; EM; 4.30 A; A/B/C/D/E/F/G/H/I/J/K/L=162-459.
DR PDB; 6HZ9; EM; 4.80 A; A/B/C/D/E/F/G/H/I/J/K/L=162-459.
DR PDB; 6UT6; EM; 3.28 A; A/B/C/D/E/F=1-459.
DR PDBsum; 3SSC; -.
DR PDBsum; 3SSD; -.
DR PDBsum; 3SSE; -.
DR PDBsum; 6GCD; -.
DR PDBsum; 6GCE; -.
DR PDBsum; 6GCF; -.
DR PDBsum; 6HZ4; -.
DR PDBsum; 6HZ5; -.
DR PDBsum; 6HZ6; -.
DR PDBsum; 6HZ7; -.
DR PDBsum; 6HZ8; -.
DR PDBsum; 6HZ9; -.
DR PDBsum; 6UT6; -.
DR AlphaFoldDB; P15005; -.
DR SMR; P15005; -.
DR BioGRID; 4262765; 164.
DR BioGRID; 853362; 2.
DR ComplexPortal; CPX-5285; McrBC 5-methylcytosine-specific restriction endonuclease complex.
DR DIP; DIP-10168N; -.
DR IntAct; P15005; 4.
DR STRING; 511145.b4346; -.
DR REBASE; 13377; EcoW3110McrBCP.
DR REBASE; 154028; Ssp60837McrBCP.
DR REBASE; 203811; Keu1446McrBCP.
DR REBASE; 2865; EcoKMcrBC.
DR REBASE; 352138; LxyHY24McrBCP.
DR REBASE; 441251; EcoBL21FMcrBCP.
DR jPOST; P15005; -.
DR PaxDb; P15005; -.
DR PRIDE; P15005; -.
DR EnsemblBacteria; AAC77302; AAC77302; b4346.
DR EnsemblBacteria; BAE78336; BAE78336; BAE78336.
DR GeneID; 949122; -.
DR KEGG; ecj:JW5871; -.
DR KEGG; eco:b4346; -.
DR PATRIC; fig|511145.12.peg.4492; -.
DR EchoBASE; EB0569; -.
DR eggNOG; COG1401; Bacteria.
DR HOGENOM; CLU_587598_0_0_6; -.
DR InParanoid; P15005; -.
DR OMA; VIMQINE; -.
DR PhylomeDB; P15005; -.
DR BioCyc; EcoCyc:EG10574-MON; -.
DR BioCyc; MetaCyc:EG10574-MON; -.
DR PRO; PR:P15005; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1905348; C:endonuclease complex; IPI:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IDA:EcoliWiki.
DR GO; GO:0010385; F:double-stranded methylated DNA binding; IDA:EcoCyc.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IDA:EcoCyc.
DR GO; GO:0003924; F:GTPase activity; IDA:EcoliWiki.
DR GO; GO:0044729; F:hemi-methylated DNA-binding; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0015666; F:restriction endodeoxyribonuclease activity; IDA:EcoliWiki.
DR GO; GO:0006308; P:DNA catabolic process; IDA:EcoliWiki.
DR GO; GO:0009307; P:DNA restriction-modification system; IC:ComplexPortal.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011704; ATPase_dyneun-rel_AAA.
DR InterPro; IPR021961; McrB_DNA-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF07728; AAA_5; 1.
DR Pfam; PF12102; MrcB_N; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Direct protein sequencing;
KW DNA-binding; Endonuclease; GTP-binding; Hydrolase; Nuclease;
KW Nucleotide-binding; Reference proteome; Restriction system.
FT CHAIN 1..459
FT /note="Type IV methyl-directed restriction enzyme EcoKMcrB
FT subunit"
FT /id="PRO_0000030347"
FT BINDING 201..208
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 300..303
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 333..336
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..161
FT /note="Missing (in isoform 33 kDa)"
FT /evidence="ECO:0000305"
FT /id="VSP_018868"
FT CONFLICT 186..212
FT /note="TILKRLTIKKNIILQGPPGVGKTFVAR -> SDTQTINHQKKYYPPGAARRW
FT KNLCCT (in Ref. 2; AAA24142)"
FT /evidence="ECO:0000305"
FT CONFLICT 224..232
FT /note="PQRVNMVQF -> RTKYGSV (in Ref. 2; AAA24142)"
FT /evidence="ECO:0000305"
FT CONFLICT 245..259
FT /note="YRPNGVGFRRKDGIF -> IVRMASASVKTHI (in Ref. 2;
FT AAA24142)"
FT /evidence="ECO:0000305"
FT HELIX 5..17
FT /evidence="ECO:0007829|PDB:6GCF"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:6GCF"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:6GCF"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:6GCF"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:6GCF"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:6GCF"
FT STRAND 61..70
FT /evidence="ECO:0007829|PDB:6GCF"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:6GCF"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:6GCF"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:6GCF"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:6GCF"
FT HELIX 102..110
FT /evidence="ECO:0007829|PDB:6GCF"
FT STRAND 120..127
FT /evidence="ECO:0007829|PDB:6GCF"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:6GCF"
FT HELIX 134..153
FT /evidence="ECO:0007829|PDB:6GCF"
FT HELIX 170..174
FT /evidence="ECO:0007829|PDB:6UT6"
FT HELIX 181..193
FT /evidence="ECO:0007829|PDB:6UT6"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:6UT6"
FT HELIX 207..219
FT /evidence="ECO:0007829|PDB:6UT6"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:6UT6"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:6UT6"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:6UT6"
FT HELIX 238..241
FT /evidence="ECO:0007829|PDB:6UT6"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:6UT6"
FT STRAND 251..256
FT /evidence="ECO:0007829|PDB:6UT6"
FT HELIX 258..267
FT /evidence="ECO:0007829|PDB:6UT6"
FT STRAND 274..280
FT /evidence="ECO:0007829|PDB:6UT6"
FT HELIX 286..290
FT /evidence="ECO:0007829|PDB:6UT6"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:6UT6"
FT TURN 294..297
FT /evidence="ECO:0007829|PDB:6UT6"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:6UT6"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:6UT6"
FT STRAND 326..333
FT /evidence="ECO:0007829|PDB:6UT6"
FT HELIX 344..349
FT /evidence="ECO:0007829|PDB:6UT6"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:6UT6"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:6UT6"
FT HELIX 362..369
FT /evidence="ECO:0007829|PDB:6UT6"
FT TURN 370..372
FT /evidence="ECO:0007829|PDB:6UT6"
FT HELIX 375..392
FT /evidence="ECO:0007829|PDB:6UT6"
FT TURN 393..395
FT /evidence="ECO:0007829|PDB:6UT6"
FT STRAND 397..399
FT /evidence="ECO:0007829|PDB:6UT6"
FT HELIX 409..411
FT /evidence="ECO:0007829|PDB:6UT6"
FT HELIX 414..416
FT /evidence="ECO:0007829|PDB:6UT6"
FT HELIX 422..431
FT /evidence="ECO:0007829|PDB:6UT6"
FT HELIX 433..440
FT /evidence="ECO:0007829|PDB:6UT6"
FT HELIX 445..453
FT /evidence="ECO:0007829|PDB:6UT6"
FT INIT_MET P15005-2:1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1312983"
SQ SEQUENCE 459 AA; 53157 MW; C8167978B0D720CA CRC64;
MESIQPWIEK FIKQAQQQRS QSTKDYPTSY RNLRVKLSFG YGNFTSIPWF AFLGEGQEAS
NGIYPVILYY KDFDELVLAY GISDTNEPHA QWQFSSDIPK TIAEYFQATS GVYPKKYGQS
YYACSQKVSQ GIDYTRFASM LDNIINDYKL IFNSGKSVIP PMSKTESYCL EDALNDLFIP
ETTIETILKR LTIKKNIILQ GPPGVGKTFV ARRLAYLLTG EKAPQRVNMV QFHQSYSYED
FIQGYRPNGV GFRRKDGIFY NFCQQAKEQP EKKYIFIIDE INRANLSKVF GEVMMLMEHD
KRGENWSVPL TYSENDEERF YVPENVYIIG LMNTADRSLA VVDYALRRRF SFIDIEPGFD
TPQFRNFLLN KKAEPSFVES LCQKMNELNQ EISKEATILG KGFRIGHSYF CCGLEDGTSP
DTQWLNEIVM TDIAPLLEEY FFDDPYKQQK WTNKLLGDS
