T1MP_ECOLX
ID T1MP_ECOLX Reviewed; 520 AA.
AC Q47163;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Type I restriction enzyme EcoprrI methylase subunit {ECO:0000305};
DE Short=M protein;
DE EC=2.1.1.72 {ECO:0000250|UniProtKB:P08957};
DE AltName: Full=Type I methyltransferase M.EcoprrI {ECO:0000303|PubMed:12654995};
DE Short=M.EcoprrI {ECO:0000303|PubMed:12654995};
GN Name=hsdM {ECO:0000303|PubMed:8145241};
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CTR5X;
RX PubMed=8145241; DOI=10.1006/jmbi.1994.1230;
RA Tyndall C., Meister J., Bickle T.A.;
RT "The Escherichia coli prr region encodes a functional type IC DNA
RT restriction system closely integrated with an anticodon nuclease gene.";
RL J. Mol. Biol. 237:266-274(1994).
RN [2]
RP NOMENCLATURE, AND SUBTYPE.
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: The subtype gamma methyltransferase (M) subunit of a type I
CC restriction enzyme. The M and S subunits together form a
CC methyltransferase (MTase) that methylates two adenine residues of the
CC sequence 5'-CCAN(7)ATGC-3'. In the presence of the R subunit the
CC complex can also act as an endonuclease, binding to the same target
CC sequence but cutting the DNA some distance from this site. Whether the
CC DNA is cut or modified depends on the methylation state of the target
CC sequence. When the target site is unmodified, the DNA is cut. When the
CC target site is hemimethylated, the complex acts as a maintenance MTase
CC modifying the DNA so that both strands become methylated. After
CC locating a non-methylated recognition site, the enzyme complex serves
CC as a molecular motor that translocates DNA in an ATP-dependent manner
CC until a collision occurs that triggers cleavage.
CC {ECO:0000250|UniProtKB:P08957, ECO:0000303|PubMed:12654995}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an
CC N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:15197, Rhea:RHEA-COMP:12418, Rhea:RHEA-
CC COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:90615, ChEBI:CHEBI:90616; EC=2.1.1.72;
CC Evidence={ECO:0000250|UniProtKB:P08957};
CC -!- SUBUNIT: The type I restriction/modification system is composed of
CC three polypeptides R, M and S; the restriction enzyme has stoichiometry
CC R(2)M(2)S(1) while the methyltransferase is M(2)S(1).
CC {ECO:0000250|UniProtKB:P08957}.
CC -!- MISCELLANEOUS: Type I restriction and modification enzymes are complex,
CC multifunctional systems which require ATP, S-adenosyl methionine and
CC Mg(2+) as cofactors and, in addition to their endonucleolytic and
CC methylase activities, are potent DNA-dependent ATPases.
CC {ECO:0000250|UniProtKB:P08957}.
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; X75452; CAA53205.1; -; Genomic_DNA.
DR AlphaFoldDB; Q47163; -.
DR SMR; Q47163; -.
DR REBASE; 3552; M.EcoprrI.
DR PRO; PR:Q47163; -.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1260.30; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR022749; D12N6_MeTrfase_N.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR004546; Restrct_endonuc_T1M.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038333; T1MK-like_N_sf.
DR Pfam; PF12161; HsdM_N; 1.
DR Pfam; PF02384; N6_Mtase; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00497; hsdM; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW DNA-binding; Methyltransferase; Restriction system;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..520
FT /note="Type I restriction enzyme EcoprrI methylase subunit"
FT /id="PRO_0000088024"
FT BINDING 198..203
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q89Z59"
FT BINDING 230..232
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q89Z59"
FT BINDING 254
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q89Z59"
SQ SEQUENCE 520 AA; 58015 MW; 79401EC1720EB257 CRC64;
MKMTSIQQRA ELHRQIWQIA NDVRGSVDGW DFKQYVLGAL FYRFISENFS SYIEAGDDSI
CYAKLDDSVI TDDIKDDAIK TKGYFIYPSQ LFCNVAAKAN TNDRLNADLN SIFVAIESSA
YGYPSEADIK GLFADFDTTS NRLGNTVKDK NARLAAVLKG VEGLKLGDFN EHQIDLFGDA
YEFLISNYAA NAGKSGGEFF TPQHVSKLIA QLAMHGQTHV NKIYDPAAGS GSLLLQAKKQ
FDDHIIEEGF FGQEINHTTY NLARMNMFLH NINYDKFDIK LGNTLTEPHF RDEKPFDAIV
SNPPYSVKWI GSDDPTLIND ERFAPAGVLA PKSKADFAFV LHALNYLSAK GRAAIVCFPG
IFYRGGAEQK IRQYLVDNNY VETVISLAPN LFFGTTIAVN ILVLSKHKTD TKVQFIDASE
LFKKETNNNI LTDAHIEQIM QVFASKEDVA HLAKSVAFET VVANDYNLSV SSYVEAKDTR
EIIDIAELNA ELKTTVSKID QLRKDIDAIV AEIEGCEVQK
