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   13-SEP-2023, entry version 88.
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; Pseudomonadota; 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   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 1.20.1260.30; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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   NCBIfam; TIGR00497; hsdM; 1.
DR   PANTHER; PTHR42933:SF1; SITE-SPECIFIC DNA-METHYLTRANSFERASE (ADENINE-SPECIFIC); 1.
DR   PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR   Pfam; PF12161; HsdM_N; 1.
DR   Pfam; PF02384; N6_Mtase; 1.
DR   PRINTS; PR00507; N12N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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
//