ID   MTPS_PROST              Reviewed;         507 AA.
AC   P00474;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Type II methyltransferase M.PstI {ECO:0000303|PubMed:12654995};
DE            Short=M.PstI {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.72;
DE   AltName: Full=Adenine-specific methyltransferase PstI;
DE   AltName: Full=Modification methylase PstI;
GN   Name=pstIM;
OS   Providencia stuartii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Providencia.
OX   NCBI_TaxID=588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS, AND
RP   FUNCTION.
RC   STRAIN=164;
RX   PubMed=6330092; DOI=10.1016/s0021-9258(17)42896-1;
RA   Walder R.Y., Walder J.A., Donelson J.E.;
RT   "The organization and complete nucleotide sequence of the PstI restriction-
RT   modification system.";
RL   J. Biol. Chem. 259:8015-8026(1984).
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: A gamma subtype methylase that recognizes the double-stranded
CC       sequence 5'-CTGCAG-3', methylates A-5 on both strands, and protects the
CC       DNA from cleavage by the PstI endonuclease.
CC       {ECO:0000269|PubMed:6330092, 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   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; K02081; AAA25672.1; -; Genomic_DNA.
DR   PIR; A00553; XYOFS.
DR   AlphaFoldDB; P00474; -.
DR   PRO; PR:P00474; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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; 3.40.50.150; -; 1.
DR   InterPro; IPR011639; RM_methylase_Eco57I-like.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF07669; Eco57I; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; DNA-binding; Methyltransferase;
KW   Restriction system; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..507
FT                   /note="Type II methyltransferase M.PstI"
FT                   /id="PRO_0000087978"
SQ   SEQUENCE   507 AA;  56877 MW;  AF5DA9341741823D CRC64;
     MTEAATQLPI SLNILVDSIR EAANSTLDET LRSKLGQFMS SSAVSELMAN LFESYVGEHE
     ILDAGAGVGS LTAAFVQNAT LNGAKSISST CYEISEVMVY NLIQVLDLCK IRAMEFEVNW
     QQKIIESDFI QASVEQLLIE NYSPKYNKAI LNPPYLKIAA KGRERALLQK VGIEASNLYS
     AFVALAIKQL KSGGELVAIT PRSFCNGPYF NDFRKQMLDE CSLNKIHVFN SRKSAFKADN
     VLQENIIYHL TKGETQRKVV TVYSSTCAND INPTIFEVPF DEIVKSNNPD LFIHIVTNEQ
     ERELANKAGG LPCSLSDLGI QVSTGKVVDF RTRENLSMEY ISNSVPLIFP QHLQRCSIVW
     PITKAKKPNA LIVNEATNNL MVPNGIYVLT RRLTAKEEKR RIVASIYYPD IANVDTVGFD
     NKINYFHANG KPLDISLAKG LWVFLNSTLI DKYFRQMNGH TQVNATDLRA LRYPTREQLE
     DIANQVDFGE FEQTKIDEII NQSLQLM