T3MO_SALTY
ID T3MO_SALTY Reviewed; 652 AA.
AC P40814;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Type III restriction-modification enzyme StyLTI Mod subunit;
DE Short=M.StyLTI;
DE EC=2.1.1.72 {ECO:0000269|PubMed:1995420};
DE AltName: Full=StyLTI methyltransferase;
DE AltName: Full=Type III methyltransferase M.StyLTI {ECO:0000303|PubMed:12654995, ECO:0000303|PubMed:1995420};
GN Name=mod {ECO:0000303|PubMed:1846861}; OrderedLocusNames=STM0357;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT7;
RX PubMed=8387444; DOI=10.1016/0378-1119(93)90623-b;
RA Dartois V., de Backer O., Colson C.;
RT "Sequence of the Salmonella typhimurium StyLT1 restriction-modification
RT genes: homologies with EcoP1 and EcoP15 type-III R-M systems and presence
RT of helicase domains.";
RL Gene 127:105-110(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=LT7;
RX PubMed=1995420; DOI=10.1016/0378-1119(91)90015-4;
RA De Backer O., Colson C.;
RT "Identification of the recognition sequence for the M.StyLTI
RT methyltransferase of Salmonella typhimurium LT7: an asymmetric site typical
RT of type-III enzymes.";
RL Gene 97:103-107(1991).
RN [4]
RP FUNCTION.
RC STRAIN=LT7;
RX PubMed=1846861; DOI=10.1128/jb.173.3.1321-1327.1991;
RA De Backer O., Colson C.;
RT "Two-step cloning and expression in Escherichia coli of the DNA
RT restriction-modification system StyLTI of Salmonella typhimurium.";
RL J. Bacteriol. 173:1321-1327(1991).
RN [5]
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 beta subtype methylase that binds the system-specific DNA
CC recognition site 5'-CAGAG-3' and methylates A-4 (of only 1 strand as
CC the other does not have an A residue). DNA restriction requires both
CC the Res and Mod subunits. {ECO:0000269|PubMed:1846861,
CC ECO:0000269|PubMed:1995420, 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:0000269|PubMed:1995420};
CC -!- SUBUNIT: Homodimer, also forms a functional restriction-competent
CC complex with Res. {ECO:0000250|UniProtKB:P12364}.
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; M90544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AE006468; AAL19311.1; -; Genomic_DNA.
DR PIR; JN0657; JN0657.
DR RefSeq; NP_459352.1; NC_003197.2.
DR RefSeq; WP_000910371.1; NC_003197.2.
DR AlphaFoldDB; P40814; -.
DR SMR; P40814; -.
DR STRING; 99287.STM0357; -.
DR REBASE; 165434; M.Fba101ORF2038P.
DR REBASE; 203812; M.Keu1446ORF2697P.
DR REBASE; 231846; M.Sen4024ORF3354P.
DR REBASE; 233833; M.Sen4839ORF3406P.
DR REBASE; 3515; M.StyLTI.
DR PaxDb; P40814; -.
DR EnsemblBacteria; AAL19311; AAL19311; STM0357.
DR GeneID; 1251876; -.
DR KEGG; stm:STM0357; -.
DR PATRIC; fig|99287.12.peg.378; -.
DR HOGENOM; CLU_020164_2_0_6; -.
DR OMA; QDDRKFT; -.
DR PhylomeDB; P40814; -.
DR BioCyc; SENT99287:STM0357-MON; -.
DR PRO; PR:P40814; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
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; 3.40.50.150; -; 1.
DR InterPro; IPR002941; DNA_methylase_N4/N6.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR002295; N4/N6-MTase_EcoPI_Mod-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR041405; T3RM_EcoP15I_C.
DR Pfam; PF01555; N6_N4_Mtase; 1.
DR Pfam; PF18273; T3RM_EcoP15I_C; 1.
DR PIRSF; PIRSF015855; TypeIII_Mtase_mKpnI; 1.
DR PRINTS; PR00506; D21N6MTFRASE.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Methyltransferase; Reference proteome; Restriction system;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..652
FT /note="Type III restriction-modification enzyme StyLTI Mod
FT subunit"
FT /id="PRO_0000088032"
FT REGION 135..138
FT /note="Binding of S-adenosyl methionine"
FT /evidence="ECO:0000255"
FT VARIANT 55
FT /note="Missing (in strain: LT7)"
FT /evidence="ECO:0000269|PubMed:8387444"
FT VARIANT 126
FT /note="A -> S (in strain: LT7)"
FT /evidence="ECO:0000269|PubMed:8387444"
SQ SEQUENCE 652 AA; 73336 MW; 385DE4851545C84E CRC64;
MLKDNQKHNE SVAPNSAFLS ELQRALPEFF TADRYNEQGE LIAKGGFDLA RFERALKARN
IDELTSGYQI DFIGKDYAKK QAGEKSVTVI VPDVEHNTLA ENKNSHNLFL TGDNLDVLRH
LQNNYADTVD MIYIDPPYNT GSDGFVYPDH FEYSDRALQD MFGLNDTELA RLKSIQGKST
HSAWLSFMYP RLFLARKLLK DTGFIFISID DNEYANLKLM MDEIFGEGGF VTNVMWKRKK
EISNDSDNVS IQGEYILVYA KTGQGALRLE PLSKEYIQKS YKEPTEQFPE GKWRPVPLTV
SKGLSGGGYT YKITTPNGTV HERLWAYPEA SYQKLVADNL VYFGKDNGGI PQRVMYAHHS
KGQPTTNYWD NVASNKEGKK EILDLFGDNV FDTPKPTALL KKIIKLAIDK DGVVLDFFAG
SGTTAHAVMA LNEEDGGQRT FILCTIDQAL SNNTIAKKAG YNTIDEISRE RITRVAAKIR
ANNPATNSDL GFKHYRFATP TQQTLDDLDS FDIATGHFIN TSGQLAAFTE SGFTDMINPF
SARGLGVPGG ASGEETLLTT WLVADGYKMD IDVQTVDFSG YCARYVDNTR LYLIDERWGT
EQTRDLLNHI GTHQLPVQTI VIYGYSFDLE SIRELEIGLK QLDQKVNLVK RY
