T3RE_SALTY
ID T3RE_SALTY Reviewed; 990 AA.
AC P40815;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Type III restriction-modification enzyme StyLTI Res subunit {ECO:0000303|PubMed:12654995};
DE Short=Type III R-M system StyLTI {ECO:0000303|PubMed:8387444};
DE EC=3.1.21.5;
DE AltName: Full=Type III restriction enzyme StyLTI {ECO:0000303|PubMed:12654995};
GN Name=res {ECO:0000303|PubMed:11677609}; OrderedLocusNames=STM0358;
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.
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 [4]
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: A type III restriction enzyme that recognizes 2 inversely
CC oriented double-stranded sequences 5'-CAGAG-3' and cleaves DNA 25-27
CC base pairs downstream. After binding to one recognition site undergoes
CC random one-dimensional diffusion along DNA until it collides with a
CC stationary enzyme bound to the second DNA site, which is when DNA
CC cleavage occurs. DNA restriction requires both the Res and Mod
CC subunits. {ECO:0000250|UniProtKB:Q5ZND2, ECO:0000303|PubMed:12654995}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of DNA to give specific double-
CC stranded fragments with terminal 5'-phosphates.; EC=3.1.21.5;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- COFACTOR:
CC Name=S-adenosyl-L-methionine; Xref=ChEBI:CHEBI:59789;
CC Evidence={ECO:0000250|UniProtKB:P08764};
CC -!- SUBUNIT: Contains two different subunits: Res and Mod.
CC {ECO:0000250|UniProtKB:Q5ZND2}.
CC -!- SIMILARITY: Belongs to the type III restriction-modification system Res
CC protein family. {ECO:0000305}.
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DR EMBL; M90544; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AE006468; AAL19312.1; -; Genomic_DNA.
DR PIR; JN0658; JN0658.
DR RefSeq; NP_459353.3; NC_003197.2.
DR RefSeq; WP_001651666.1; NC_003197.2.
DR AlphaFoldDB; P40815; -.
DR SMR; P40815; -.
DR REBASE; 1788; StyLTI.
DR REBASE; 231845; Sen4024ORF3354P.
DR REBASE; 233832; Sen4839ORF3406P.
DR PaxDb; P40815; -.
DR EnsemblBacteria; AAL19312; AAL19312; STM0358.
DR GeneID; 1251877; -.
DR KEGG; stm:STM0358; -.
DR HOGENOM; CLU_011799_1_0_6; -.
DR OMA; ELWQTIN; -.
DR PhylomeDB; P40815; -.
DR BioCyc; SENT99287:STM0358-MON; -.
DR PRO; PR:P40815; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0015668; F:type III site-specific deoxyribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014883; VRR_NUC.
DR Pfam; PF04851; ResIII; 1.
DR Pfam; PF08774; VRR_NUC; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
PE 3: Inferred from homology;
KW ATP-binding; DNA-binding; Endonuclease; Helicase; Hydrolase; Nuclease;
KW Nucleotide-binding; Reference proteome; Restriction system;
KW S-adenosyl-L-methionine.
FT CHAIN 1..990
FT /note="Type III restriction-modification enzyme StyLTI Res
FT subunit"
FT /id="PRO_0000077375"
FT DOMAIN 884..970
FT /note="VRR-NUC"
FT /evidence="ECO:0000255"
FT REGION 50..545
FT /note="Helicase-like domain"
FT /evidence="ECO:0000250|UniProtKB:P08764"
FT REGION 913..937
FT /note="Endonuclease domain"
FT /evidence="ECO:0000250|UniProtKB:P08764"
FT VARIANT 17
FT /note="A -> R (in strain: LT7)"
FT /evidence="ECO:0000269|PubMed:8387444"
FT VARIANT 293..298
FT /note="KLILRR -> EINPPT (in strain: LT7)"
FT /evidence="ECO:0000269|PubMed:8387444"
FT VARIANT 350
FT /note="S -> T (in strain: LT7)"
FT /evidence="ECO:0000269|PubMed:8387444"
FT VARIANT 420
FT /note="L -> V (in strain: LT7)"
FT /evidence="ECO:0000269|PubMed:8387444"
FT VARIANT 464..465
FT /note="SG -> R (in strain: LT7)"
FT /evidence="ECO:0000269|PubMed:8387444"
FT VARIANT 536..537
FT /note="GL -> AV (in strain: LT7)"
FT /evidence="ECO:0000269|PubMed:8387444"
FT VARIANT 945..990
FT /note="DQVILDAQRKFFDMLRRQNINVEFAEATSAPAVFSTINGLIEGKAN -> IR
FT LFLMRNVNSSICCVGKISMSSLRKDQRAGGIFYDQWLD (in strain: LT7)"
FT /evidence="ECO:0000269|PubMed:8387444"
SQ SEQUENCE 990 AA; 113388 MW; 8E821E02A895D16E CRC64;
MMNILLEELP HQEQALAAIL ASFTGIDHAQ ADHNHYANPL IKERYDDKAN IDVKMETGTG
KTYVYTRLMY ELHQKYGLFK FVLVVPTPAI KEGARNFITS DYARQHFSQF YENTRMELCT
INAGDFKVKS GRKNFPAQLL SFTDASRRDS HTIQVLLINA QMLNSASMTR DDYDQTLLGG
LTSPVKGLQM TRPVVIIDEP HRFARDNKFY RAIQAIQPQM IVRFGATFPD IVEGKGKNKC
VRKDYYRRQP QFDLNAVDSF NDGLVKGIDI YYPNLPEEQA NNRYIVDSVT AKKLILRRGS
KIAEVGVGEN LADVDAGFEG SIEYAGSKML SNDLELEAGM ALVPGTFGAS YQELIIQDAI
DKHFDTEQAN FLRSNEPENN APRIKTLSLF FIDSIKSYRD DEGWLKVTFE RLLKKKLTQL
IDDYQRKTLP REVEYLSFLQ ATLASLHSDN QNVHAGYFGE DRGSGDEAIQ AEVDDILKNK
EKLLSFSDHH GNWETRRFLF SKWTLREGWD NPNVFVIAKL RSSGSESSKI QEVGRGLRLP
VDENGHRVHQ EEWPSRLSFL IGYDEKAFAS MLVDEINRDS KVQLNEQKLD EAMITLIVTE
RQKVDPAFTE LRLLEDLDDK KLINRSNEFK PSVTLNGETK SGFAWLLEFY PELTQARVRA
DRIRDNKPAS RLRVRLRKEN WEQLSSIWEQ FSRRYMLQFE RSGASLEQIA AEVLRDPALY
IRQKPSQVQQ RLVSNEDNGR FEVAQREGEL AASEFMAGMK YGHFLKQLAL RTSLPVNVLH
PVLMAMLRDV LHGDSRYLSE ISLDNMTRAL QTRINAHFAQ RHDYLPLDFQ ASTSVFDSTA
RQFREEISAE IVGKNVDENA IDDPRSLYQI PPLRYDSVDP ELPLLKYDYP QQVSVFGKLP
KRAIQIPKYT GGSTTPDFVY RIERQDADSV YLLVETKAEN MRVGDQVILD AQRKFFDMLR
RQNINVEFAE ATSAPAVFST INGLIEGKAN
