T1S_SALTY
ID T1S_SALTY Reviewed; 469 AA.
AC P06187;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Type I restriction enzyme StySJI specificity subunit {ECO:0000303|PubMed:3025838};
DE Short=S protein {ECO:0000303|PubMed:3025838};
DE AltName: Full=Type I restriction and modification system SB {ECO:0000303|PubMed:2838725};
DE AltName: Full=Type I specificity subunit S.StySJI {ECO:0000303|PubMed:12654995};
DE Short=S.StySJI {ECO:0000303|PubMed:12654995};
DE AltName: Full=Type-1 restriction enzyme StySJI specificity subunit;
GN Name=hsdS {ECO:0000303|PubMed:3025838}; OrderedLocusNames=STM4524;
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], FUNCTION, AND DOMAIN.
RC STRAIN=LT2;
RX PubMed=2838725; DOI=10.1111/j.1365-2958.1987.tb00521.x;
RA Gann A.A.F., Campbell A.J.B., Collins J.F., Coulson A.F.W., Murray N.E.;
RT "Reassortment of DNA recognition domains and the evolution of new
RT specificities.";
RL Mol. Microbiol. 1:13-22(1987).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 153-197, FUNCTION, AND DOMAIN.
RX PubMed=3025838; DOI=10.1073/pnas.83.24.9368;
RA Fuller-Pace F.V., Murray N.E.;
RT "Two DNA recognition domains of the specificity polypeptides of a family of
RT type I restriction enzymes.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:9368-9372(1986).
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: The specificity (S) subunit of a type I restriction enzyme;
CC this subunit dictates DNA sequence specificity. The M and S subunits
CC together form a methyltransferase (MTase) that methylates two adenine
CC residues of the sequence 5'-GAGN(6)GTRC-3'. In the presence of the R
CC subunit the complex can also act as an endonuclease, binding to the
CC same target sequence but cutting the DNA some distance from this site.
CC Whether the DNA is cut or modified depends on the methylation state of
CC the target sequence. When the target site is unmodified, the DNA is
CC cut. When the target site is hemimethylated, the complex acts as a
CC maintenance MTase modifying the DNA so that both strands become
CC methylated (PubMed:3025838, PubMed:12654995). After locating a non-
CC methylated recognition site, the enzyme complex serves as a molecular
CC motor that translocates DNA in an ATP-dependent manner until a
CC collision occurs that triggers cleavage (By similarity).
CC {ECO:0000250|UniProtKB:P05719, ECO:0000269|PubMed:3025838,
CC ECO:0000303|PubMed:12654995}.
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:P05719}.
CC -!- DOMAIN: Contains two DNA recognition domains, each specifying
CC recognition of one of the two defined components of the target sequence
CC (PubMed:3025838, PubMed:2838725). The recognition domains can be
CC exchanged between different S proteins, generating enzymes that have
CC new sequence specificities (PubMed:2838725).
CC {ECO:0000269|PubMed:2838725, ECO:0000269|PubMed:3025838}.
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:P05719}.
CC -!- SIMILARITY: Belongs to the type-I restriction system S methylase
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Y00524; CAA68580.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL23342.1; -; Genomic_DNA.
DR EMBL; K03551; AAA27146.1; -; Genomic_DNA.
DR RefSeq; NP_463383.1; NC_003197.2.
DR RefSeq; WP_000014001.1; NC_003197.2.
DR AlphaFoldDB; P06187; -.
DR SMR; P06187; -.
DR STRING; 99287.STM4524; -.
DR REBASE; 205123; S2.Bve1413ORF3003P.
DR REBASE; 3686; S.StyLTIII.
DR REBASE; 3700; S.StySJI.
DR PaxDb; P06187; -.
DR EnsemblBacteria; AAL23342; AAL23342; STM4524.
DR GeneID; 1256050; -.
DR KEGG; stm:STM4524; -.
DR PATRIC; fig|99287.12.peg.4767; -.
DR HOGENOM; CLU_021095_10_2_6; -.
DR OMA; MLAIDAC; -.
DR PhylomeDB; P06187; -.
DR BioCyc; SENT99287:STM4524-MON; -.
DR PRO; PR:P06187; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 3.90.220.20; -; 2.
DR InterPro; IPR000055; Restrct_endonuc_typeI_TRD.
DR InterPro; IPR044946; Restrct_endonuc_typeI_TRD_sf.
DR Pfam; PF01420; Methylase_S; 2.
PE 3: Inferred from homology;
KW DNA-binding; Reference proteome; Restriction system.
FT CHAIN 1..469
FT /note="Type I restriction enzyme StySJI specificity
FT subunit"
FT /id="PRO_0000198039"
SQ SEQUENCE 469 AA; 51910 MW; E86A039C641127E8 CRC64;
MSGGKLPEGW ATSTINEMCN LNPKLKLDDD LDVGFMPMAG VPTTYLGKCN FETKKWSEVK
KGFTQFQNDD VIFAKITPCF ENGKAVVIKE FPNGYGAGST EYYVLRSING LINPHWLFAL
VKTKDFLTNG ALNMSGSVGH KRVTKEFLEN YGVPVPPLAE QKVIAEKLDT LLAQVDSTKA
RLEQIPQILK RFRQSVIVAA VNGQLTKELH KKNKFKLTEL NISIPSLWKI SEIGQFADVK
GGKRLPKGES LIAENTGFPY IRAGQLKNGT VLPEGQLYLE EYIQKSISRY TVSSGDLYIT
IVGACIGDAG IIPDVYNNAN LTENAAKICN LNENIFNRFL SLWLRSSYLQ DIINSEIKSG
AQGKLALARI KSLPLILPPL QEQHEIVRRV EQLFAYADTI EKQVNNALTR VNSLTQSILA
KAFRGELTAQ WRAENPELIS GENSAAALLE KIKAERAASG GKKTSRKKA
