T1S1_ECOLX
ID T1S1_ECOLX Reviewed; 404 AA.
AC P10485;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Type I restriction enzyme EcoR124II specificity subunit {ECO:0000305};
DE Short=S protein;
DE AltName: Full=Type I restriction enzyme EcoR124/3 specificity subunit {ECO:0000303|PubMed:2784505};
DE AltName: Full=Type I specificity subunit S.EcoR124II {ECO:0000303|PubMed:12654995};
DE Short=S.EcoR124II {ECO:0000303|PubMed:12654995};
DE AltName: Full=Type-1 restriction enzyme EcoR124II specificity subunit;
GN Name=hsdS; Synonyms=hss;
OS Escherichia coli.
OG Plasmid IncFIV R124/3.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2784505; DOI=10.1016/0022-2836(89)90369-0;
RA Price C., Lingner J., Bickle J., Firman T.A., Glover S.W.;
RT "Basis for changes in DNA recognition by the EcoR124 and EcoR124/3 type I
RT DNA restriction and modification enzymes.";
RL J. Mol. Biol. 205:115-125(1989).
RN [2]
RP SEQUENCE REVISION TO 179-180; 340-344 AND C-TERMINUS.
RA Blundell A.;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
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).
RN [4] {ECO:0007744|PDB:7BST, ECO:0007744|PDB:7BTO, ECO:0007744|PDB:7BTP, ECO:0007744|PDB:7BTQ, ECO:0007744|PDB:7BTR}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.97 ANGSTROMS) OF 1-1032 IN COMPLEX WITH
RP R AND S SUBUNITS AND WITH ESCHERICHIA PHAGE T7 PROTEIN OCR, STRUCTURE BY
RP ELECTRON MICROSCOPY (6.33 ANGSTROMS) IN COMPLEX WITH M SUBUNIT AND DNA,
RP FUNCTION, INTERACTION WITH ESCHERICHIA PHAGE T7 PROTEIN OCR (MICROBIAL
RP INFECTION), DOMAIN, AND DNA-BINDING.
RX PubMed=32483229; DOI=10.1038/s41564-020-0731-z;
RA Gao Y., Cao D., Zhu J., Feng H., Luo X., Liu S., Yan X.X., Zhang X.,
RA Gao P.;
RT "Structural insights into assembly, operation and inhibition of a type I
RT restriction-modification system.";
RL Nat. Microbiol. 5:1107-1118(2020).
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 A-3 on the
CC top and bottom strand of the sequence 5'-GAAN(7)RTCG-3'. In the
CC presence of the R subunit the complex can also act as an endonuclease,
CC binding to the same target sequence but cutting the DNA some distance
CC from this site. Whether the DNA is cut or modified depends on the
CC methylation state of the target sequence. When the target site is
CC unmodified, the DNA is cut. When the target site is hemimethylated, the
CC complex acts as a maintenance MTase modifying the DNA so that both
CC strands become methylated (PubMed:32483229, PubMed:12654995). 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 (Probable).
CC {ECO:0000269|PubMed:32483229, ECO:0000303|PubMed:12654995,
CC ECO:0000305|PubMed:32483229}.
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). There is an
CC equilibrium between R(2)M(2)S(1) and R(1)M(2)S(1); the latter is
CC methylation and translocation proficient but restriction deficient.
CC {ECO:0000269|PubMed:32483229}.
CC -!- SUBUNIT: (Microbial infection) Holoenenzyme interacts with Escherichia
CC phage T7 protein Ocr; this interaction leads to the inhibition of the
CC restriction activity, but may still allow methylation and
CC translocation. {ECO:0000269|PubMed:32483229}.
CC -!- DOMAIN: Contains two DNA recognition domains (TRD), each specifying
CC recognition of one of the two defined components of the target
CC sequence. {ECO:0000269|PubMed:2784505, ECO:0000305|PubMed:32483229}.
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:0000269|PubMed:32483229}.
CC -!- SIMILARITY: Belongs to the type-I restriction system S methylase
CC family. {ECO:0000305}.
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DR EMBL; X13145; CAB37630.2; -; Genomic_DNA.
DR PIR; S02167; S02167.
DR PDB; 7BST; EM; 4.37 A; A=1-404.
DR PDB; 7BTO; EM; 3.97 A; I=1-404.
DR PDB; 7BTP; EM; 4.01 A; E=1-404.
DR PDB; 7BTQ; EM; 4.54 A; E=1-404.
DR PDB; 7BTR; EM; 4.54 A; E=1-404.
DR PDBsum; 7BST; -.
DR PDBsum; 7BTO; -.
DR PDBsum; 7BTP; -.
DR PDBsum; 7BTQ; -.
DR PDBsum; 7BTR; -.
DR AlphaFoldDB; P10485; -.
DR SMR; P10485; -.
DR DIP; DIP-17003N; -.
DR REBASE; 204160; S.Bli1441ORF2992P.
DR REBASE; 204720; S.Bsu333ORF2986P.
DR REBASE; 3647; S.EcoR124I.
DR REBASE; 3648; S.EcoR124II.
DR PRIDE; P10485; -.
DR PRO; PR:P10485; -.
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 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Plasmid; Restriction system.
FT CHAIN 1..404
FT /note="Type I restriction enzyme EcoR124II specificity
FT subunit"
FT /id="PRO_0000198036"
FT REGION 1..153
FT /note="Target-recognition domain 1"
FT /evidence="ECO:0000305|PubMed:32483229"
FT REGION 154..199
FT /note="Conserved region 1"
FT /evidence="ECO:0000305|PubMed:32483229"
FT REGION 200..349
FT /note="Target-recognition domain 2"
FT /evidence="ECO:0000305|PubMed:32483229"
FT REGION 350..404
FT /note="Conserved region 2"
FT /evidence="ECO:0000305|PubMed:32483229"
SQ SEQUENCE 404 AA; 46179 MW; 164B882F0F594D16 CRC64;
MSEMSYLEKL LDGVEVEWLP LGEITKYEQP TKYLVKAKDY HDTYTIPVLT AGKTFILGYT
NETHGIYQAS KAPVIIFDDF TTANKWVDFD FKAKSSAMKM VTSCDDNKTL LKYVYYWLNT
LPSEFAEGDH KRQWISNYSQ KKIPIPCPDN PEKSLAIQSE IVRILDKFTA LTAELTAELN
MRKKQYNYYR DQLLSFKEGE VEWKTLGEIG KWYGGGTPSK NKIEFWENGS IPWISPKDMG
RTLVDSSEDY ITEEAVLHSS TKLIPANSIA IVVRSSILDK VLPSALIKVP ATLNQDMKAV
IPHENILVKY IYHMIGSRGS DILRAAKKTG GSVASIDSKK LFSFKIPVPN INEQQRIVEI
LDKFDTLTNS ITEGLPREIE LRQKQYEYYR DLLFSFPKPE TVSN
