T1SH_HAEIN
ID T1SH_HAEIN Reviewed; 459 AA.
AC P44152;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Type I restriction enzyme HindI specificity subunit {ECO:0000305};
DE Short=S protein;
DE AltName: Full=Type I specificity subunit S.HindI {ECO:0000303|PubMed:12654995};
DE Short=S.HindI {ECO:0000303|PubMed:12654995};
DE AltName: Full=Type-1 restriction enzyme HindVIIP specificity subunit;
GN Name=hsdS {ECO:0000303|PubMed:7542800}; OrderedLocusNames=HI_1286;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP FUNCTION AS A METHYLASE.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=4591672; DOI=10.1016/0022-2836(73)90515-9;
RA Roy P.H., Smith H.O.;
RT "DNA methylases of Hemophilus influenzae Rd. I. Purification and
RT properties.";
RL J. Mol. Biol. 81:427-444(1973).
RN [3]
RP PARTIAL RECOGNITION SEQUENCE.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=4544320; DOI=10.1016/0022-2836(73)90516-0;
RA Roy P.H., Smith H.O.;
RT "DNA methylases of Hemophilus influenzae Rd. II. Partial recognition site
RT base sequences.";
RL J. Mol. Biol. 81:445-459(1973).
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 adenosines in
CC the sequence 5'-RAACN(5)TAG-3'. Methylation protects against cleavage
CC by HindI (PubMed:4591672) (Probable). In the presence of the R subunit
CC the complex can also act as an endonuclease, binding to the same target
CC sequence but cutting the DNA some distance from this site. Whether the
CC DNA is cut or modified depends on the methylation state of the target
CC sequence. When the target site is unmodified, the DNA is cut. When the
CC target site is hemimethylated, the complex acts as a maintenance MTase
CC modifying the DNA so that both strands become methylated (Probable)
CC (PubMed:12654995). After locating a non-methylated recognition site,
CC the enzyme complex serves as a molecular motor that translocates DNA in
CC an ATP-dependent manner until a collision occurs that triggers cleavage
CC (By similarity). {ECO:0000250|UniProtKB:P05719,
CC ECO:0000269|PubMed:4591672, ECO:0000303|PubMed:12654995,
CC ECO:0000305|PubMed:4544320, ECO:0000305|PubMed:4591672}.
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, ECO:0000305|PubMed:4544320,
CC ECO:0000305|PubMed:4591672}.
CC -!- DOMAIN: Contains two DNA recognition domains, each specifying
CC recognition of one of the two defined components of the target
CC sequence. {ECO:0000250|UniProtKB:P05719}.
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}.
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DR EMBL; L42023; AAC22935.1; -; Genomic_DNA.
DR PIR; H64024; H64024.
DR RefSeq; NP_439438.1; NC_000907.1.
DR RefSeq; WP_005694527.1; NC_000907.1.
DR AlphaFoldDB; P44152; -.
DR SMR; P44152; -.
DR STRING; 71421.HI_1286; -.
DR REBASE; 155514; S.VscVS05ORF3158P.
DR REBASE; 191854; S2.Apa1447ORF2799P.
DR REBASE; 191858; S2.Apa1447ORF3031P.
DR REBASE; 191870; S2.Apa1342ORF2943P.
DR REBASE; 191873; S1.Apa1342ORF3157P.
DR REBASE; 203816; S.Lbr1106ORF30P.
DR REBASE; 231751; S.Sen4839ORF3820P.
DR REBASE; 5608; S.HindI.
DR EnsemblBacteria; AAC22935; AAC22935; HI_1286.
DR KEGG; hin:HI_1286; -.
DR PATRIC; fig|71421.8.peg.1338; -.
DR eggNOG; COG0732; Bacteria.
DR HOGENOM; CLU_021095_2_1_6; -.
DR OMA; KRWFVDF; -.
DR PhylomeDB; P44152; -.
DR BioCyc; HINF71421:G1GJ1-1312-MON; -.
DR PRO; PR:P44152; -.
DR Proteomes; UP000000579; 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 1: Evidence at protein level;
KW DNA-binding; Reference proteome; Repeat; Restriction system.
FT CHAIN 1..459
FT /note="Type I restriction enzyme HindI specificity subunit"
FT /id="PRO_0000198040"
SQ SEQUENCE 459 AA; 51402 MW; F925AACF03C88D96 CRC64;
MSDWKEYSLG DISRNISRRF DFNAYPNVVF INTGDVLNNK FLHCEISNVK DLPGQAKKAI
KKGDILYSEI RPGNGRYLFV DNDLDNYVVS TKFMVIEPNA NIVLPEFLFL LLISNETTEY
FKMIAESRSG TFPQITFDSV SSLSLNIPDK ETQQKILDII TPLDDKIELN TQINQTLEQI
AQALFKSWFV DFDPVRAKAQ ALSDGMSLEQ AELAAMQAIS GKTPEELTAL SQTQPDRYAE
LAETAKAFPC EMVEVDGVEV DGVEVPRGWE MKALSDLGQI ICGKTPSKSN KEFYGDDVPF
IKIPDMHNQV FITQTTDNLS VVGANYQSKK YIPAKSICVS CIATVGLVSM TSKPSHTNQQ
INSIIPDDEQ SCEFLYLSLK QPSMTKYLKD LASGGTATLN LNTSTFSKIE IITPSKEIIY
IFQKKVVSIF EKTLSNSIEN KRLTEIRDLL LPRLLNGEI
