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T1M_BACTN
ID   T1M_BACTN               Reviewed;         472 AA.
AC   Q89Z59;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Type I restriction enzyme BthVORF4518P methylase subunit;
DE            Short=M protein;
DE            EC=2.1.1.72 {ECO:0000250|UniProtKB:P08957};
DE   AltName: Full=Type I methyltransferase M.BthVORF4518P {ECO:0000303|PubMed:12654995};
DE            Short=M.BthVORF4518P;
GN   Name=hsdM {ECO:0000305}; OrderedLocusNames=BT_4518;
OS   Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS   CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=226186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC   VPI-5482 / E50;
RX   PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA   Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(2003).
RN   [2]
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).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH
RP   S-ADENOSYL-L-METHIONINE.
RG   Joint center for structural genomics (JCSG);
RT   "Crystal structure of type I restriction enzyme protein (NP_813429.1) from
RT   bacteriodes thetaiotaomicron VPI-5482 at 2.20 A resolution resolution.";
RL   Submitted (JAN-2007) to the PDB data bank.
CC   -!- FUNCTION: The subtype gamma methyltransferase (M) subunit of a type I
CC       restriction enzyme. The M and S subunits together form a
CC       methyltransferase (MTase) that methylates two adenine residues of an
CC       undetermined sequence. In the presence of the R subunit the complex can
CC       also act as an endonuclease, binding to the same target sequence but
CC       cutting the DNA some distance from this site. Whether the DNA is cut or
CC       modified depends on the methylation state of the target sequence. When
CC       the target site is unmodified, the DNA is cut. When the target site is
CC       hemimethylated, the complex acts as a maintenance MTase modifying the
CC       DNA so that both strands become methylated. 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. {ECO:0000250|UniProtKB:P08957,
CC       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:0000250|UniProtKB:P08957};
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:P08957}.
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:P08957}.
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AE015928; AAO79623.1; -; Genomic_DNA.
DR   RefSeq; NP_813429.1; NC_004663.1.
DR   RefSeq; WP_011109305.1; NC_004663.1.
DR   PDB; 2OKC; X-ray; 2.20 A; A/B=1-444.
DR   PDBsum; 2OKC; -.
DR   AlphaFoldDB; Q89Z59; -.
DR   SMR; Q89Z59; -.
DR   STRING; 226186.BT_4518; -.
DR   REBASE; 191896; M.Apa1447ORF2439P.
DR   REBASE; 246644; M.Mmy2708ORF27P.
DR   REBASE; 403240; Ssp8227ORF2875P.
DR   REBASE; 7071; M.BthVORF4518P.
DR   PaxDb; Q89Z59; -.
DR   PRIDE; Q89Z59; -.
DR   DNASU; 1073274; -.
DR   EnsemblBacteria; AAO79623; AAO79623; BT_4518.
DR   GeneID; 60925694; -.
DR   KEGG; bth:BT_4518; -.
DR   PATRIC; fig|226186.12.peg.4602; -.
DR   eggNOG; COG0286; Bacteria.
DR   HOGENOM; CLU_018284_2_0_10; -.
DR   InParanoid; Q89Z59; -.
DR   OMA; THRLALM; -.
DR   EvolutionaryTrace; Q89Z59; -.
DR   PRO; PR:Q89Z59; -.
DR   Proteomes; UP000001414; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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; 1.20.1260.30; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR022749; D12N6_MeTrfase_N.
DR   InterPro; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR038333; T1MK-like_N_sf.
DR   Pfam; PF12161; HsdM_N; 1.
DR   Pfam; PF02384; N6_Mtase; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA-binding; Methyltransferase; Reference proteome;
KW   Restriction system; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..472
FT                   /note="Type I restriction enzyme BthVORF4518P methylase
FT                   subunit"
FT                   /id="PRO_0000310988"
FT   BINDING         151..156
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:2OKC"
FT   BINDING         181..183
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:2OKC"
FT   BINDING         214
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:2OKC"
FT   BINDING         243..244
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000269|Ref.3, ECO:0007744|PDB:2OKC"
FT   HELIX           11..24
FT                   /evidence="ECO:0007829|PDB:2OKC"
FT   HELIX           29..51
FT                   /evidence="ECO:0007829|PDB:2OKC"
FT   HELIX           64..68
FT                   /evidence="ECO:0007829|PDB:2OKC"
FT   HELIX           73..87
FT                   /evidence="ECO:0007829|PDB:2OKC"
FT   HELIX           91..96
FT                   /evidence="ECO:0007829|PDB:2OKC"
FT   TURN            97..99
FT                   /evidence="ECO:0007829|PDB:2OKC"
FT   HELIX           107..118
FT                   /evidence="ECO:0007829|PDB:2OKC"
FT   HELIX           128..142
FT                   /evidence="ECO:0007829|PDB:2OKC"
FT   TURN            145..147
FT                   /evidence="ECO:0007829|PDB:2OKC"
FT   HELIX           150..152
FT                   /evidence="ECO:0007829|PDB:2OKC"
FT   HELIX           156..166
FT                   /evidence="ECO:0007829|PDB:2OKC"
FT   STRAND          174..176
FT                   /evidence="ECO:0007829|PDB:2OKC"
FT   HELIX           183..193
FT                   /evidence="ECO:0007829|PDB:2OKC"
FT   HELIX           200..207
FT                   /evidence="ECO:0007829|PDB:2OKC"
FT   STRAND          210..215
FT                   /evidence="ECO:0007829|PDB:2OKC"
FT   HELIX           217..229
FT                   /evidence="ECO:0007829|PDB:2OKC"
FT   STRAND          238..241
FT                   /evidence="ECO:0007829|PDB:2OKC"
FT   TURN            244..246
FT                   /evidence="ECO:0007829|PDB:2OKC"
FT   STRAND          253..258
FT                   /evidence="ECO:0007829|PDB:2OKC"
FT   STRAND          277..279
FT                   /evidence="ECO:0007829|PDB:2OKC"
FT   HELIX           284..295
FT                   /evidence="ECO:0007829|PDB:2OKC"
FT   STRAND          296..307
FT                   /evidence="ECO:0007829|PDB:2OKC"
FT   HELIX           308..312
FT                   /evidence="ECO:0007829|PDB:2OKC"
FT   HELIX           316..327
FT                   /evidence="ECO:0007829|PDB:2OKC"
FT   STRAND          328..335
FT                   /evidence="ECO:0007829|PDB:2OKC"
FT   STRAND          338..343
FT                   /evidence="ECO:0007829|PDB:2OKC"
FT   STRAND          348..357
FT                   /evidence="ECO:0007829|PDB:2OKC"
FT   STRAND          360..366
FT                   /evidence="ECO:0007829|PDB:2OKC"
FT   STRAND          375..378
FT                   /evidence="ECO:0007829|PDB:2OKC"
FT   HELIX           382..385
FT                   /evidence="ECO:0007829|PDB:2OKC"
FT   HELIX           386..393
FT                   /evidence="ECO:0007829|PDB:2OKC"
FT   TURN            401..403
FT                   /evidence="ECO:0007829|PDB:2OKC"
FT   STRAND          408..413
FT                   /evidence="ECO:0007829|PDB:2OKC"
FT   HELIX           414..419
FT                   /evidence="ECO:0007829|PDB:2OKC"
FT   HELIX           421..423
FT                   /evidence="ECO:0007829|PDB:2OKC"
SQ   SEQUENCE   472 AA;  53127 MW;  3891797D2845329D CRC64;
     MATNSSTEQS LTKKVWNLAT TLAGQGIGFT DYITQLTYLL FLKMDAENVE MFGEESAIPT
     GYQWADLIAF DGLDLVKQYE ETLKLLSELD NLIGTIYTKA QNKIDKPVYL KKVITMIDEE
     QWLIMDGDVK GAIYESILEK NGQDKKSGAG QYFTPRPLIQ AMVDCINPQM GETVCDPACG
     TGGFLLTAYD YMKGQSASKE KRDFLRDKAL HGVDNTPLVV TLASMNLYLH GIGTDRSPIV
     CEDSLEKEPS TLVDVILANP PFGTRPAGSV DINRPDFYVE TKNNQLNFLQ HMMLMLKTGG
     RAAVVLPDNV LFEAGAGETI RKRLLQDFNL HTILRLPTGI FYAQGVKANV LFFSKGQPTK
     EIWFYDYRTD IKHTLATNKL ERHHLDDFVS CYNNRVEIYD AENNPQGRWR KYPVDEIIAR
     DKTSLDITWI KPGGEVDDRS LAELMADIKD KSQTISRAVT ELEKLLANIE EN
 
 
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