T2S3_STAAU
ID T2S3_STAAU Reviewed; 489 AA.
AC P16667;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Type II restriction enzyme Sau3AI {ECO:0000303|PubMed:12654995};
DE Short=R.Sau3AI {ECO:0000303|PubMed:2227451};
DE EC=3.1.21.4 {ECO:0000269|PubMed:2227451};
DE AltName: Full=Endonuclease Sau3AI;
DE AltName: Full=Type-2 restriction enzyme Sau3AI;
GN Name=sau3AIR;
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 49834 / 3A;
RX PubMed=2227451; DOI=10.1016/0378-1119(90)90465-4;
RA Seeber S., Kessler C., Goetz F.;
RT "Cloning, expression and characterization of the Sau3AI restriction and
RT modification genes in Staphylococcus carnosus TM300.";
RL Gene 94:37-43(1990).
RN [2]
RP NOMENCLATURE, AND SUBTYPES.
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: An E and P subtype restriction enzyme that recognizes the
CC double-stranded sequence 5'-GATC-3' and cleaves before G-1.
CC {ECO:0000269|PubMed:2227451, 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=3.1.21.4;
CC Evidence={ECO:0000269|PubMed:2227451};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
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DR EMBL; M32470; AAA26672.1; -; Genomic_DNA.
DR PIR; JQ0759; JQ0759.
DR RefSeq; WP_000446878.1; NZ_WOUL01000015.1.
DR PDB; 2REU; X-ray; 1.90 A; A=233-489.
DR PDB; 4PXG; X-ray; 2.45 A; A/B=1-489.
DR PDBsum; 2REU; -.
DR PDBsum; 4PXG; -.
DR AlphaFoldDB; P16667; -.
DR SMR; P16667; -.
DR REBASE; 1604; Sau3AI.
DR REBASE; 252065; Psp7025ORF2592P.
DR PRIDE; P16667; -.
DR EvolutionaryTrace; P16667; -.
DR PRO; PR:P16667; -.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0009036; F:type II site-specific deoxyribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR CDD; cd00583; MutH_Sau3AI; 1.
DR Gene3D; 3.40.600.10; -; 2.
DR InterPro; IPR011337; DNA_rep_MutH/RE_typeII_Sau3AI.
DR InterPro; IPR037057; DNA_rep_MutH/T2_RE_sf.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR Pfam; PF02976; MutH; 1.
DR SMART; SM00927; MutH; 1.
DR SUPFAM; SSF52980; SSF52980; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Endonuclease; Hydrolase; Magnesium; Nuclease;
KW Restriction system.
FT CHAIN 1..489
FT /note="Type II restriction enzyme Sau3AI"
FT /id="PRO_0000077358"
FT HELIX 7..17
FT /evidence="ECO:0007829|PDB:4PXG"
FT HELIX 22..26
FT /evidence="ECO:0007829|PDB:4PXG"
FT HELIX 38..44
FT /evidence="ECO:0007829|PDB:4PXG"
FT STRAND 64..72
FT /evidence="ECO:0007829|PDB:4PXG"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:4PXG"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:4PXG"
FT HELIX 91..95
FT /evidence="ECO:0007829|PDB:4PXG"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:4PXG"
FT HELIX 103..108
FT /evidence="ECO:0007829|PDB:4PXG"
FT STRAND 109..117
FT /evidence="ECO:0007829|PDB:4PXG"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:4PXG"
FT STRAND 128..136
FT /evidence="ECO:0007829|PDB:4PXG"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:4PXG"
FT HELIX 141..159
FT /evidence="ECO:0007829|PDB:4PXG"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:4PXG"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:4PXG"
FT STRAND 171..178
FT /evidence="ECO:0007829|PDB:4PXG"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:4PXG"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:4PXG"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:4PXG"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:4PXG"
FT HELIX 205..215
FT /evidence="ECO:0007829|PDB:4PXG"
FT HELIX 229..232
FT /evidence="ECO:0007829|PDB:4PXG"
FT HELIX 237..245
FT /evidence="ECO:0007829|PDB:2REU"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:2REU"
FT HELIX 253..259
FT /evidence="ECO:0007829|PDB:2REU"
FT HELIX 269..278
FT /evidence="ECO:0007829|PDB:2REU"
FT HELIX 294..299
FT /evidence="ECO:0007829|PDB:4PXG"
FT STRAND 301..308
FT /evidence="ECO:0007829|PDB:2REU"
FT HELIX 325..329
FT /evidence="ECO:0007829|PDB:2REU"
FT HELIX 343..350
FT /evidence="ECO:0007829|PDB:2REU"
FT STRAND 352..360
FT /evidence="ECO:0007829|PDB:2REU"
FT STRAND 366..374
FT /evidence="ECO:0007829|PDB:2REU"
FT HELIX 378..382
FT /evidence="ECO:0007829|PDB:2REU"
FT HELIX 384..398
FT /evidence="ECO:0007829|PDB:2REU"
FT STRAND 401..406
FT /evidence="ECO:0007829|PDB:2REU"
FT STRAND 413..418
FT /evidence="ECO:0007829|PDB:2REU"
FT HELIX 423..425
FT /evidence="ECO:0007829|PDB:2REU"
FT STRAND 427..436
FT /evidence="ECO:0007829|PDB:2REU"
FT STRAND 440..443
FT /evidence="ECO:0007829|PDB:2REU"
FT STRAND 446..448
FT /evidence="ECO:0007829|PDB:2REU"
FT STRAND 454..457
FT /evidence="ECO:0007829|PDB:2REU"
FT STRAND 466..470
FT /evidence="ECO:0007829|PDB:2REU"
FT STRAND 472..476
FT /evidence="ECO:0007829|PDB:2REU"
FT HELIX 478..485
FT /evidence="ECO:0007829|PDB:2REU"
FT HELIX 486..488
FT /evidence="ECO:0007829|PDB:2REU"
SQ SEQUENCE 489 AA; 56471 MW; FFC3762A949B86EB CRC64;
MESYLTKQAV HNRAKEAVGK SVLELNGGES IKQSKSSVGD AFENWFGKKK DSDSKPDMAE
AGVELKATPF KKLKNGKYSS KERLVLNIIN YEKVANENFE TSSFLSKNNT IELAFYEYIK
GTPSDNWIIK EAVLYEMHKN PIDYEIIKQD WEIINQYINE GKAHELSEGL TSYLAPCTKG
ANASSLRNQP YSDIKAKQRA FSLKSGYMTS ILRKYVLGDE KIDSIVKDPF EIKEKSIEDI
VFEKFQPYIN WSIDKLCEHF SINKGEKGLN YRIASAILNL KGKTTKSKPF PEVEEFEKSS
IVVKTVHFNK KNVNKESMSF GAFKFEELAN EEWEDSEGYP SAQWRNFLLE TRFLFFVVKE
DEDGVDIFKG IKFFSMPEED INGPVKRMWD DTVKKLKEGV TLEAVPDKST KDGWRIKNNF
VDKSDDLICH VRPHTNNRDY RGGSNADKLP KKINWINRPD SDDYSDEWMT KQSFWINNDY
IKKQVEDLL
