T1SX_MYCGE
ID T1SX_MYCGE Reviewed; 383 AA.
AC Q49434;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Putative type I specificity subunit S.MgeORF438P {ECO:0000303|PubMed:12654995};
DE Short=S protein;
DE Short=S.MgeORF438P {ECO:0000303|PubMed:12654995};
DE AltName: Full=Putative type-1 restriction enzyme specificity subunit MG438;
GN OrderedLocusNames=MG438;
OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS (Mycoplasmoides genitalium).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=243273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT "The minimal gene complement of Mycoplasma genitalium.";
RL Science 270:397-403(1995).
RN [2]
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 [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=16407165; DOI=10.1073/pnas.0510013103;
RA Glass J.I., Assad-Garcia N., Alperovich N., Yooseph S., Lewis M.R.,
RA Maruf M., Hutchison C.A. III, Smith H.O., Venter J.C.;
RT "Essential genes of a minimal bacterium.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:425-430(2006).
RN [4] {ECO:0007744|PDB:1YDX}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS), AND DOMAIN.
RX PubMed=16038930; DOI=10.1016/j.jmb.2005.06.050;
RA Calisto B.M., Pich O.Q., Pinol J., Fita I., Querol E., Carpena X.;
RT "Crystal structure of a putative type I restriction-modification S subunit
RT from Mycoplasma genitalium.";
RL J. Mol. Biol. 351:749-762(2005).
CC -!- FUNCTION: The specificity (S) subunit of a type I restriction enzyme;
CC this subunit dictates DNA sequence specificity. This bacterium does not
CC encode the associated endonuclease or methylase subunits.
CC {ECO:0000269|PubMed:7569993, ECO:0000303|PubMed:12654995}.
CC -!- DOMAIN: Contains two target DNA recognition domains (TRD), each
CC specifying recognition of one of the two defined components of the
CC target sequence (Probable). The TDRs show high structural similarity
CC and each forms a globular structure. The two TDRs are separated by 2
CC long, conserved antiparallel helices that form a coiled coil structure
CC (PubMed:16038930). {ECO:0000269|PubMed:16038930,
CC ECO:0000305|PubMed:16038930}.
CC -!- DISRUPTION PHENOTYPE: Not essential, it can be deleted.
CC {ECO:0000269|PubMed:16407165}.
CC -!- SIMILARITY: Belongs to the type-I restriction system S methylase
CC family. {ECO:0000305}.
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DR EMBL; L43967; AAC72457.1; -; Genomic_DNA.
DR PIR; D64248; D64248.
DR RefSeq; WP_009885596.1; NZ_AAGX01000001.1.
DR PDB; 1YDX; X-ray; 2.30 A; A=1-383.
DR PDBsum; 1YDX; -.
DR AlphaFoldDB; Q49434; -.
DR SMR; Q49434; -.
DR STRING; 243273.MG_438; -.
DR REBASE; 3674; S.MgeORF438P.
DR EnsemblBacteria; AAC72457; AAC72457; MG_438.
DR KEGG; mge:MG_438; -.
DR eggNOG; COG0732; Bacteria.
DR HOGENOM; CLU_721242_0_0_14; -.
DR OMA; KFAYYAL; -.
DR OrthoDB; 827072at2; -.
DR BioCyc; MGEN243273:G1GJ2-531-MON; -.
DR EvolutionaryTrace; Q49434; -.
DR PRO; PR:Q49434; -.
DR Proteomes; UP000000807; 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 3D-structure; Coiled coil; DNA-binding; Reference proteome;
KW Restriction system.
FT CHAIN 1..383
FT /note="Putative type I specificity subunit S.MgeORF438P"
FT /id="PRO_0000198042"
FT REGION 1..142
FT /note="TRD1"
FT /evidence="ECO:0000269|PubMed:16038930"
FT REGION 143..182
FT /note="Conserved region 1"
FT /evidence="ECO:0000269|PubMed:16038930"
FT REGION 183..330
FT /note="TRD2"
FT /evidence="ECO:0000269|PubMed:16038930"
FT REGION 331..370
FT /note="Conserved region 2"
FT /evidence="ECO:0000269|PubMed:16038930"
FT COILED 143..182
FT /evidence="ECO:0000269|PubMed:16038930,
FT ECO:0007744|PDB:1YDX"
FT COILED 331..370
FT /evidence="ECO:0000269|PubMed:16038930,
FT ECO:0007744|PDB:1YDX"
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:1YDX"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:1YDX"
FT HELIX 18..21
FT /evidence="ECO:0007829|PDB:1YDX"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:1YDX"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:1YDX"
FT STRAND 40..49
FT /evidence="ECO:0007829|PDB:1YDX"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:1YDX"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:1YDX"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:1YDX"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:1YDX"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:1YDX"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:1YDX"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:1YDX"
FT HELIX 101..109
FT /evidence="ECO:0007829|PDB:1YDX"
FT HELIX 112..116
FT /evidence="ECO:0007829|PDB:1YDX"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:1YDX"
FT HELIX 129..134
FT /evidence="ECO:0007829|PDB:1YDX"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:1YDX"
FT HELIX 143..182
FT /evidence="ECO:0007829|PDB:1YDX"
FT HELIX 186..191
FT /evidence="ECO:0007829|PDB:1YDX"
FT HELIX 196..200
FT /evidence="ECO:0007829|PDB:1YDX"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:1YDX"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:1YDX"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:1YDX"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:1YDX"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:1YDX"
FT STRAND 228..237
FT /evidence="ECO:0007829|PDB:1YDX"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:1YDX"
FT STRAND 249..255
FT /evidence="ECO:0007829|PDB:1YDX"
FT TURN 259..262
FT /evidence="ECO:0007829|PDB:1YDX"
FT STRAND 264..269
FT /evidence="ECO:0007829|PDB:1YDX"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:1YDX"
FT STRAND 277..284
FT /evidence="ECO:0007829|PDB:1YDX"
FT HELIX 289..310
FT /evidence="ECO:0007829|PDB:1YDX"
FT HELIX 317..321
FT /evidence="ECO:0007829|PDB:1YDX"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:1YDX"
FT HELIX 331..369
FT /evidence="ECO:0007829|PDB:1YDX"
SQ SEQUENCE 383 AA; 44111 MW; 38A8341227AEEC65 CRC64;
MTPKLKLNNN INWTKRTIDS LFDLKKGEML EKELITPEGK YEYFNGGVKN SGRTDKFNTF
KNTISVIVGG SCGYVRLADK NFFCGQSNCT LNLLDPLELD LKFAYYALKS QQERIEALAF
GTTIQNIRIS DLKELEIPFT SNKNEQHAIA NTLSVFDERL ENLASLIEIN RKLRDEYAHK
LFSLDEAFLS HWKLEALQSQ MHEITLGEIF NFKSGKYLKS EERLEEGKFP YYGAGIDNTG
FVAEPNTEKD TISIISNGYS LGNIRYHEIP WFNGTGSIAL EPMNNEIYVP FFYCALKYLQ
KDIKERMKSD DSPFLSLKLA GEIKVPYVKS FQLQRKAGKI VFLLDQKLDQ YKKELSSLTV
IRDTLLKKLF PDMTERTKSI KDY
