T1SA_MYCPN
ID T1SA_MYCPN Reviewed; 335 AA.
AC P75604;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Putative type I specificity subunit S.MpnORF89P {ECO:0000303|PubMed:12654995};
DE Short=S protein;
DE Short=S.MpnORF89P {ECO:0000303|PubMed:12654995};
DE AltName: Full=Putative type-1 specificity subunit MPN_089;
DE AltName: Full=S.MpnORFAP;
GN OrderedLocusNames=MPN_089; ORFNames=MP066, R02_orf335;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
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).
CC -!- FUNCTION: The specificity (S) subunit of a type I methyltransferase
CC (MTase); this subunit dictates DNA sequence specificity. The single R
CC subunit has multiple frameshifts and is probably not expressed.
CC {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:8948633}.
CC -!- SUBUNIT: The methyltransferase is composed of M and S polypeptides.
CC {ECO:0000250|UniProtKB:P05719}.
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 -!- SIMILARITY: Belongs to the type-I restriction system S methylase
CC family. {ECO:0000305}.
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DR EMBL; U00089; AAB95713.1; -; Genomic_DNA.
DR PIR; S73392; S73392.
DR RefSeq; NP_109777.1; NC_000912.1.
DR AlphaFoldDB; P75604; -.
DR SMR; P75604; -.
DR IntAct; P75604; 3.
DR STRING; 272634.MPN_089; -.
DR REBASE; 391273; S.Eco6193ORF160P.
DR REBASE; 6708; S.MpnORF89P.
DR EnsemblBacteria; AAB95713; AAB95713; MPN_089.
DR KEGG; mpn:MPN_089; -.
DR PATRIC; fig|272634.6.peg.88; -.
DR HOGENOM; CLU_021095_6_0_14; -.
DR OMA; ASSNCGI; -.
DR BioCyc; MPNE272634:G1GJ3-143-MON; -.
DR PRO; PR:P75604; -.
DR Proteomes; UP000000808; 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 3: Inferred from homology;
KW DNA-binding; Reference proteome; Restriction system.
FT CHAIN 1..335
FT /note="Putative type I specificity subunit S.MpnORF89P"
FT /id="PRO_0000198044"
SQ SEQUENCE 335 AA; 38602 MW; 4657C6877C29354C CRC64;
MGRIKTYDFD GEYVTWTTRW SYAGSIYYRN GKFSASSNCG ILKVLNKEIN PKFLAYALKK
EAKKFVNTTS AIPILRTQKV VEIPIDFPPL QIQEKIATIL DTFTELSAEL SAELSAELSA
ELSAELRERK KQYAFYRDYL LNLKNWKEEN KYYKLGEIAQ KVLVGGEKPA DFSKEKNEVY
KYPILSNNSK AEEFLVYSKT FRVEEKSITV SARGTIGAVF YRDFAYLPAV SLICFVPKEE
FDIRFLFHAL RAIKFKKQGS ATGQLTVAQF KEYGIHVPSL KKQKEIAAIL DPLYSFFTDL
NEGIPAEIEL RKKQLDYYQN FLFNWVQNQK AASIL