ID   T1SY_MYCPN              Reviewed;         145 AA.
AC   P75487;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Putative type I specificity subunit S.MpnORF289P C-terminus {ECO:0000303|PubMed:12654995};
DE            Short=S protein;
DE            Short=S.MpnORF289P C-terminus {ECO:0000303|PubMed:12654995};
DE   AltName: Full=Putative type-1 specificity subunit MPN_290;
DE   AltName: Full=S.MpnORFEAP;
GN   OrderedLocusNames=MPN_290; ORFNames=H10_orf145L, MP545;
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 C-terminal section of a specificity (S) subunit of a type
CC       I methyltransferase (MTase); this subunit dictates DNA sequence
CC       specificity. The single R subunit has multiple frameshifts and is
CC       probably not expressed. {ECO:0000303|PubMed:12654995,
CC       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; AAB96193.1; -; Genomic_DNA.
DR   PIR; S73871; S73871.
DR   RefSeq; NP_109978.1; NC_000912.1.
DR   AlphaFoldDB; P75487; -.
DR   SMR; P75487; -.
DR   STRING; 272634.MPN_290; -.
DR   REBASE; 6702; S.MpnORF289P.
DR   EnsemblBacteria; AAB96193; AAB96193; MPN_290.
DR   KEGG; mpn:MPN_290; -.
DR   PATRIC; fig|272634.6.peg.314; -.
DR   HOGENOM; CLU_021095_6_1_14; -.
DR   OMA; FLFNWIQ; -.
DR   BioCyc; MPNE272634:G1GJ3-457-MON; -.
DR   PRO; PR:P75487; -.
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; -; 1.
DR   InterPro; IPR000055; Restrct_endonuc_typeI_TRD.
DR   InterPro; IPR044946; Restrct_endonuc_typeI_TRD_sf.
DR   Pfam; PF01420; Methylase_S; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Reference proteome; Restriction system.
FT   CHAIN           1..145
FT                   /note="Putative type I specificity subunit S.MpnORF289P C-
FT                   terminus"
FT                   /id="PRO_0000198048"
SQ   SEQUENCE   145 AA;  16827 MW;  DABD6EA23F708DE4 CRC64;
     MVYSKTFRVE EKSITVSARG TIGVVFYRDF AYLPAVSLIC FVPKEEFDIR FLFHALRAIK
     FKKQGSATGQ LTVAQFKEYG IHVPSLKKQK EIAAILDPLY SFFTDLNEGL PAEIELRKKQ
     LDYYQNFLFN WIQKQKELVE QASTN