ID   T1SD_MYCPN              Reviewed;         330 AA.
AC   P75435;
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=Type I restriction enzyme MpnII specificity subunit {ECO:0000305};
DE            Short=S protein;
DE   AltName: Full=Type I specificity subunit S.MpnII {ECO:0000303|PubMed:23300489};
DE            Short=S.MpnII {ECO:0000303|PubMed:23300489};
DE   AltName: Full=Type-1 restriction enzyme specificity subunit MpnII;
GN   OrderedLocusNames=MPN_343; ORFNames=H91_orf330, MP493;
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).
RN   [3]
RP   FUNCTION, GENOME METHYLATION, SUBUNIT, AND INDUCTION.
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=23300489; DOI=10.1371/journal.pgen.1003191;
RA   Lluch-Senar M., Luong K., Llorens-Rico V., Delgado J., Fang G., Spittle K.,
RA   Clark T.A., Schadt E., Turner S.W., Korlach J., Serrano L.;
RT   "Comprehensive methylome characterization of Mycoplasma genitalium and
RT   Mycoplasma pneumoniae at single-base resolution.";
RL   PLoS Genet. 9:e1003191-e1003191(2013).
CC   -!- FUNCTION: The specificity (S) subunit of a type I restriction enzyme;
CC       this subunit dictates DNA sequence specificity. The M and S subunits
CC       together form a methyltransferase (MTase) that probably methylates A-2
CC       on the top strand and A-3 on the bottom strand of the sequence 5'-
CC       GAN(7)TAY-3'. As the bacterial DNA is methylated on this sequence and
CC       this is the only type I methylase in the genome, it is probably
CC       responsible for all of the methylation on this site in the genome. The
CC       R subunit has multiple frameshifts and is probably not expressed in
CC       this bacteria. {ECO:0000305|PubMed:23300489}.
CC   -!- SUBUNIT: The methyltransferase is composed of M and S polypeptides.
CC       {ECO:0000305|PubMed:23300489}.
CC   -!- INDUCTION: Detected at low levels after 6 but not 96 hours growth (at
CC       protein level). {ECO:0000269|PubMed:23300489}.
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}.
CC   -!- SIMILARITY: Belongs to the type-I restriction system S methylase
CC       family. {ECO:0000305}.
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DR   EMBL; U00089; AAB96141.1; -; Genomic_DNA.
DR   PIR; S73819; S73819.
DR   AlphaFoldDB; P75435; -.
DR   SMR; P75435; -.
DR   IntAct; P75435; 1.
DR   REBASE; 6704; S.MpnII.
DR   EnsemblBacteria; AAB96141; AAB96141; MPN_343.
DR   KEGG; mpn:MPN_343; -.
DR   HOGENOM; CLU_021095_6_2_14; -.
DR   OMA; NACPIPN; -.
DR   PRO; PR:P75435; -.
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   1: Evidence at protein level;
KW   DNA-binding; Reference proteome; Restriction system.
FT   CHAIN           1..330
FT                   /note="Type I restriction enzyme MpnII specificity subunit"
FT                   /id="PRO_0000198047"
SQ   SEQUENCE   330 AA;  37222 MW;  85B577796FFB31CE CRC64;
     MEAPKFVNNA CPIPNLNLSR TEEIELDFPP LQIQQKIATI LDTFTELSAE LSAELSAELS
     AELSAELSAE LSAELSAELS AELSAELSAE LSAELSAELS AELSAELSAE LRERKKQYAF
     YRDYLLNQEN IRKIYGANIP FETFQVKDIC EIRRGRAITK AYIRNNPGEN PVYSAATTND
     GELGRIKDCD FDGEYITWTT NGYAGVVFYR NGKFNASQDC GVLKVKNKKI CTKFLSFLLK
     IEAPKFVHNL ASRPKLSQKV MAEIELSFPP LEIQEKIADI LFAFEKLCND LVEGIPAEIE
     LRKKQLDYYQ NFLFNWVQEQ KKNSLSTNLN