T1SZ_MYCPN
ID T1SZ_MYCPN Reviewed; 187 AA.
AC P75488;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Putative type I specificity subunit S.MpnORF289P N-terminus {ECO:0000303|PubMed:12654995};
DE Short=S protein;
DE Short=S.MpnORF289P N-terminus {ECO:0000303|PubMed:12654995};
DE AltName: Full=Putative type-1 specificity subunit MPN_289;
DE AltName: Full=S.MpnORFEBP;
GN OrderedLocusNames=MPN_289; ORFNames=H10_orf187V, MP546;
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 N-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; AAB96194.1; -; Genomic_DNA.
DR PIR; S73872; S73872.
DR RefSeq; NP_109977.1; NC_000912.1.
DR RefSeq; WP_010874646.1; NC_000912.1.
DR AlphaFoldDB; P75488; -.
DR SMR; P75488; -.
DR IntAct; P75488; 1.
DR STRING; 272634.MPN_289; -.
DR EnsemblBacteria; AAB96194; AAB96194; MPN_289.
DR KEGG; mpn:MPN_289; -.
DR PATRIC; fig|272634.6.peg.313; -.
DR HOGENOM; CLU_021095_6_2_14; -.
DR OMA; GQFNATN; -.
DR BioCyc; MPNE272634:G1GJ3-456-MON; -.
DR PRO; PR:P75488; -.
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..187
FT /note="Putative type I specificity subunit S.MpnORF289P N-
FT terminus"
FT /id="PRO_0000198049"
SQ SEQUENCE 187 AA; 21289 MW; 610CCDE0592453B6 CRC64;
MQIKTYKIKD ICDIKRGRVI SKLYIKNNPG EFPVYSSATV NNGEIGRIKD CDLKGEYVTW
TTDGAQAGSV FYRNGQFNAT NVCGILKVNN DEIYPKFLAY ALRLKAPKFV NYACPIPKLM
QGTLAEIELD FTSKKIQEKI ATILDTFTEL SAELSAELSA ELSAELRERK KQYVFYSDYL
LNPKNWK