Y133_MYCPN
ID Y133_MYCPN Reviewed; 301 AA.
AC P75265;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Uncharacterized lipoprotein MG186 homolog;
DE Flags: Precursor;
GN OrderedLocusNames=MPN_133; ORFNames=E07_orf301, MP021;
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 IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 29342 / M129;
RX PubMed=11271496;
RX DOI=10.1002/1522-2683(200011)21:17<3765::aid-elps3765>3.0.co;2-6;
RA Regula J.T., Ueberle B., Boguth G., Goerg A., Schnoelzer M., Herrmann R.,
RA Frank R.;
RT "Towards a two-dimensional proteome map of Mycoplasma pneumoniae.";
RL Electrophoresis 21:3765-3780(2000).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
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DR EMBL; U00089; AAB95669.1; -; Genomic_DNA.
DR PIR; S73347; S73347.
DR RefSeq; NP_109821.1; NC_000912.1.
DR RefSeq; WP_010874490.1; NC_000912.1.
DR AlphaFoldDB; P75265; -.
DR IntAct; P75265; 1.
DR STRING; 272634.MPN_133; -.
DR EnsemblBacteria; AAB95669; AAB95669; MPN_133.
DR GeneID; 66609217; -.
DR KEGG; mpn:MPN_133; -.
DR PATRIC; fig|272634.6.peg.147; -.
DR HOGENOM; CLU_972608_0_0_14; -.
DR OMA; NAKINIW; -.
DR BioCyc; MPNE272634:G1GJ3-225-MON; -.
DR Proteomes; UP000000808; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR Gene3D; 2.40.50.90; -; 1.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR016071; Staphylococal_nuclease_OB-fold.
DR SMART; SM00318; SNc; 1.
DR SUPFAM; SSF50199; SSF50199; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS50830; TNASE_3; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Endonuclease; Hydrolase; Lipoprotein; Membrane; Nuclease;
KW Palmitate; Reference proteome; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 27..301
FT /note="Uncharacterized lipoprotein MG186 homolog"
FT /id="PRO_0000034399"
FT DOMAIN 46..243
FT /note="TNase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT REGION 64..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 27
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 27
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 301 AA; 33218 MW; 153C8A774CB3AEFB CRC64;
MKGFSCSRPG YLTGLLLLAV APILTACTRD YTTKNEFQLT TAQQAKLKPA TIEYWRDGDT
PEINYASEER RKEAEQKSKE NAKKEDKKEE KKTEDSQDSS SASTQVRSSK HGLRIYGIDT
PEKHVSSKGD STGDEKIEAE KASNYAEKLI PKGSTVWVWS LNTYSYDREV GALFFKSNPK
QTFFQSFEVA MVEAGHAIPI AGTGLNLIAD PELSADDPLS VIGLQLANAA NKAYNAKINI
WSHDTDGYRS LTAVYKLRGA DISWTRFLDE ANGYSSASAG TGASLYQLWD QRQAKLAQKG
S