PIMT_ECOLI
ID PIMT_ECOLI Reviewed; 208 AA.
AC P0A7A5; P24206; Q2MA86;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Protein-L-isoaspartate O-methyltransferase;
DE EC=2.1.1.77 {ECO:0000269|PubMed:1860862};
DE AltName: Full=L-isoaspartyl protein carboxyl methyltransferase;
DE AltName: Full=Protein L-isoaspartyl methyltransferase;
DE AltName: Full=Protein-beta-aspartate methyltransferase;
DE Short=PIMT;
GN Name=pcm; OrderedLocusNames=b2743, JW2713;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-40, AND CATALYTIC
RP ACTIVITY.
RC STRAIN=K12 / JA200;
RX PubMed=1860862; DOI=10.1016/s0021-9258(18)98723-5;
RA Fu J.C., Ding L., Clarke S.;
RT "Purification, gene cloning, and sequence analysis of an L-isoaspartyl
RT protein carboxyl methyltransferase from Escherichia coli.";
RL J. Biol. Chem. 266:14562-14572(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
RC STRAIN=MP180;
RX PubMed=7928962; DOI=10.1128/jb.176.19.6015-6022.1994;
RA Li C., Ichikawa J.K., Ravetto J.J., Kuo H.-C., Fu J.C., Clarke S.;
RT "A new gene involved in stationary-phase survival located at 59 minutes on
RT the Escherichia coli chromosome.";
RL J. Bacteriol. 176:6015-6022(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 191-208.
RC STRAIN=MP180;
RX PubMed=8132457; DOI=10.1128/jb.176.6.1630-1638.1994;
RA Ichikawa J.K., Li C., Fu J.C., Clarke S.;
RT "A gene at 59 minutes on the Escherichia coli chromosome encodes a
RT lipoprotein with unusual amino acid repeat sequences.";
RL J. Bacteriol. 176:1630-1638(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 193-208.
RC STRAIN=K12 / DH1 / ATCC 33849 / DSM 4235 / NCIB 12045;
RX PubMed=8208244; DOI=10.1007/bf00284200;
RA Takayanagi Y., Tanaka K., Takahashi H.;
RT "Structure of the 5' upstream region and the regulation of the rpoS gene of
RT Escherichia coli.";
RL Mol. Gen. Genet. 243:525-531(1994).
CC -!- FUNCTION: Catalyzes the methyl esterification of L-isoaspartyl residues
CC in peptides and proteins that result from spontaneous decomposition of
CC normal L-aspartyl and L-asparaginyl residues. It plays a role in the
CC repair and/or degradation of damaged proteins. This enzyme does not act
CC on D-aspartyl residues.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-L-isoaspartate + S-adenosyl-L-methionine =
CC [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:12705, Rhea:RHEA-COMP:12143, Rhea:RHEA-
CC COMP:12144, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:90596,
CC ChEBI:CHEBI:90598; EC=2.1.1.77;
CC Evidence={ECO:0000269|PubMed:1860862};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12706;
CC Evidence={ECO:0000269|PubMed:1860862};
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. L-
CC isoaspartyl/D-aspartyl protein methyltransferase family. {ECO:0000305}.
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DR EMBL; M63493; AAA24302.1; -; Genomic_DNA.
DR EMBL; U29579; AAA69253.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75785.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76820.1; -; Genomic_DNA.
DR EMBL; L07942; AAA79840.1; -; Genomic_DNA.
DR EMBL; L07869; AAA17874.1; -; Unassigned_DNA.
DR EMBL; D17549; BAA04486.1; -; Genomic_DNA.
DR PIR; JH0242; JH0242.
DR RefSeq; NP_417223.1; NC_000913.3.
DR RefSeq; WP_000254708.1; NZ_STEB01000027.1.
DR PDB; 3LBF; X-ray; 1.80 A; A/B/C/D=1-208.
DR PDBsum; 3LBF; -.
DR AlphaFoldDB; P0A7A5; -.
DR SMR; P0A7A5; -.
DR BioGRID; 4263145; 14.
DR BioGRID; 849321; 1.
DR IntAct; P0A7A5; 2.
DR STRING; 511145.b2743; -.
DR jPOST; P0A7A5; -.
DR PaxDb; P0A7A5; -.
DR PRIDE; P0A7A5; -.
DR EnsemblBacteria; AAC75785; AAC75785; b2743.
DR EnsemblBacteria; BAE76820; BAE76820; BAE76820.
DR GeneID; 66673383; -.
DR GeneID; 944923; -.
DR KEGG; ecj:JW2713; -.
DR KEGG; eco:b2743; -.
DR PATRIC; fig|1411691.4.peg.3997; -.
DR EchoBASE; EB0683; -.
DR eggNOG; COG2518; Bacteria.
DR HOGENOM; CLU_055432_2_0_6; -.
DR InParanoid; P0A7A5; -.
DR OMA; TISAIHM; -.
DR PhylomeDB; P0A7A5; -.
DR BioCyc; EcoCyc:EG10689-MON; -.
DR BioCyc; MetaCyc:EG10689-MON; -.
DR BRENDA; 2.1.1.77; 2026.
DR EvolutionaryTrace; P0A7A5; -.
DR PRO; PR:P0A7A5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoCyc.
DR GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; IDA:EcoCyc.
DR GO; GO:0030091; P:protein repair; IMP:EcoCyc.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_00090; PIMT; 1.
DR InterPro; IPR000682; PCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11579; PTHR11579; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00080; pimt; 1.
DR PROSITE; PS01279; PCMT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Methyltransferase;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1860862"
FT CHAIN 2..208
FT /note="Protein-L-isoaspartate O-methyltransferase"
FT /id="PRO_0000111886"
FT ACT_SITE 59
FT /evidence="ECO:0000250"
FT HELIX 4..15
FT /evidence="ECO:0007829|PDB:3LBF"
FT HELIX 21..29
FT /evidence="ECO:0007829|PDB:3LBF"
FT HELIX 32..35
FT /evidence="ECO:0007829|PDB:3LBF"
FT HELIX 38..43
FT /evidence="ECO:0007829|PDB:3LBF"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:3LBF"
FT HELIX 61..70
FT /evidence="ECO:0007829|PDB:3LBF"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:3LBF"
FT HELIX 88..96
FT /evidence="ECO:0007829|PDB:3LBF"
FT STRAND 97..106
FT /evidence="ECO:0007829|PDB:3LBF"
FT HELIX 107..119
FT /evidence="ECO:0007829|PDB:3LBF"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:3LBF"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:3LBF"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:3LBF"
FT STRAND 142..150
FT /evidence="ECO:0007829|PDB:3LBF"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:3LBF"
FT STRAND 162..172
FT /evidence="ECO:0007829|PDB:3LBF"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:3LBF"
FT STRAND 178..185
FT /evidence="ECO:0007829|PDB:3LBF"
FT STRAND 188..196
FT /evidence="ECO:0007829|PDB:3LBF"
SQ SEQUENCE 208 AA; 23258 MW; BFA179567527A118 CRC64;
MVSRRVQALL DQLRAQGIQD EQVLNALAAV PREKFVDEAF EQKAWDNIAL PIGQGQTISQ
PYMVARMTEL LELTPQSRVL EIGTGSGYQT AILAHLVQHV CSVERIKGLQ WQARRRLKNL
DLHNVSTRHG DGWQGWQARA PFDAIIVTAA PPEIPTALMT QLDEGGILVL PVGEEHQYLK
RVRRRGGEFI IDTVEAVRFV PLVKGELA
