ID   PIMT2_PELPD             Reviewed;         225 AA.
AC   A1ASW6;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Protein-L-isoaspartate O-methyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_00090};
DE            EC=2.1.1.77 {ECO:0000255|HAMAP-Rule:MF_00090};
DE   AltName: Full=L-isoaspartyl protein carboxyl methyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_00090};
DE   AltName: Full=Protein L-isoaspartyl methyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_00090};
DE   AltName: Full=Protein-beta-aspartate methyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_00090};
DE            Short=PIMT 2 {ECO:0000255|HAMAP-Rule:MF_00090};
GN   Name=pcm2 {ECO:0000255|HAMAP-Rule:MF_00090}; OrderedLocusNames=Ppro_2838;
OS   Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Desulfuromonadaceae; Pelobacter.
OX   NCBI_TaxID=338966;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2379 / NBRC 103807 / OttBd1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Lovley D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Pelobacter propionicus DSM 2379.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000255|HAMAP-
CC       Rule:MF_00090}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00090};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00090}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. L-
CC       isoaspartyl/D-aspartyl protein methyltransferase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00090}.
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DR   EMBL; CP000482; ABL00437.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1ASW6; -.
DR   SMR; A1ASW6; -.
DR   STRING; 338966.Ppro_2838; -.
DR   EnsemblBacteria; ABL00437; ABL00437; Ppro_2838.
DR   KEGG; ppd:Ppro_2838; -.
DR   eggNOG; COG2518; Bacteria.
DR   HOGENOM; CLU_055432_2_0_7; -.
DR   OMA; FDRILIW; -.
DR   Proteomes; UP000006732; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030091; P:protein repair; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..225
FT                   /note="Protein-L-isoaspartate O-methyltransferase 2"
FT                   /id="PRO_0000351897"
FT   ACT_SITE        73
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00090"
SQ   SEQUENCE   225 AA;  25003 MW;  81FF49AA01D2C202 CRC64;
     MRYRCPMNCP SLRNQEYRRE IMISEQLMGR GIRDPAVLAA MRQVPREAFV DQGMRELAYE
     DHPLPIDGGQ TISQPYIVAY MTEALELSSS DRVLEIGTGS GYAAAVLSRI VHTVYSVERL
     EELARGARQR LESLGYNNVE VFEGDGTLGW PEHAPYDAIV VTAGAPAVPK PLLRQLVVGG
     RLVIPVGASS FLQNLIRVRR QGEDDYRSEE LCGVRFVPLV GAEGW