ID   PIMT_ESCF3              Reviewed;         208 AA.
AC   B7LWJ2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Protein-L-isoaspartate O-methyltransferase {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 {ECO:0000255|HAMAP-Rule:MF_00090};
DE   AltName: Full=Protein L-isoaspartyl methyltransferase {ECO:0000255|HAMAP-Rule:MF_00090};
DE   AltName: Full=Protein-beta-aspartate methyltransferase {ECO:0000255|HAMAP-Rule:MF_00090};
DE            Short=PIMT {ECO:0000255|HAMAP-Rule:MF_00090};
GN   Name=pcm {ECO:0000255|HAMAP-Rule:MF_00090}; OrderedLocusNames=EFER_0325;
OS   Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS   14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 / JCM
RC   21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928158; CAQ87888.1; -; Genomic_DNA.
DR   RefSeq; WP_000254699.1; NC_011740.1.
DR   AlphaFoldDB; B7LWJ2; -.
DR   SMR; B7LWJ2; -.
DR   EnsemblBacteria; CAQ87888; CAQ87888; EFER_0325.
DR   GeneID; 60903513; -.
DR   GeneID; 66507314; -.
DR   KEGG; efe:EFER_0325; -.
DR   HOGENOM; CLU_055432_2_0_6; -.
DR   OMA; TISAIHM; -.
DR   OrthoDB; 1948290at2; -.
DR   BioCyc; EFER585054:EFER_RS01800-MON; -.
DR   Proteomes; UP000000745; 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; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..208
FT                   /note="Protein-L-isoaspartate O-methyltransferase"
FT                   /id="PRO_1000117208"
FT   ACT_SITE        59
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00090"
SQ   SEQUENCE   208 AA;  23272 MW;  63FBB9BD034A5D0D CRC64;
     MVSRRVQALL DQLRAQGIKD EQVLNALAAV PREKFIDEAF EQKAWDNIAL PIGQGQTISQ
     PYMVARMTEL LELTPQSRVL EIGTGSGYQT AILAHLVQHV CSVERIKGLQ WQARRRLKNL
     DLHNVSTRHG DGWQGWQARA PFDAIIVTAA PPEIPTALMT QLDEGGILVL PVGEEHQYLK
     RVRRRGGEFI IDTVEAVRFV PLVKGELA