ID   PIMT_HELPJ              Reviewed;         209 AA.
AC   Q9ZKC2;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Protein-L-isoaspartate O-methyltransferase;
DE            EC=2.1.1.77;
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=jhp_1017;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
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 (By similarity).
CC       {ECO:0000250}.
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   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. L-
CC       isoaspartyl/D-aspartyl protein methyltransferase family. {ECO:0000305}.
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DR   EMBL; AE001439; AAD06603.1; -; Genomic_DNA.
DR   PIR; D71858; D71858.
DR   RefSeq; WP_001084537.1; NZ_CP011330.1.
DR   AlphaFoldDB; Q9ZKC2; -.
DR   SMR; Q9ZKC2; -.
DR   STRING; 85963.jhp_1017; -.
DR   EnsemblBacteria; AAD06603; AAD06603; jhp_1017.
DR   KEGG; hpj:jhp_1017; -.
DR   PATRIC; fig|85963.30.peg.1573; -.
DR   eggNOG; COG2518; Bacteria.
DR   OMA; DGNKGWE; -.
DR   Proteomes; UP000000804; 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..209
FT                   /note="Protein-L-isoaspartate O-methyltransferase"
FT                   /id="PRO_0000111893"
FT   ACT_SITE        59
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   209 AA;  23919 MW;  C681649134A96946 CRC64;
     MNSIKNHLMC EEIHKRFNLH PKVREAMESI EREVFVPAPF KHFAYTLNAL SMQAQQYISS
     PLTVAKMTQY LEIDHVDSVL EIGCGSGYQA AVLSQIFRRV FSIERIESLY IEARLRLKTL
     GLDNVHVKFA DGNKGWERYA PYDRILFSAC AKNIPQALID QLEEGGILVA PIQENNEQVI
     KRFVKQNNAL RVQKVLEKCL FVPVVDGVQ