ID   PIMT_PSEAE              Reviewed;         211 AA.
AC   P45683; Q9HY06;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 2.
DT   03-AUG-2022, entry version 126.
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=PA3624;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 108-211.
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=7959068; DOI=10.1016/0378-1119(94)90862-1;
RA   Tanaka K., Takahashi H.;
RT   "Cloning, analysis and expression of an rpoS homologue gene from
RT   Pseudomonas aeruginosa PAO1.";
RL   Gene 150:81-85(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 (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; AE004091; AAG07012.1; -; Genomic_DNA.
DR   EMBL; D26134; BAA05129.1; -; Genomic_DNA.
DR   PIR; F83193; F83193.
DR   PIR; S55062; S55062.
DR   RefSeq; NP_252314.1; NC_002516.2.
DR   RefSeq; WP_003098558.1; NZ_QZGE01000001.1.
DR   AlphaFoldDB; P45683; -.
DR   SMR; P45683; -.
DR   STRING; 287.DR97_4315; -.
DR   PaxDb; P45683; -.
DR   PRIDE; P45683; -.
DR   DNASU; 880441; -.
DR   EnsemblBacteria; AAG07012; AAG07012; PA3624.
DR   GeneID; 880441; -.
DR   KEGG; pae:PA3624; -.
DR   PATRIC; fig|208964.12.peg.3793; -.
DR   PseudoCAP; PA3624; -.
DR   HOGENOM; CLU_055432_2_0_6; -.
DR   InParanoid; P45683; -.
DR   OMA; TISAIHM; -.
DR   PhylomeDB; P45683; -.
DR   BioCyc; PAER208964:G1FZ6-3694-MON; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; IBA:GO_Central.
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..211
FT                   /note="Protein-L-isoaspartate O-methyltransferase"
FT                   /id="PRO_0000111897"
FT   ACT_SITE        60
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   211 AA;  23407 MW;  2C3071381C00A5D9 CRC64;
     MTSQRTRERL IQRLYEEGLS NAHVLEVIRR TPRHLFVDEA LSHRAYEDTA LPIGHNQTIS
     QPFMVARMTE LLLAAGPLDK VMEIGTGSGY QTAVLAQLVE RVFSVERIQA LQDKAKERLA
     ELNLRNVVFR WGDGWEGWSA LAPYNGIIVT AAATEVPQSL LDQLAPGGRL VIPVGGGEVQ
     QLMLIVRTED GFSRQVLDSV RFVPLLNGPI A