ID   PIMT_PHOLL              Reviewed;         208 AA.
AC   Q7N8K3;
DT   09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   16-JUN-2009, entry version 34.
DE   RecName: Full=Protein-L-isoaspartate O-methyltransferase;
DE            EC=2.1.1.77;
DE   AltName: Full=Protein-beta-aspartate methyltransferase;
DE            Short=PIMT;
DE   AltName: Full=Protein L-isoaspartyl methyltransferase;
DE   AltName: Full=L-isoaspartyl protein carboxyl methyltransferase;
GN   Name=pcm; OrderedLocusNames=plu0717;
OS   Photorhabdus luminescens subsp. laumondii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Photorhabdus.
OX   NCBI_TaxID=141679;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TT01;
RX   MEDLINE=22957627; PubMed=14528314; DOI=10.1038/nbt886;
RA   Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA   Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA   Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S.,
RA   Medigue C., Lanois A., Powell K., Siguier P., Vincent R., Wingate V.,
RA   Zouine M., Glaser P., Boemare N., Danchin A., Kunst F.;
RT   "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT   luminescens.";
RL   Nat. Biotechnol. 21:1307-1313(2003).
CC   -!- FUNCTION: Catalyzes the methyl esterification of L-isoaspartyl
CC       residues in peptides and proteins that result from spontaneous
CC       decomposition of normal L-aspartyl and L-asparaginyl residues. It
CC       plays a role in the repair and/or degradation of damaged proteins
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + protein L-
CC       isoaspartate = S-adenosyl-L-homocysteine + protein L-isoaspartate
CC       alpha-methyl ester.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the L-isoaspartyl/D-aspartyl protein
CC       methyltransferase family.
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DR   EMBL; BX571861; CAE13012.1; -; Genomic_DNA.
DR   RefSeq; NP_928062.1; -.
DR   GeneID; 2800680; -.
DR   GenomeReviews; BX470251_GR; plu0717.
DR   KEGG; plu:plu0717; -.
DR   NMPDR; fig|243265.1.peg.686; -.
DR   PhotoList; plu0717; -.
DR   HOGENOM; Q7N8K3; -.
DR   OMA; Q7N8K3; KELNYAN.
DR   BioCyc; PLUM243265:PLU0717-MON; -.
DR   BRENDA; 2.1.1.77; 308689.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-meth...; IEA:HAMAP.
DR   GO; GO:0006464; P:protein modification process; IEA:HAMAP.
DR   GO; GO:0030091; P:protein repair; IEA:HAMAP.
DR   HAMAP; MF_00090; -; 1.
DR   InterPro; IPR000682; PCMT.
DR   PANTHER; PTHR11579; PCMT; 1.
DR   Pfam; PF01135; PCMT; 1.
DR   TIGRFAMs; TIGR00080; pimt; 1.
DR   PROSITE; PS01279; PCMT; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Methyltransferase;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    208       Protein-L-isoaspartate O-
FT                                methyltransferase.
FT                                /FTId=PRO_0000111895.
FT   ACT_SITE     59     59       By similarity.
SQ   SEQUENCE   208 AA;  23157 MW;  5223D7B1A6FB66A4 CRC64;
     MLSRAMKNLL TQLRQQGIED ERLLAAISAV PRERFVDEAL AHKAYENTAL PIGYGQTISQ
     PYIVARMTEL LQLTPDAKIL EIGTGSGYQT AILAHLVKHV FSVERIKGLQ WQAKRRLKQL
     DLHNVSTRHG DGWQGWPSRG LFDAIIVTAA PPYIPQELML QLTDGGVMVL PVGEHTQILK
     SVKRHGNGFH SEVIEAVRFV PLVQGELA
//