ID   PIMT_SHIFL              Reviewed;         208 AA.
AC   Q83JY3;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 47.
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=SF2766, S2959;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   MEDLINE=22272406; PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H.,
RA   Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J.,
RA   Sun L., Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S.,
RA   Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y.,
RA   Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   MEDLINE=22590274; PubMed=12704152;
RX   DOI=10.1128/IAI.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W.,
RA   Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A.,
RA   Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S.,
RA   Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella
RT   flexneri serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(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   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the L-isoaspartyl/D-aspartyl protein
CC       methyltransferase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AE005674; AAN44255.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP18081.1; -; Genomic_DNA.
DR   RefSeq; NP_708548.1; -.
DR   RefSeq; NP_838271.1; -.
DR   HSSP; Q8TZR3; 1JG1.
DR   GeneID; 1025767; -.
DR   GeneID; 1079224; -.
DR   GenomeReviews; AE005674_GR; SF2766.
DR   GenomeReviews; AE014073_GR; S2959.
DR   KEGG; sfl:SF2766; -.
DR   KEGG; sfx:S2959; -.
DR   HOGENOM; Q83JY3; -.
DR   OMA; Q83JY3; KELNYAN.
DR   BioCyc; SFLE198214:AAN44255.1-MON; -.
DR   BRENDA; 2.1.1.77; 189495.
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   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    208       Protein-L-isoaspartate O-
FT                                methyltransferase.
FT                                /FTId=PRO_0000111904.
FT   ACT_SITE     59     59       By similarity.
FT   CONFLICT     82     82       T -> I (in Ref. 2; AAP18081).
SQ   SEQUENCE   208 AA;  23246 MW;  AE51795664D7ADE8 CRC64;
     MVSRRVQALL DQLRAQGIQD EQVLNALAAV PREKFVDEAF EQKAWDNIAL PIGQGQTISQ
     PYMVARMTEL LELTPQSRVL ETGTGSGYQT AILAHLVQHV CSVERIKGLQ WQARRRLKNL
     DLHNVSTRHG DGWQGWQARA PFDAIIVTAA PPEIPTALMT QLDEGGILVL PVGEEHQYLK
     RVRRRGGEFI IDTVEAVRFV PLVKGELA
//