(data stored in ACNUC7421 zone)

SWISSPROT: A0A0H2ZKB0_PSEAB

ID   A0A0H2ZKB0_PSEAB        Unreviewed;       280 AA.
AC   A0A0H2ZKB0;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   07-JUN-2017, entry version 10.
DE   RecName: Full=Chemotaxis protein methyltransferase {ECO:0000256|PIRNR:PIRNR000410};
DE            EC=2.1.1.80 {ECO:0000256|PIRNR:PIRNR000410};
GN   Name=cheR {ECO:0000313|EMBL:ABJ15132.1};
GN   OrderedLocusNames=PA14_02200 {ECO:0000313|EMBL:ABJ15132.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ15132.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ15132.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ15132.1,
RC   ECO:0000313|Proteomes:UP000000653};
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
CC   -!- FUNCTION: Methylation of the membrane-bound methyl-accepting
CC       chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester
CC       residues in MCP. {ECO:0000256|PIRNR:PIRNR000410}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + protein L-glutamate
CC       = S-adenosyl-L-homocysteine + protein L-glutamate methyl ester.
CC       {ECO:0000256|PIRNR:PIRNR000410}.
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; CP000438; ABJ15132.1; -; Genomic_DNA.
DR   RefSeq; WP_003083930.1; NC_008463.1.
DR   EnsemblBacteria; ABJ15132; ABJ15132; PA14_02200.
DR   KEGG; pau:PA14_02200; -.
DR   KO; K00575; -.
DR   OMA; FREEHHF; -.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0008983; F:protein-glutamate O-methyltransferase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.10.155.10; -; 1.
DR   InterPro; IPR026024; Chemotaxis_MeTrfase_CheR.
DR   InterPro; IPR022642; CheR_C.
DR   InterPro; IPR000780; CheR_MeTrfase.
DR   InterPro; IPR022641; CheR_N.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   Pfam; PF01739; CheR; 1.
DR   Pfam; PF03705; CheR_N; 1.
DR   PIRSF; PIRSF000410; CheR; 1.
DR   PRINTS; PR00996; CHERMTFRASE.
DR   SMART; SM00138; MeTrc; 1.
DR   SUPFAM; SSF47757; SSF47757; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS50123; CHER; 1.
PE   4: Predicted;
DR   PRODOM; A0A0H2ZKB0.
DR   SWISS-2DPAGE; A0A0H2ZKB0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000653};
KW   Methyltransferase {ECO:0000256|PIRNR:PIRNR000410,
KW   ECO:0000313|EMBL:ABJ15132.1};
KW   S-adenosyl-L-methionine {ECO:0000256|PIRNR:PIRNR000410,
KW   ECO:0000256|PIRSR:PIRSR000410-1};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000410,
KW   ECO:0000313|EMBL:ABJ15132.1}.
FT   DOMAIN       10    280       CheR-type methyltransferase.
FT                                {ECO:0000259|PROSITE:PS50123}.
FT   REGION      208    209       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|PIRSR:PIRSR000410-1}.
FT   REGION      226    227       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|PIRSR:PIRSR000410-1}.
FT   BINDING      85     85       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PIRSR:PIRSR000410-1}.
FT   BINDING      87     87       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PIRSR:PIRSR000410-1}.
FT   BINDING      91     91       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PIRSR:PIRSR000410-1}.
FT   BINDING     125    125       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PIRSR:PIRSR000410-1}.
FT   BINDING     150    150       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PIRSR:PIRSR000410-1}.
SQ   SEQUENCE   280 AA;  32024 MW;  3D343E491DC157F2 CRC64;
     MPTSTPSPVF GNQEFHYTRE DFQQVRERLY RLTGISLAES KAQLVYSRLS RRLRLLRLGS
     FAEYFTHLDR EPGEQQLFVN ALTTNLTAFF RERHHFPLLA DLARRQLQRH RPLRIWSAAA
     STGEEPYSIA ITLVEALGSF DPPVKIVASD IDTGVLDCAR LGVYPLERLE QMPAPLKKRF
     FLRGTGPNAG KARVVEELRQ LVEFRQINLL EADWSIAGEL DAIFCRNVMI YFDKPTQTRL
     LERMVALLRP EGLFFAGHSE NFVHASHLVR PVGQTVYSPA
//

If you have problems or comments...

PBIL Back to PBIL home page