ID   AMSI_ERWAM              Reviewed;         144 AA.
AC   Q46630;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Probable low molecular weight protein-tyrosine-phosphatase AmsI;
DE            EC=3.1.3.48;
GN   Name=amsI;
OS   Erwinia amylovora (Fire blight bacteria).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=552;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=EA1/79;
RX   PubMed=7596293; DOI=10.1111/j.1365-2958.1995.tb02361.x;
RA   Bugert P., Geider K.;
RT   "Molecular analysis of the ams operon required for exopolysaccharide
RT   synthesis of Erwinia amylovora.";
RL   Mol. Microbiol. 15:917-933(1995).
CC   -!- FUNCTION: May function as a phosphatase required for amylovoran (an
CC       exopolysaccharide that functions as a virulence factor) production.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620; EC=3.1.3.48;
CC   -!- SIMILARITY: Belongs to the low molecular weight phosphotyrosine protein
CC       phosphatase family. {ECO:0000305}.
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DR   EMBL; X77921; CAA54881.1; -; Genomic_DNA.
DR   PIR; S61893; S52140.
DR   RefSeq; WP_004158327.1; NZ_RQKG01000006.1.
DR   PDB; 4D74; X-ray; 1.57 A; A=1-144.
DR   PDBsum; 4D74; -.
DR   AlphaFoldDB; Q46630; -.
DR   SMR; Q46630; -.
DR   GeneID; 8912405; -.
DR   OMA; AFFPQKA; -.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   InterPro; IPR023485; Ptyr_pPase.
DR   InterPro; IPR036196; Ptyr_pPase_sf.
DR   InterPro; IPR017867; Tyr_phospatase_low_mol_wt.
DR   Pfam; PF01451; LMWPc; 1.
DR   PRINTS; PR00719; LMWPTPASE.
DR   SMART; SM00226; LMWPc; 1.
DR   SUPFAM; SSF52788; SSF52788; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Exopolysaccharide synthesis; Hydrolase; Protein phosphatase;
KW   Virulence.
FT   CHAIN           1..144
FT                   /note="Probable low molecular weight protein-tyrosine-
FT                   phosphatase AmsI"
FT                   /id="PRO_0000046578"
FT   ACT_SITE        9
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P11064"
FT   ACT_SITE        15
FT                   /evidence="ECO:0000250|UniProtKB:P11064"
FT   ACT_SITE        115
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P11064"
FT   STRAND          4..14
FT                   /evidence="ECO:0007829|PDB:4D74"
FT   HELIX           15..26
FT                   /evidence="ECO:0007829|PDB:4D74"
FT   STRAND          30..36
FT                   /evidence="ECO:0007829|PDB:4D74"
FT   HELIX           47..55
FT                   /evidence="ECO:0007829|PDB:4D74"
FT   HELIX           70..75
FT                   /evidence="ECO:0007829|PDB:4D74"
FT   STRAND          77..83
FT                   /evidence="ECO:0007829|PDB:4D74"
FT   HELIX           85..93
FT                   /evidence="ECO:0007829|PDB:4D74"
FT   HELIX           95..100
FT                   /evidence="ECO:0007829|PDB:4D74"
FT   STRAND          101..103
FT                   /evidence="ECO:0007829|PDB:4D74"
FT   HELIX           121..143
FT                   /evidence="ECO:0007829|PDB:4D74"
SQ   SEQUENCE   144 AA;  15772 MW;  85B64E5EBC52961F CRC64;
     MINSILVVCI GNICRSPTGE RLLKAALPER KIASAGLKAM VGGSADETAS IVANEHGVSL
     QDHVAQQLTA DMCRDSDLIL VMEKKHIDLV CRINPSVRGK TMLFGHWINQ QEIADPYKKS
     RDAFEAVYGV LENAAQKWVN ALSR