ID   AEPA_PECCC              Reviewed;         465 AA.
AC   Q06555; Q53463;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Exoenzymes regulatory protein AepA;
DE   Flags: Precursor;
GN   Name=aepA;
OS   Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp.
OS   carotovora).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=71;
RX   PubMed=8324248; DOI=10.1094/mpmi-6-299;
RA   Liu Y., Murata H., Chatterjee A., Chatterjee A.K.;
RT   "Characterization of a novel regulatory gene aepA that controls
RT   extracellular enzyme production in the phytopathogenic bacterium Erwinia
RT   carotovora subsp. carotovora.";
RL   Mol. Plant Microbe Interact. 6:299-308(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
RC   STRAIN=71;
RX   PubMed=7944360; DOI=10.1128/aem.60.9.3150-3159.1994;
RA   Murata H., Chatterjee A., Liu Y., Chatterjee A.K.;
RT   "Regulation of the production of extracellular pectinase, cellulase, and
RT   protease in the soft rot bacterium Erwinia carotovora subsp. carotovora:
RT   evidence that aepH of E. carotovora subsp. carotovora 71 activates gene
RT   expression in E. carotovora subsp. carotovora, E. carotovora subsp.
RT   atroseptica, and Escherichia coli.";
RL   Appl. Environ. Microbiol. 60:3150-3159(1994).
CC   -!- FUNCTION: Involved in the control of extracellular enzymes production.
CC       Stimulates PEL, PEH, CEL, and PRT production.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       {ECO:0000305}.
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DR   EMBL; L13457; AAA71984.1; -; Unassigned_DNA.
DR   EMBL; S74077; AAB32244.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q06555; -.
DR   SMR; Q06555; -.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   Gene3D; 2.30.40.10; -; 1.
DR   InterPro; IPR013108; Amidohydro_3.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   Pfam; PF07969; Amidohydro_3; 1.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
PE   3: Inferred from homology;
KW   Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..465
FT                   /note="Exoenzymes regulatory protein AepA"
FT                   /id="PRO_0000020635"
SQ   SEQUENCE   465 AA;  50729 MW;  66B2BC7B45C3696F CRC64;
     MKFNVKMLSV TLGLFTSHAF AHTVYENARI YTVNDRQPTA SVLVVDQGKI VYVGGNDGAK
     PFKATATELV DLEGKTVLPG FIESHAHPAT VAVMEAGDFV YVDGARTLSQ ILSQLKAYLV
     AHPKANYLLA QGFNVASLGL PQGALPTAAD LDTVSESVPI VVYDSGMHAG WANSAALNVA
     HVDANTPDPI PGKHYFERDN KGNPTGFMHE SAMHNVVDAQ QFNAVENVAE KLQPILKTYH
     SLGFTAITDV GDTFSTTVAA IARLNEQGKL KVYYQRGYFY DAAKSTEQNI ASLKGLREKY
     HQGNLSINLY KLFMDGTIEM DSGAMYQPYP NGNVVEPFLS QKQINDNVAA ALKAGFSVHV
     HAIGDKAQQS ILDAFAANKK INPQLARVIA HNQVFEPQGV QKFAAMKDNL FLQTTPNWAV
     MYEKDETKTK IGQDAYHHQF LLGQAAREGV AVTSALTILR IPLMR