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Database: UniProt
Entry: H0E2E1_9ACTN
LinkDB: H0E2E1_9ACTN
Original site: H0E2E1_9ACTN 
ID   H0E2E1_9ACTN            Unreviewed;       611 AA.
AC   H0E2E1;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   03-MAY-2023, entry version 34.
DE   SubName: Full=Exoenzymes regulatory protein aepA {ECO:0000313|EMBL:EHN12161.1};
GN   ORFNames=PAI11_09540 {ECO:0000313|EMBL:EHN12161.1};
OS   Patulibacter medicamentivorans.
OC   Bacteria; Actinomycetota; Thermoleophilia; Solirubrobacterales;
OC   Patulibacteraceae; Patulibacter.
OX   NCBI_TaxID=1097667 {ECO:0000313|EMBL:EHN12161.1, ECO:0000313|Proteomes:UP000005143};
RN   [1] {ECO:0000313|EMBL:EHN12161.1, ECO:0000313|Proteomes:UP000005143}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=I11 {ECO:0000313|EMBL:EHN12161.1,
RC   ECO:0000313|Proteomes:UP000005143};
RX   PubMed=23212173; DOI=10.1007/s10532-012-9610-5;
RA   Almeida B., Kjeldal H., Lolas I., Knudsen A.D., Carvalho G., Nielsen K.L.,
RA   Barreto Crespo M.T., Stensballe A., Nielsen J.L.;
RT   "Quantitative proteomic analysis of ibuprofen-degrading Patulibacter sp.
RT   strain I11.";
RL   Biodegradation 24:615-630(2013).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHN12161.1}.
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DR   EMBL; AGUD01000043; EHN12161.1; -; Genomic_DNA.
DR   RefSeq; WP_007571485.1; NZ_AGUD01000043.1.
DR   AlphaFoldDB; H0E2E1; -.
DR   PATRIC; fig|1097667.3.peg.951; -.
DR   OrthoDB; 3238066at2; -.
DR   Proteomes; UP000005143; Unassembled WGS sequence.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   CDD; cd01300; YtcJ_like; 1.
DR   Gene3D; 3.10.310.70; -; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR   InterPro; IPR013108; Amidohydro_3.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR033932; YtcJ-like.
DR   PANTHER; PTHR22642; IMIDAZOLONEPROPIONASE; 1.
DR   PANTHER; PTHR22642:SF2; PROTEIN LONG AFTER FAR-RED 3; 1.
DR   Pfam; PF07969; Amidohydro_3; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000005143};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..611
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003531988"
FT   DOMAIN          77..578
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   611 AA;  65705 MW;  0232C425EE6C2276 CRC64;
     MSSRIWCSCG VLAALAAVVP AASASAVQPA DTVLRNGSVL TVDAHDRVAQ AVALRRGRIA
     FVGSDRAVRR YVGKRTKVVD LRGRTAMPGL VDGHAHPLAG GDILDDCDLG NGEATIPELQ
     AAIRACDAAT PAKDGDDWLQ VSNWNPVGVK PAGTVVSRHD LDAISTTRPI IVSASDGHND
     WVNSRALEIA GITDSTPNPS DGEIVRDPDG SARGLLKDGA GGLVTAKIPG KTLDDSLADA
     RRGQQALNAS GVTTAVDASA GESTLRTWST LARRGGLDLR LSSFLRIDNS QSPADAWSYA
     SGLSKRYAAP GLTIKGVKFF LDGVMEYPAQ TAALLQPYLV QRDGRWTPGT DRGDLYFAQK
     PLDALVALFD RKGWRIHMHA IGDRAVRTGL DAVAAARRAN HSSPRRLNAA IAHLQLVDPA
     DYGRFRKLGV FADMQLQWGN RDVWTEEALG PFLGRERHQR IYPAKSLIAA GAPFAQGSDW
     PVDALDPWLE LEVANTRTID PKRGALYRSR QGIPLRTAIR AHTIGAARQL GMQGRIGSLE
     VGKAADVIVL DRDLLRVPVT KVSDTRVLRT FLGGRTVYAD SKAGRATVRL AQERHEPNGR
     AHQHDRGREQ H
//
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