ID   A0A0M8SXB0_9ACTN        Unreviewed;       804 AA.
AC   A0A0M8SXB0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Penicillin amidase {ECO:0000313|EMBL:KOU46540.1};
GN   ORFNames=ADK56_29810 {ECO:0000313|EMBL:KOU46540.1};
OS   Streptomyces sp. MMG1522.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1415545 {ECO:0000313|EMBL:KOU46540.1, ECO:0000313|Proteomes:UP000037713};
RN   [1] {ECO:0000313|EMBL:KOU46540.1, ECO:0000313|Proteomes:UP000037713}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MMG1522 {ECO:0000313|EMBL:KOU46540.1,
RC   ECO:0000313|Proteomes:UP000037713};
RA   Noorani M.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S45 family.
CC       {ECO:0000256|ARBA:ARBA00006586}.
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:KOU46540.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LGDF01000158; KOU46540.1; -; Genomic_DNA.
DR   RefSeq; WP_030292221.1; NZ_LGDF01000158.1.
DR   AlphaFoldDB; A0A0M8SXB0; -.
DR   PATRIC; fig|1415545.3.peg.6392; -.
DR   Proteomes; UP000037713; Unassembled WGS sequence.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:InterPro.
DR   CDD; cd01936; Ntn_CA; 1.
DR   Gene3D; 1.10.1400.10; -; 1.
DR   Gene3D; 2.30.120.10; -; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   Gene3D; 1.10.439.10; Penicillin Amidohydrolase, domain 1; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR043147; Penicillin_amidase_A-knob.
DR   InterPro; IPR023343; Penicillin_amidase_dom1.
DR   InterPro; IPR043146; Penicillin_amidase_N_B-knob.
DR   InterPro; IPR002692; S45.
DR   PANTHER; PTHR34218:SF3; ACYL-HOMOSERINE LACTONE ACYLASE PVDQ; 1.
DR   PANTHER; PTHR34218; PEPTIDASE S45 PENICILLIN AMIDASE; 1.
DR   Pfam; PF01804; Penicil_amidase; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..804
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005823048"
SQ   SEQUENCE   804 AA;  85595 MW;  0A35447117206631 CRC64;
     MRLRNRLRLL GVAGLALFTV SASLPPATAS GAGRERHPSG GGLSAVIRYT EYGIPHIVAK
     DYAQLGFGTG WAQAADQVCT LADGFLTVRG ERSRFFGPDA ATDYSLSSAA TNLSSDLYFR
     GVRDSGTVEK LLKVAAPAGP SRDVKETMRG FAAGYNAWIA QNRITDPACR DASWVRPVTA
     LDVAARGYAL AVLGGQGRGT DGITAAQPPT AAPPPAGVTP EEAASAAKRL LSAQNADMGS
     NAVAFDGSTT VNGRGLLLGN PHYPWQGGRR FWQSQQTIPG ELNVSGASLL GATTISIGHN
     ADVAWSHTVA TGVTLNLHQL TLDPADPTVY LVDGKPERMT KRTVSVPVKG AADVTRTQWW
     TRYGPVTTSM GAALPLPWTA TTAYALNDPN ATNLRMADTG LGFSKARGTK DVERSLHRNQ
     GMPWVNTIAA DRAGHSFFAQ SQVLPRITDD LAERCSTPLG RATYPASGLA VLDGSRKDCA
     LGSDRDAVQP GIFGPGRMPV LKNRPYVENS NDSAWLTNAD RPLTGYERVF GTIATPRSMR
     TRGAIEDVAS MADKGRLKVS DLQRQQFANR APAGELAASE VAKWCAALPG GTAVGTGGTP
     VDVSDACTVL RRWDRSVDSD SRGALLFDRF WRKASAVPAA ELWKTPFDPA DPVRTPRDLN
     TAAPGVGRAL ADAVAELRAA GIALDAPLGK HQFVVRDGKR LPIGGGTESL GIWNKTEPVW
     NAAGGGYTEV SSGSSYIQAV GWDDSRCPVA RTLLTYSQSE NPKSPHSSDQ TRLYAGERWV
     TSRFCEKDIA RSPDLRVVRV HERR
//