ID   A0A022M735_9ACTN        Unreviewed;       931 AA.
AC   A0A022M735;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Penicillin acylase {ECO:0000313|EMBL:EYT78362.1};
GN   ORFNames=CF54_37625 {ECO:0000313|EMBL:EYT78362.1};
OS   Streptomyces sp. Tu 6176.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1470557 {ECO:0000313|EMBL:EYT78362.1, ECO:0000313|Proteomes:UP000020060};
RN   [1] {ECO:0000313|EMBL:EYT78362.1, ECO:0000313|Proteomes:UP000020060}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tu 6176 {ECO:0000313|EMBL:EYT78362.1,
RC   ECO:0000313|Proteomes:UP000020060};
RA   Olano C., Cano-Prieto C., Mendez C., Salas J.A.;
RT   "Draft genome sequence of Streptomyces sp. Tu 6176, producer of the
RT   cytotoxic benzoxazol nataxazol.";
RL   Submitted (MAR-2014) 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:EYT78362.1}.
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DR   EMBL; JFJQ01001178; EYT78362.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A022M735; -.
DR   MEROPS; S45.001; -.
DR   HOGENOM; CLU_311672_0_0_11; -.
DR   OrthoDB; 5240333at2; -.
DR   Proteomes; UP000020060; 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   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 2.
DR   Gene3D; 1.10.439.10; Penicillin Amidohydrolase, domain 1; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR023343; Penicillin_amidase_dom1.
DR   InterPro; IPR002692; S45.
DR   PANTHER; PTHR34218:SF4; ACYL-HOMOSERINE LACTONE ACYLASE QUIP; 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   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..44
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           45..931
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001505752"
SQ   SEQUENCE   931 AA;  99074 MW;  0DC4C05E294A4308 CRC64;
     MPRRTPLSAL DRMRTPRRFP GFLKTASVCV LIAGLLSPFS QAVAASGTPK AAAADDYCGG
     QCSDILPPGE NGNATLAQIL LNQAFGTQPG HAEDQLGPYA NLAKGYPALT TDKINTFFND
     ASFGVPSGQV ASSEKPAGRG DVTIVRDKKT GVPHITGTTR YGTEFGAGYA AAEDRLWLMD
     VFRHVGRGQL TSFAGGAPAN QGLEQQFYRN APYTEADLQA QIDTAVAKNG ERGQQALADV
     NAYLAGINAY IDASDPGRYF PGEYVLTGHK DAITNAGTID HFKVTDMVAL ASVVGSLFGA
     GGGGEVNNAL SLLEAQAKYG VAEGTRVWES FRERNDPEAV LTLHDGQSFP YAAKPASAQG
     EALPDAGSVT AEPLLYDRTG SAKSQAATGT ADTVAKSALS SARRGMSNAL VVSGAHTASG
     HPVAVFGPQT GYFAPQLLLL QEIQGPGISA RGASFAGLSM YVELGRGQDY SWSATTSGQD
     IIDTYAVELC QDDHHYLYHG TCTAMEQVQQ ANAWKPTVAD GTAAGSYTMR VWRTRYGPVQ
     YRATVGGKKV AYTTLRSSYL HEADSIIGFQ MLNDPDYVKG PQDFQKAAQH INFTFNWFYA
     DSRHTAYYNS GDNPVRAAGV DAEFPVWAQP AYEWRGWDPA ANTADYTAPA AHPNSVDQDY
     YISWNNKQAE DYAAAPWGEG SVHRGNLLED RVKKLVAAGG VTRTALTQAM ADAAVADLRA
     EDVLPKLLKV IDSAPVTDTA AAAAVDKLRA WLTAGAHRTE TSAGSQKYAD ADAVRILDAW
     WPLLVKAEFE PGLGSALYTA FGANLPVDEA PSAGHGPTGS HAGSAFQYGW WSYVDKDIRA
     VLGEQVNGPL AQKYCGAGSL TACRDTLLGT LKQAAGMTAA QVYPGDDQCS AGDQWCADSI
     AQRALGGIKH GRISWQNRPT YQQVVEYTSH R
//