ID A0A0M8Z2U3_9ACTN Unreviewed; 935 AA.
AC A0A0M8Z2U3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Penicillin acylase {ECO:0000313|EMBL:KOX49417.1};
GN ORFNames=ADL09_09230 {ECO:0000313|EMBL:KOX49417.1};
OS Streptomyces sp. NRRL F-7442.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519498 {ECO:0000313|EMBL:KOX49417.1, ECO:0000313|Proteomes:UP000037772};
RN [1] {ECO:0000313|EMBL:KOX49417.1, ECO:0000313|Proteomes:UP000037772}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL F-7442 {ECO:0000313|EMBL:KOX49417.1,
RC ECO:0000313|Proteomes:UP000037772};
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:KOX49417.1}.
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DR EMBL; LGEH01000094; KOX49417.1; -; Genomic_DNA.
DR RefSeq; WP_031084552.1; NZ_LGEH01000094.1.
DR AlphaFoldDB; A0A0M8Z2U3; -.
DR PATRIC; fig|1519498.3.peg.1923; -.
DR Proteomes; UP000037772; 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; 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: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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..44
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 45..935
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005829773"
SQ SEQUENCE 935 AA; 99597 MW; 6DB6F138E34FCA61 CRC64;
MSRRTPRNAL DRLRTPRGLH GFLKTASVCA LIAGVLSPLS PAMAAGTGSA EVKAAQAAAN
DHCGGQCSDI LPPGQNGNAT LAQILLNQAF GTQPSHAEDQ LGPYAKLATG YQGLSNDKIN
TFFNDASFGV PDGQAASTVR PAGRDDVTIV RDKKTGVPHI TGTTRYGTEF GAGYAAAQDR
LWLMDLFRHV GRGQLTPFAG GAPANQGLEQ QFWRSAPYTE ADLEAQIESA AAKSGERGKL
ALADVDAYVA GVNAYIDASD KGRYFPGEYV LTGHKDAITN AGTIERFKRS DLIALASVIG
SLFGAGGGGE VNNALSLLAA QEKYGVAEGT KVWESFRQRN DPEAVLTQQD GSFPYLPTPA
DPQGRALPDA GSVRAEPLVY DRTGSAGAAG ATGASAKAAD AAVTSARRGM SNALVVSGEH
TASGHPVAVF GPQTGYFAPQ LLMLQEIQGP GISARGASFA GLSMYVELGR GQDYAWSATT
SGQDIIDTYA VELCQDDYHY LYRGTCTPME KVERRNAWKP TVADPTAAGS YTMRVWRTKY
GPVESRATVG GKKVAYTTLR SSYLHEADSI IGFQMLNDPD YLNGPERFQG AVQHINYTFN
WFYADSEHTA YYNSGDNPVR ASGVDAEFPV WARQAYEWQD WDPAANTARY TGASAHPQSV
DQGYYVSWNN KQAKDYPAAS WGNGSVHRGD LLDDRVKKLV AEGGVTRTAL VKAMAEAGLA
DLRAEDVLPG LLKVVESAPV SDPAAKTAVD GLKAWLSAGG LRTETSAGAK KYAHADAIRT
LDAWWPLLVK AEFEPGLGSD LYTAFTRNLP VDESPSAAHG PTGAHAGSAF QYGWWSYVDK
DIRSVLGESV KGPLAHAYCG DGDLTACRNT LVSTLKEAAG RTAAQVYPGD ENCSAGDQWC
ADSVIHRTLG GIKHGGIGWQ NRPTYQQVVE FTSHR
//
