ID A0A2A3H7X2_9ACTN Unreviewed; 893 AA.
AC A0A2A3H7X2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=Penicillin acylase {ECO:0000313|EMBL:PBC64663.1};
GN ORFNames=BKI49_06475 {ECO:0000313|EMBL:PBC64663.1};
OS Streptomyces sp. Tue6028.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2036037 {ECO:0000313|EMBL:PBC64663.1, ECO:0000313|Proteomes:UP000217789};
RN [1] {ECO:0000313|EMBL:PBC64663.1, ECO:0000313|Proteomes:UP000217789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tue6028 {ECO:0000313|EMBL:PBC64663.1,
RC ECO:0000313|Proteomes:UP000217789};
RA Greule A., Flemming S., Bechthold A.;
RT "The Draft Genome Sequence of Streptomyces sp. Tue6028 - Producer of
RT Polyketomycin and Foxicin.";
RL Submitted (OCT-2016) 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:PBC64663.1}.
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DR EMBL; MLCE01000008; PBC64663.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A3H7X2; -.
DR Proteomes; UP000217789; 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; 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; IPR043147; Penicillin_amidase_A-knob.
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 Reference proteome {ECO:0000313|Proteomes:UP000217789}.
SQ SEQUENCE 893 AA; 95052 MW; B9D6148DA892A746 CRC64;
MSPLSQAAAT AAPSAAATND YCGGQCSDIL PPGENGNATL VEILLNQAFG TQPGHAEDQL
APYGNLAKGY SGLTDAKIND FFNDASFGVP SDQVASTTKP RSDVTIVRDK KTGVPHITGT
TRYGTEFGAG YAAAQDRLWL MDVFRHVGRG QLTSFAGGAP SNQGLEQEFW RNAPYTEADL
QAQIDNATAQ AGERGKQALA DANAYIAGIN AYIDASDSGR YFPGEYVLTG HKDSITNAGT
IDHFKLTDLV ALASVIGALF GSGGGGEVNN ALSLLAAQSK YGVVEGTKVW ESFRQRNDPE
AVLTVHDGQS FPYAVKPDDA QGQALPDAGS VTREPLVYDR TGSAGTAAAT GASTTAAKTS
VSSAKRGMSN ALVVSGKHTA SGHPIAVFGP QTGYFAPQLL MLQEIQGPGL SARGASFAGL
SMYVELGRGQ DYSWSATTSG QDIIDTYAVE LCQDDYHYLY HGTCTAMDKV ERTNSWKPTV
ADGTAAGSYR MQVYRTKYGP VEYRATVGGK KVAYTTLRSS FMHEADSIIG FQMLNDPDYV
KSPQTFQSAV QHINYTFNWF YADSSHTAYY NSGDNPVRAT GVDADFPVWA QPAYEWRNWD
AATNTAQYTP ASAHPNSVDQ DYYISWNNKQ AKDYAAAPWG EGSVHRGNLL EDRVKKLVSA
GGVTRSALVK AMADAALADL RAEDVLPKLL KVINSSTVTD PAAAAAVSKL SAWVTAGAKR
TETSAGSHTY ADADAIRILD AWWPLLVKAE FEPVLGSDLY AAFTGSIPVD EAPSAGHGPT
GSHAGSSFQY GWWSYVDKDI RAVLGESVQG GLTQKYCGSG SLGACRDALI STLKEAAGKT
AAQVYPGDDQ CSAGDQWCAD SIVQRTLGGI KHGKISWQNR PTYQQVVEYT SHR
//