PAC2_PSES3
ID PAC2_PSES3 Reviewed; 774 AA.
AC P15558;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Penicillin acylase 2 proenzyme;
DE EC=3.5.1.11;
DE AltName: Full=Cephalosporin acylase II;
DE AltName: Full=Penicillin acylase II;
DE AltName: Full=Penicillin amidase II;
DE Contains:
DE RecName: Full=Penicillin acylase 2 small subunit;
DE AltName: Full=Penicillin acylase II small subunit;
DE Contains:
DE RecName: Full=Penicillin acylase 2 large subunit;
DE AltName: Full=Penicillin acylase II large subunit;
DE Flags: Precursor;
GN Name=acyII;
OS Pseudomonas sp. (strain SE83).
OC Bacteria; Proteobacteria.
OX NCBI_TaxID=309;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-38 AND 240-276,
RP AND SUBUNIT.
RC STRAIN=SE83;
RX PubMed=3680178; DOI=10.1128/jb.169.12.5821-5826.1987;
RA Matsuda A., Toma K., Komatsu K.;
RT "Nucleotide sequences of the genes for two distinct cephalosporin acylases
RT from a Pseudomonas strain.";
RL J. Bacteriol. 169:5821-5826(1987).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + penicillin = 6-aminopenicillanate + a carboxylate;
CC Xref=Rhea:RHEA:18693, ChEBI:CHEBI:15377, ChEBI:CHEBI:29067,
CC ChEBI:CHEBI:51356, ChEBI:CHEBI:57869; EC=3.5.1.11;
CC -!- SUBUNIT: Heterodimer of a small subunit and a large subunit processed
CC from the same precursor. {ECO:0000269|PubMed:3680178}.
CC -!- SIMILARITY: Belongs to the peptidase S45 family. {ECO:0000305}.
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DR EMBL; M18278; AAA25690.1; -; Genomic_DNA.
DR PIR; A28392; A28392.
DR AlphaFoldDB; P15558; -.
DR SMR; P15558; -.
DR MEROPS; S45.003; -.
DR PRIDE; P15558; -.
DR BRENDA; 3.5.1.93; 5085.
DR GO; GO:0008953; F:penicillin amidase activity; IEA:UniProtKB-EC.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1400.10; -; 1.
DR Gene3D; 1.10.439.10; -; 1.
DR Gene3D; 2.30.120.10; -; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR014395; Pen/GL7ACA/AHL_acylase.
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; PTHR34218; 1.
DR Pfam; PF01804; Penicil_amidase; 1.
DR PIRSF; PIRSF001227; Pen_acylase; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
PE 1: Evidence at protein level;
KW Antibiotic resistance; Direct protein sequencing; Hydrolase; Zymogen.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3680178"
FT CHAIN 2..774
FT /note="Penicillin acylase 2 proenzyme"
FT /id="PRO_0000253349"
FT CHAIN 2..?239
FT /note="Penicillin acylase 2 small subunit"
FT /id="PRO_0000021991"
FT CHAIN 240..774
FT /note="Penicillin acylase 2 large subunit"
FT /id="PRO_0000021992"
FT ACT_SITE 240
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
SQ SEQUENCE 774 AA; 83694 MW; 1AE1A6EE53010B94 CRC64;
MTMAAKTDRE ALQAALPPLS GSLSIPGLSA PVRVQRDGWG IPHIKASGEA DAYRALGFVH
AQDRLFQMEL TRRKALGRAA EWLGAEAAEA DILVRRLGME KVCRRDFEAL GAEAKDMLRA
YVAGVNAFLA SGAPLPIEYG LLGAEPEPWE PWHSIAVMRR LGLLMGSVWF KLWRMLALPV
VGAANALKLR YDDGGQDLLC IPPGVEAERL EADLAALRPA VDALLKAMGG DASDAAGGGS
NNWAVAPGRT ATGRPILAGD PHRVFEIPGM YAQHHLACDR FDMIGLTVPG VPGFPHFAHN
GKVAYCVTHA FMDIHDLYLE QFAEDGRTAR FGNEFEPVAW RRDRIAVRGG ADREFDIVET
RHGPVIAGDP LEGAALTLRS VQFAETDLSF DCLTRMPGAS TVAQLYDATR GWGLIDHNLV
AGDVAGSIGH LVRARVPSRP RENGWLPVPG WSGEHEWRGW IPHEAMPRVI DPPGGLIVTA
NNRVVADDHP DYLCTDCHPP YRAERIMERL VASPAFAVDD AAAIHADTLS PHVGLLRARL
EALGIQGSLP AEELRQTLIA WDGRMDAGSQ AASAYNAFRR ALTRLVTARS GLEQAIAHPF
AAVPPGVSPQ GQVWWAVPTL LRNDDAGMLK GWSWDEALSE ALSVATQNLT GRGWGEEHRP
RFTHPLSAQF PAWAALLNPV SRPIGGDGDT VLANGLVPSA GPEATYGALS RYVFDVGNWD
NSRWVVFHGA SGHPASPHYA DQNAPWSDCA MVPMLYSWDR IAAEAVTSQE LVPA