ID K0I177_9BURK Unreviewed; 790 AA.
AC K0I177;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Peptidase S45 penicillin amidase {ECO:0000313|EMBL:AFU46000.1};
GN ORFNames=C380_11495 {ECO:0000313|EMBL:AFU46000.1};
OS Acidovorax sp. KKS102.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=358220 {ECO:0000313|EMBL:AFU46000.1, ECO:0000313|Proteomes:UP000006306};
RN [1] {ECO:0000313|EMBL:AFU46000.1, ECO:0000313|Proteomes:UP000006306}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KKS102 {ECO:0000313|EMBL:AFU46000.1,
RC ECO:0000313|Proteomes:UP000006306};
RX PubMed=23209225; DOI=10.1128/JB.01848-12;
RA Ohtsubo Y., Maruyama F., Mitsui H., Nagata Y., Tsuda M.;
RT "Complete Genome Sequence of Acidovorax sp. Strain KKS102, a
RT Polychlorinated-Biphenyl Degrader.";
RL J. Bacteriol. 194:6970-6971(2012).
CC -!- SIMILARITY: Belongs to the peptidase S45 family.
CC {ECO:0000256|ARBA:ARBA00006586}.
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; CP003872; AFU46000.1; -; Genomic_DNA.
DR RefSeq; WP_015014016.1; NC_018708.1.
DR AlphaFoldDB; K0I177; -.
DR STRING; 358220.C380_11495; -.
DR MEROPS; S45.005; -.
DR KEGG; ack:C380_11495; -.
DR PATRIC; fig|358220.3.peg.2341; -.
DR eggNOG; COG2366; Bacteria.
DR HOGENOM; CLU_017615_0_0_4; -.
DR OrthoDB; 9760084at2; -.
DR Proteomes; UP000006306; Chromosome.
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; 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:SF3; ACYL-HOMOSERINE LACTONE ACYLASE PVDQ; 1.
DR PANTHER; PTHR34218; PEPTIDASE S45 PENICILLIN AMIDASE; 1.
DR Pfam; PF01804; Penicil_amidase; 1.
DR PIRSF; PIRSF001227; Pen_acylase; 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..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..790
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003833030"
FT ACT_SITE 234
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
SQ SEQUENCE 790 AA; 84991 MW; 05FCCA0F34495A96 CRC64;
MHEPSTHRSL SMALTTLAAA CTTLFLTGCA SQPGAAGTDR SVTIERTTYG VPHITANDPE
SLAYGVAYAY AQDNVCMTAD QLVTARGQRS STFGAQTIGL LGRRYIPNAQ IDLFMAAHMD
DAMLERAWAK TSAETQALAR GYVAGYNRFL ADNAATLPEA CRGKPWVQPM TMAQYRRMAE
VVAVQAGIAA LADGMLGAQP PAAKAAQAPA ADVNLADAAQ ALRDVGLLDS PLGSNAWAFG
KDVTANGSGM LLGNPHFPWS GPNRFYEMHL TIPGQMDVMG VGIGTYPMVS IGFNKDVAWS
HTVSTGKRFT FYEVTLAEGD PTTYLVDGKP EKMTARKISA QVPSPDGKLQ MREHTVWSTR
WGPLVVVPRA GLTWNAKTAY ALRDANTGNT RMMDAALAFA RARSVQDLHK AHANLGLPWV
NTLAADRSGQ TMYADVSVVP DVDAAQLARC APSQPAAALR AAAGLVVLNG SRAECDWRRD
SASPVPGLIP IGRMPVAFRT DWVHNSNDSF VYTHPGQKFE GISPLVGDAS LTRPRTRAGL
AEIPEMLSRG KVTLQAIQGQ LFENRNFMAR VVVPDLLAAC DKAPTAESRD GCAALKGWDR
RNNVDARSAH VFREFWRTAR NIPGVHRVPF DPAQPVATPA GLKMDDATTA AKVWEALDGA
VKAIRTSGYT LDATLGSVQR PAITEEAIAL HGGEEFEGVL NNLGRQEPAP ITKAGLRIDY
GTSYVQTVTF DAKGPVAQAI LTYGQSTNPA SPHANDQMRE FSAKRWHTLP FHRDDVVKAR
VGEPLRLVRP
//
