ID A0A100Y950_9ACTN Unreviewed; 806 AA.
AC A0A100Y950;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Penicillin amidase {ECO:0000313|EMBL:KUH39979.1};
GN ORFNames=ATE80_04075 {ECO:0000313|EMBL:KUH39979.1};
OS Streptomyces kanasensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=936756 {ECO:0000313|EMBL:KUH39979.1, ECO:0000313|Proteomes:UP000054011};
RN [1] {ECO:0000313|EMBL:KUH39979.1, ECO:0000313|Proteomes:UP000054011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZX01 {ECO:0000313|EMBL:KUH39979.1,
RC ECO:0000313|Proteomes:UP000054011};
RA Zhang G., Han L., Feng J., Zhang X.;
RT "Genome-wide analysis reveals the secondary metabolome in Streptomyces
RT kanasensis ZX01.";
RL Submitted (NOV-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:KUH39979.1}.
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DR EMBL; LNSV01000006; KUH39979.1; -; Genomic_DNA.
DR RefSeq; WP_058940725.1; NZ_LNSV01000006.1.
DR AlphaFoldDB; A0A100Y950; -.
DR STRING; 936756.ATE80_04075; -.
DR OrthoDB; 4759017at2; -.
DR Proteomes; UP000054011; 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:SF3; ACYL-HOMOSERINE LACTONE ACYLASE PVDQ; 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 Reference proteome {ECO:0000313|Proteomes:UP000054011};
KW Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..43
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 44..806
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007091368"
SQ SEQUENCE 806 AA; 86025 MW; 429A4ACA0767E048 CRC64;
MDQLTSSAVL LGGTVLLRTH LRRLLPAAVA LLATAATTLP ATAAGPPAEG RNPSAGGLSA
TIRYTEYGIP HILARDYAGL GFGTGWAQAA DQACVLADGF VTVRGERSRY FGPDAVPDGS
LSSARRNLSS DLYFTGVREA RTVERLLARP APAGPSRTQK ELMRGWAAGY NAWLAKNRVT
DPACAGKPWV RPVTPLDVAR RSYALAVLGG QGAAVEAITA AAPPAAGPAA GPAPDARRLA
EAARGMFDER TATMGSNAVA FAGGTTANGR GLLLGNPHYP WHGGRRFWQS QQTIPGELNV
QGASLLGAPL VQIGFSDKVA WSHTVATGRT FNLHQLSLDP ADPTAYVVDG RSERMVRRTV
TVPVASGDPV TRTQWWTRYG PVVTAFAGDP LPWTATTAYA LHDPNAENLR MADTSLGLAK
ARSTRDVERA LRRTQGLPWV NTVASDRNGG TLFAQAQVLP RITDELAERC STPLGRALYP
AAGIAVLDGS RGACALGRDR DAVQPGIMGP SRWPVLRDAA YAENSNDSAW LANADRPFTR
YERVFGDIGT ERSLRTRGAI EDVAAMADRG GLTVADLQRQ QFANRVPAAD LTADDVVRAC
PAALPDEPAA CGALARWDRR VDTTSRGALL FDRFWLRLQR EVPGPDRWKV PFSAADPVGT
PRSLNTAAPG FATALRGAVT EVRAAGIPFD APLGEHQYVV RGGERIPVHG GTGTGVWNMT
VPVWDAARGA YTEVQHGTSH VQAVGWDDSR CPVARTLLSY AQSSDPGSPH HADQTRLYSQ
ERWVTARFCE RDILSDPALR VVRVAQ
//
