ID A0A0K9XI24_9ACTN Unreviewed; 807 AA.
AC A0A0K9XI24;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Penicillin amidase {ECO:0000313|EMBL:KNB52312.1};
GN ORFNames=AC230_12270 {ECO:0000313|EMBL:KNB52312.1};
OS Streptomyces caatingaensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1678637 {ECO:0000313|EMBL:KNB52312.1, ECO:0000313|Proteomes:UP000037288};
RN [1] {ECO:0000313|Proteomes:UP000037288}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMAA 1322 {ECO:0000313|Proteomes:UP000037288};
RA Santos S.N., Gacesa R., Taketani R.G., Long P.F., Melo I.S.;
RT "Draft genome sequence of Streptomyces sp. CMAA 1322, a bacterium isolated
RT from Caatinga biome, from dry forest semiarid of Brazil.";
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:KNB52312.1}.
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DR EMBL; LFXA01000007; KNB52312.1; -; Genomic_DNA.
DR RefSeq; WP_049716168.1; NZ_LFXA01000007.1.
DR AlphaFoldDB; A0A0K9XI24; -.
DR STRING; 1678637.AC230_12270; -.
DR PATRIC; fig|1678637.3.peg.2644; -.
DR OrthoDB; 4759017at2; -.
DR Proteomes; UP000037288; 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:UP000037288};
KW Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..807
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039058164"
SQ SEQUENCE 807 AA; 85708 MW; 7B5C2B25061548FA CRC64;
MRLRHRLRAL TVGALALLTG AGALPAASAA TAGDDNRPSG GGLSATIRYT EYGIPHIVAK
DYASLGFGDG WAQAADQVCT LADGFVTLRG ERSRHFGPDA APGPDLSDAS TNLSSDLFFR
GIRDARTVER LLARPAPEGP SRPARELARG WAAGYNAWLA RNRITDERCR GASWVRPVTE
LDVARRGYAL TVLGGQGGTV DGITGARPSS GAAPRTAARR APEAAAKALF AARAGDMGSN
AVAFSGAVTA TGRGLLLGNP HYPWQGGRRF WQAQLTIPGE LDVAGVSLLG MPVVEIGHNP
YVAWSHTVAT GVPFGLYELR AAPGNPHAYL VDGVPEAMTE RKVTVPVRGE DGRVTDVTRS
QWWTRYGPVL TSLGGELPLP WTGKTLYAIT DPNAAQLRFT DTSLAFGKAR SVHDVRDALR
RTQGLPWVNT VAADRAGHSL MSQSQVLPRI TDDLAGRCST ALGRRLYPGT GLAVLDGSRR
ACALGRDRDA LQPGVFGPSA MPTLTDAPYA ENSNDSAWLS NADRPLTGYP RVFGDIGTPR
SLRTRGAVED VAALARRGRL TVDDLREQQF ADRVPAGALA AADTAAACAK LPGGRATGSD
GKAVDVSAAC GVLARWDRTV RPGSRGALLF DRYWRKLTAA VPQDKLWRVP FSAEDPVRTP
RSLDTAHPAV ARVLADAVAE LRAQGTALDA PWGEHQFVER GGKRLPIPGG SHDLGVWNVV
QSRWDAARGA YTDVRSGTSY LQAVGFDGGP CPVARTLLTY SQSSDPASPH YSDQTELFSA
GRMVKARFCE KDILASPALR VVRVGGR
//
