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Database: UniProt
Entry: A0A1I5WX08_9RHOB
LinkDB: A0A1I5WX08_9RHOB
Original site: A0A1I5WX08_9RHOB 
ID   A0A1I5WX08_9RHOB        Unreviewed;       626 AA.
AC   A0A1I5WX08;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Penicillin amidase {ECO:0000313|EMBL:SFQ24161.1};
DE   Flags: Fragment;
GN   ORFNames=SAMN04488047_1625 {ECO:0000313|EMBL:SFQ24161.1};
OS   Tranquillimonas alkanivorans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Tranquillimonas.
OX   NCBI_TaxID=441119 {ECO:0000313|EMBL:SFQ24161.1, ECO:0000313|Proteomes:UP000199356};
RN   [1] {ECO:0000313|EMBL:SFQ24161.1, ECO:0000313|Proteomes:UP000199356}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19547 {ECO:0000313|EMBL:SFQ24161.1,
RC   ECO:0000313|Proteomes:UP000199356};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S45 family.
CC       {ECO:0000256|ARBA:ARBA00006586}.
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DR   EMBL; FOXA01000062; SFQ24161.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5WX08; -.
DR   STRING; 441119.SAMN04488047_1625; -.
DR   OrthoDB; 9760084at2; -.
DR   Proteomes; UP000199356; 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; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 2.
DR   Gene3D; 1.10.439.10; Penicillin Amidohydrolase, domain 1; 2.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
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; 3.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 2.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000199356};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..626
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011459415"
FT   NON_TER         626
FT                   /evidence="ECO:0000313|EMBL:SFQ24161.1"
SQ   SEQUENCE   626 AA;  67514 MW;  98DC3B9A3127A82F CRC64;
     MKTVFRVTLR VFLALAAATT ATAALVGYLL LASVPDYDED FTVPGIRGPV DILRDASAIP
     HISAASTADV YFALGFVHAQ DRLGQMLRAR RSAAAEAMRQ RRVTFGRPVS AALDAYADGV
     NAWISELARG GRGGGGPELL MLGAPIQPWE PSDSLALARA FLENLQIAHS SDESKIMGGQ
     VPAGRPNNAP GLLSHRRDAS LDVWAVPASR TVSGAPILAA DVTGPLALPS QWYLADLQLP
     SGPVVGATLP GIPFVVIGRS HSLLWGFRSI GPPAEVTTSE LPDAASEAFL AVLGRLTQSS
     SASDAAGKVA DLPPTGLQLV AADGQAVEAW PRCARPTCEP ARDFLEVRRD VLDDRQTVYS
     IESAIAVQQD VVSAVARTLL PLMARELWFD APAVRGEGIT SSTLRSDVLN RLASWNGEME
     RLAPEPLVFW AWARALQQRI LQDEFPAADH VWRRPRPDFL HAVLSDREGS AIWCDVRLSK
     RRETCDELLL ASFDDALNWI IDRYGDDPSS WSWGSEHVMV MKWSAIRSGS VLDGVADLKA
     FAGGGPYTQK STLFDEGEAN PFESRSGTNF QAVMTLGEDT ASHFIAPAGQ SGHPLSRFYD
     NLFSRWKHAD YLDMSSDLSI ARSAAA
//
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