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Database: UniProt
Entry: A0A1B7UMN9_9GAMM
LinkDB: A0A1B7UMN9_9GAMM
Original site: A0A1B7UMN9_9GAMM 
ID   A0A1B7UMN9_9GAMM        Unreviewed;       783 AA.
AC   A0A1B7UMN9;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Penicillin amidase {ECO:0000313|EMBL:OBP15751.1};
GN   ORFNames=A5320_10700 {ECO:0000313|EMBL:OBP15751.1};
OS   Rheinheimera sp. SA_1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Rheinheimera.
OX   NCBI_TaxID=1827365 {ECO:0000313|EMBL:OBP15751.1, ECO:0000313|Proteomes:UP000092258};
RN   [1] {ECO:0000313|EMBL:OBP15751.1, ECO:0000313|Proteomes:UP000092258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA_1 {ECO:0000313|EMBL:OBP15751.1,
RC   ECO:0000313|Proteomes:UP000092258};
RA   Lavstsen T., Jespersen J.S.;
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PIRSR:PIRSR001227-2};
CC       Note=Binds 1 Ca(2+) ion per dimer. {ECO:0000256|PIRSR:PIRSR001227-2};
CC   -!- SUBUNIT: Heterodimer of an alpha subunit and a beta subunit processed
CC       from the same precursor. {ECO:0000256|ARBA:ARBA00038735}.
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:OBP15751.1}.
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DR   EMBL; LXWK01000015; OBP15751.1; -; Genomic_DNA.
DR   RefSeq; WP_068064665.1; NZ_LXWK01000015.1.
DR   AlphaFoldDB; A0A1B7UMN9; -.
DR   STRING; 1827365.A5320_10700; -.
DR   OrthoDB; 9760084at2; -.
DR   Proteomes; UP000092258; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:InterPro.
DR   GO; GO:0009372; P:quorum sensing; IEA:UniProtKB-KW.
DR   CDD; cd03747; Ntn_PGA_like; 1.
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:SF4; ACYL-HOMOSERINE LACTONE ACYLASE QUIP; 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   Calcium {ECO:0000256|PIRSR:PIRSR001227-2};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001227-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092258};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   ACT_SITE        254
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         186
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         330
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         333
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   783 AA;  87182 MW;  0E288B01A002A74E CRC64;
     MKWLKPMFYV VLTLVAIVAI TLYSALHSSL PLYEGATSAE VTAKVQLSRD AQGYLTVRAQ
     NRLDAAYGLG FAHAQDRYFQ MDLLRRNSAG ELSELFGERA LPMDISRRMH RFRDRAEAIL
     TTLPAPQKLL LQHYTQGVNE GLTQLPMRPF EYWLLQQKPA AWQDTDSLLV AYSMYLDLQS
     AAGADELAQG VLKQAIPDDW YQFLNQHSSD WQAAIDGSKV TAIPLPESDY PRVLSNQKVA
     CQDCRLRDSR DIGSNNFSVS GKLTSHGAAL LADDMHLGIR VPGTWFKAQL IWGEGEAQHS
     VAGVSLPGSP SIVAGSNGHI AWGFTNSTAD WHDVIKLQSD ENPQRYITPA GAKEYSYNNE
     VIKVKGLADV VMLVKETEWG PVMPAPFGQF ALRWVAYDPQ ALNLELQQLE QVRTVDDALK
     IASKVGMPAQ NLLVADKQGN HAWTLIGPIP KRTLQDMDTP QDWSTGHNFW DGYLSDTDYP
     TVKNPDTQRL WTANSRVVGG DALKLLGDGG YDLGARGMQI RDGLLAVDQH SEQSLHQIQL
     DHRALFLKRW QQLLLEVLTD DFVARHQLGQ YRSYVELDSA AASPASVGYS LVRAFRDQSL
     QQVFAPIASL MEQQKLKLTD LKLVLETPGW ALIQAKRPDT VPAPFISWQQ LLEQAVLKSR
     DALLAKTDGD LANARWGLFN QAKIEHPLSS AIPWFGQFLN MSASEMAGDR HMPRVQQPIH
     GQSQRMVVAP GQEAKGILTI PAGQSGHPLS PFYRADHAFW LNEAELGFLP GEQKYLLELQ
     PRG
//
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