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Entry: A0A024Q9J0_9BACI
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ID   A0A024Q9J0_9BACI        Unreviewed;       794 AA.
AC   A0A024Q9J0;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Penicillin acylase 2 {ECO:0000313|EMBL:CDQ38875.1};
GN   Name=acyII {ECO:0000313|EMBL:CDQ38875.1};
GN   ORFNames=BN990_01151 {ECO:0000313|EMBL:CDQ38875.1};
OS   Virgibacillus massiliensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX   NCBI_TaxID=1462526 {ECO:0000313|EMBL:CDQ38875.1, ECO:0000313|Proteomes:UP000028875};
RN   [1] {ECO:0000313|EMBL:CDQ38875.1, ECO:0000313|Proteomes:UP000028875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Vm-5 {ECO:0000313|EMBL:CDQ38875.1,
RC   ECO:0000313|Proteomes:UP000028875};
RA   Urmite Genomes U.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000028875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Vm-5 {ECO:0000313|Proteomes:UP000028875};
RA   Khelaifia S., Croce O., Lagier J.C., Raoult D.;
RT   "Draft genome sequence of Virgibacillus massiliensis Vm-5.";
RL   Submitted (MAY-2014) 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   -!- 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:CDQ38875.1}.
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DR   EMBL; CCDP010000001; CDQ38875.1; -; Genomic_DNA.
DR   RefSeq; WP_038242863.1; NZ_WMER01000001.1.
DR   AlphaFoldDB; A0A024Q9J0; -.
DR   STRING; 1462526.BN990_01151; -.
DR   MEROPS; S45.003; -.
DR   eggNOG; COG2366; Bacteria.
DR   OrthoDB; 9759796at2; -.
DR   Proteomes; UP000028875; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   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   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001227-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028875};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   TRANSMEM        20..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   ACT_SITE        259
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         331
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   794 AA;  90516 MW;  85F346D86360A9DF CRC64;
     MEERVFDKQP HRQERKKKKF AFITSGILLL TIGSLILFVN AFIGRSVEQV NGTINLPILK
     EQVQVITDEN GVPHIKAAND HDLYVAQGYV QAQYRLFQME MSRRQASGTL SEVVGEAAID
     QDKYFRTLGL RRAATKSYDI YSEQAKQVLQ YFSDGVNAYV DEAIRTNRLP IEFTLMGIKP
     EAWTPIDSLT IGKYMAFDLG GHWERQAFNY YLLQNYPENK AYELFPDYPE EKPVIMEEPY
     VSIPESFDKA IIPPAFNGSN NWVVSGDKTA SGLPLLADDP HLGLATPSIW LQMQLESDTN
     HVSGVIFAGV PGIILGHNDT IAWGVTNTGP DVQQLYLEKQ HPERENQFYY EGKWEKATVI
     EEPIKVKNEE TLDYHVVETR HGPIISEFAE ESGKDTMLSL RWTALEPTTE LEAILEINRA
     SDWSSFEKGL EKFLVPAQNF VFAQKNGTIA YKANGNIPIY QDGTDALLPL PGWEKESEWK
     GYIPFEQLPR IVNPAKGYIA TANNKITTED YPYHISNVWA QPYRYERIAE VLESSNALTV
     RDMQDLQMDT KNMQAEEFVP VFLSILRNMN ISEKEKQAVN VMKKWDYHDE ATAVQPLIFH
     HWMNELEAII YQDIPDNMMD LFGSRGQTTD ELIRKSVEGK DAIWVENAGG LQQVVKDALT
     NSLNKLENDF GKKMNDWQWG DYHQVSFRHP LSEINPVLEF FFNNEAPLPV GGSKVTPMAA
     AYKTETGIVN HGASWRFVVD MEEPKKGYHI VGPGQSGHFK SDWYHDQLTD WVHGSYHETT
     LSQSQGNLLI FQPE
//
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