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
//