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Database: UniProt
Entry: A0A0A5FWJ6_9BACI
LinkDB: A0A0A5FWJ6_9BACI
Original site: A0A0A5FWJ6_9BACI 
ID   A0A0A5FWJ6_9BACI        Unreviewed;       794 AA.
AC   A0A0A5FWJ6;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Beta-lactam antibiotic acylase {ECO:0000313|EMBL:KGX84299.1};
GN   ORFNames=N784_13725 {ECO:0000313|EMBL:KGX84299.1};
OS   Pontibacillus litoralis JSM 072002.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Pontibacillus.
OX   NCBI_TaxID=1385512 {ECO:0000313|EMBL:KGX84299.1, ECO:0000313|Proteomes:UP000030401};
RN   [1] {ECO:0000313|EMBL:KGX84299.1, ECO:0000313|Proteomes:UP000030401}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JSM 072002 {ECO:0000313|EMBL:KGX84299.1,
RC   ECO:0000313|Proteomes:UP000030401};
RA   Huang J., Wang G.;
RL   Submitted (AUG-2013) 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:KGX84299.1}.
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DR   EMBL; AVPG01000042; KGX84299.1; -; Genomic_DNA.
DR   RefSeq; WP_036836400.1; NZ_AVPG01000042.1.
DR   AlphaFoldDB; A0A0A5FWJ6; -.
DR   MEROPS; S45.003; -.
DR   eggNOG; COG2366; Bacteria.
DR   OrthoDB; 9759796at2; -.
DR   Proteomes; UP000030401; 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:UP000030401};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   TRANSMEM        21..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   ACT_SITE        258
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         330
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   794 AA;  89575 MW;  B455795284687BD0 CRC64;
     MEVIPLPRRK KGWRTWQKVS LIVTLVLGFI VVGGLLFLNS WINRSLPQVE GEVAINGLHA
     SVEVIRDANG VPHIKAENEW DLYRAQGFIQ AQDRLFQMDM ARRQASGQLS EVVGSATVTQ
     DKYFRALGLR RAAQKSYEAY SQESKEILQA YADGVNAYIT QAEENNRLPV EFTLMGNSPE
     PWTPLDSLTI GKYMAFDLGG HWERQAFHYY LLQTLPKEKA LELFSTYPEQ APTIIQEAEI
     DVASLLQQAV IPHSYNGSNN WVVSGEKTAS GKPLLADDPH LGLATPSIWY EMHLSSPEQN
     VSGVIFAGVP GIILGHNDSI AWGVTNTGPD VQQLYIEKRH PDQPNEFLFE GEYEEAAVIE
     EPIKVKGEGT VAYEVMETRH GPIISQFAEA SGEEAVLSLR WTALDATAEL EAIIEMNKAT
     NWNQFERALE KFEVPAQNFV FASQDGTIAY KANGKIPIYS NGDDALLPLE GWKAENEWDG
     YIPWDELPRV VNPDKGYIAT ANNKVVGEDY PYHISNNWAQ PYRYKRIAQV LEQGDDFTAA
     EMKNLQMDQH NLQGEEFVPI FLEHVDQGAL SDEEQKAIAI LKEWNYVDAV DGAAPLIFHT
     WMQTFSKQLY EEDIPEEMIK LFNGRAQTTD ELIRQAHRGE EVIWIEEQGG LRQALTIALE
     ETVAMLSEQY GSDATKWKWG DYHQVSFEHP LSSVSYLERF FNPKDPIPVG GSKVTVMAAA
     YEEDTGIVDH GASWRFVADT ADLTQASHTV SPGQAGHFRS EWYHNQRDQW VTGEYHQTKV
     KQYEGSVLML QPKE
//
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