ID   A0A246FPQ9_9BACT        Unreviewed;       830 AA.
AC   A0A246FPQ9;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Penicillin acylase family protein {ECO:0000313|EMBL:OWP64735.1};
GN   ORFNames=CDA63_02960 {ECO:0000313|EMBL:OWP64735.1};
OS   Hymenobacter amundsenii.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Hymenobacter.
OX   NCBI_TaxID=2006685 {ECO:0000313|EMBL:OWP64735.1, ECO:0000313|Proteomes:UP000197277};
RN   [1] {ECO:0000313|EMBL:OWP64735.1, ECO:0000313|Proteomes:UP000197277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCM 8682 {ECO:0000313|EMBL:OWP64735.1,
RC   ECO:0000313|Proteomes:UP000197277};
RA   Sedlacek I., Kralova S., Pantucek R., Svec P., Holochova P., Stankova E.,
RA   Vrbovska V., Busse H.-J.;
RT   "Hymenobacter amundsenii sp. nov. isolated from regoliths in Antarctica.";
RL   Submitted (JUN-2017) 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:OWP64735.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; NIRR01000002; OWP64735.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A246FPQ9; -.
DR   OrthoDB; 9759796at2; -.
DR   Proteomes; UP000197277; 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   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   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   ACT_SITE        278
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         350
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         353
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   830 AA;  93115 MW;  4F96E93068A49002 CRC64;
     MLRYVKAVLA LLTTVILAWV LNTKQGDVPP VARLLSPYQG FWRNGETATD FPAQQTLHLP
     GLHQTVRVRF DDRRVPHVFA LNDHDLYYAQ GYLTARDRLW QMEFMTRVAA GRISEVVGPK
     ALEYDRFQRR MGLPLGAANS LREMLKNDTT RLVLESYSAG VNAYISQLRP ADYPFEYKLL
     DYAPEPWQPL KCALLLKLMA WDLSGRSDDL RLSNILSKYG SEVTRDLFPD YPVREDPVVP
     VGAPLAFTPL PVPAAPPLFG AAVSGLVPER EPDAELGSNN FAVAGSRSAS GLPLLANDPH
     LQLNLPSIWY QIQLSAPGQN VYGVTIPGAP AIIIGFNESV AWGVTNVGGD VLDWYQLKFR
     DSTRREYWHD GRWKPVRRVV EHVAVRGRPD VLDTVLYTHH GPVVYDHDEK PFNAQTPVRH
     ALRWTAHEGA NEVLAFVKLN HARNYADYDQ ALRTYASPAQ NFIFASSQND IAIRPNGRFP
     LKYPDQGKFI LDGSDARQDW QGWIPMSQTP RVKNPERGFL SSANQHSAGP DYPYYLGWDY
     APWDRAHRIN EQLATMHHAT ADTLRRLQND DLGINAQTML PWMLAMVQAG GTPVSQTGER
     GGSLQTAVLQ TLQGWNYHYT AKAVAATVFE LWYQELVRRL WEDDFSRAAT GLEMRYPARD
     RTNQLLLNQS GNPAASFQGA SPWIDDRRTP EKENVHDLLT ASLQFTVDSL TRKFGPLGPG
     WAWANQKSTD INHLAQLPGF GHQDIVCPGS PGTVNATGAR NGPSWRMVVA LGPQVKAYGI
     FPGGQSGNPA SRYYDDMLES WRTGQLDELV FLRAADENHP RLQAAWRLEQ
//