ID A0A1I6MCU1_9BACT Unreviewed; 870 AA.
AC A0A1I6MCU1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Penicillin amidase {ECO:0000313|EMBL:SFS13524.1};
GN ORFNames=SAMN05421771_2329 {ECO:0000313|EMBL:SFS13524.1};
OS Granulicella pectinivorans.
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Granulicella.
OX NCBI_TaxID=474950 {ECO:0000313|EMBL:SFS13524.1, ECO:0000313|Proteomes:UP000199024};
RN [1] {ECO:0000313|EMBL:SFS13524.1, ECO:0000313|Proteomes:UP000199024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21001 {ECO:0000313|EMBL:SFS13524.1,
RC ECO:0000313|Proteomes:UP000199024};
RA de Groot N.N.;
RL Submitted (OCT-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 -!- SIMILARITY: Belongs to the peptidase S45 family.
CC {ECO:0000256|ARBA:ARBA00006586}.
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DR EMBL; FOZL01000001; SFS13524.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6MCU1; -.
DR STRING; 474950.SAMN05421771_2329; -.
DR OrthoDB; 9759796at2; -.
DR Proteomes; UP000199024; 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:UP000199024};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT TRANSMEM 49..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 315
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT BINDING 392
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 395
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ SEQUENCE 870 AA; 95461 MW; A1FB9C1C7623AC5A CRC64;
MHPLDPTLPE PELITRQSPP EPGSEFTPGK RRYGLFDLDR PRPGRLVRIL GLILPILLAV
GLVAYATAMY YSRKALIASL PQLDGTLSVP GLSAPVTVLR DAQGVPHIRA ANLDDLLLAQ
GYVTAQDRLW QMDGLRRNAA GDLAEVLGSA LIDHDRIQRI LQIRASAERT LATLPPNQFH
ELEQYAKGVN ASIAAQRTHL PFEFIALRYE PAPWTPTDTL LIGLSMFQQL SNGYTQKLAR
EAISAKLPPE LLADLYPVGS WRDHPPGHTI DLSIPVEEIE QIPLDESQSK LNLTPDHVNA
LLQSLSPCGD CIPGSNNWVV SGAHSTTGKP ILANDTHLAH TVPGIWYETD LEAPLPNGGS
FHAAGVAIPG TPFIEIGHNA HLAWGMTVLP ADTQDVYIER IQNNQYQSPD GAFHPIEHRT
ELIKVRNGTD VSLDVKLTRH GNVLTPIISS LFHDEKRPLS LRWTIYDPTT LTAAFGNINA
ASDWPSFNAA LSQYGGPPMN LVYADDQGHI AFHAIGRIPT RGIDPAHPEA IPPVPTDATA
PDALTHEWSG FIPYEQLPSA IDPPGGILAT ANARTAPDGY PYPIALNWAS PYRNERIWKQ
LASKPRFSPA DMIDLQTDVY SDLDHVIAQR LAYAIDHAID HPAIDGKPRP HIDQKQLHDA
ADLLRSWNGK VDANSSAAAI VDATRAALWA MLLNPRLGQL ASLYTWGSRD YAEEQLIMHT
PDRWLPKSFA TWDDLLTEAV LKGISASHAP FDITKWRSGS LHPVDIEHPI YSQSEILKAL
IGRPIGTGTH PQSGDLTTVK QVDRTFGPSQ RLTVDLSNPD NTTLNVVLGQ SGNPASPNFL
DQFPFWLAGK TFPFPFSHET IRATHTLILK
//
