ID I3ZLW9_TERRK Unreviewed; 744 AA.
AC I3ZLW9;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Penicilin amidase {ECO:0000313|EMBL:AFL90237.1};
GN OrderedLocusNames=Terro_4029 {ECO:0000313|EMBL:AFL90237.1};
OS Terriglobus roseus (strain DSM 18391 / NRRL B-41598 / KBS 63).
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Terriglobus.
OX NCBI_TaxID=926566 {ECO:0000313|EMBL:AFL90237.1, ECO:0000313|Proteomes:UP000006056};
RN [1] {ECO:0000313|EMBL:AFL90237.1, ECO:0000313|Proteomes:UP000006056}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18391 / NRRL B-41598 / KBS 63
RC {ECO:0000313|Proteomes:UP000006056};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Munk A.C.C.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "Complete genome of Terriglobus roseus DSM 18391.";
RL Submitted (JUN-2012) 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; CP003379; AFL90237.1; -; Genomic_DNA.
DR RefSeq; WP_014787497.1; NC_018014.1.
DR AlphaFoldDB; I3ZLW9; -.
DR STRING; 926566.Terro_4029; -.
DR MEROPS; S45.002; -.
DR KEGG; trs:Terro_4029; -.
DR PATRIC; fig|926566.3.peg.3972; -.
DR eggNOG; COG2366; Bacteria.
DR HOGENOM; CLU_021155_0_0_0; -.
DR OrthoDB; 9759796at2; -.
DR Proteomes; UP000006056; Chromosome.
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 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 Reference proteome {ECO:0000313|Proteomes:UP000006056};
KW Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..744
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003685023"
FT ACT_SITE 215
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT BINDING 285
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 287
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 288
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ SEQUENCE 744 AA; 82800 MW; D1A7ACA6B12580F0 CRC64;
MKPCTAAAAL LFAVAATPAF AQKSAVSSTM PEPARWSAHA KAITVTRDNW GIAHVHGKTD
ADAVFGMIYT QCEDDFNRVE NNYLVNLGRL AEADGEAKIW QDLRQQLFID PQVLKQDYAD
SPQWLKALMD AWADGANFYL SKHPETKPRV LTHFEPWMAL SFTEGSIGGD IERVNLTELE
KFYGAKSTAQ RSIDEQNAMA AQLAQVNRDV EPSGSNGAAI APGNTANHHP LLLINPHTSF
FFRSELQMQS DEGLNAYGAV TWGQIFVYQG FNDRAGWMHT SSNVDAVDEF RDTLMRVDGK
VLGYRYGSDT KPFKTRAITL QYKAADGSMK LRSFDAKFDH RGPIVRADGD AWVSIELMNK
PVPALQQSFL RTKARSYADY KTTMELMANS SNNTIFASAD GDIAYWHGNY IPERDTRYDF
TKPVDGSNPA TDWQGLMPLA QIPQLHNPHS GWLENVNNAP WSGAGESSLK KADYPPYVEQ
SIETARGLHM VKVLNDRRDF TLDSLLAAAF DPYLPYFART VPVLLKAYDA LPQDDAQRKA
LAPQMEVLRK WDYKWGADSV ATSLAIYWGE ATGSPVAGEA YREHTLWEDY VATKIPAATL
LTGLQTATDK LTADFGAWQK PWGEINRYQR LDDSIVPHFD DAQPSIAIPF TASVWGSLAS
SAARAYPNTK KRYGTHGNSF VAVVEFGPKR VSARAITCGG ESGDPSSKHF NDEQDRYASG
DFREVMYYPD QLKGHIERTY HPGE
//
