ID A0A1D8G1R2_9ACTN Unreviewed; 940 AA.
AC A0A1D8G1R2;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Acyl-homoserine lactone acylase QuiP {ECO:0000313|EMBL:AOT59384.1};
DE EC=3.5.1.97 {ECO:0000313|EMBL:AOT59384.1};
GN Name=quiP {ECO:0000313|EMBL:AOT59384.1};
GN ORFNames=A4G23_02224 {ECO:0000313|EMBL:AOT59384.1};
OS Streptomyces rubrolavendulae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=285473 {ECO:0000313|EMBL:AOT59384.1, ECO:0000313|Proteomes:UP000095349};
RN [1] {ECO:0000313|EMBL:AOT59384.1, ECO:0000313|Proteomes:UP000095349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJM4426 {ECO:0000313|EMBL:AOT59384.1,
RC ECO:0000313|Proteomes:UP000095349};
RA Kim J.-G.;
RT "Streptomyces rubrolavendulae MJM4426 Genome sequencing and assembly.";
RL Submitted (SEP-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}.
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; CP017316; AOT59384.1; -; Genomic_DNA.
DR RefSeq; WP_069976770.1; NZ_CP017316.1.
DR AlphaFoldDB; A0A1D8G1R2; -.
DR STRING; 285473.A4G23_02224; -.
DR KEGG; srn:A4G23_02224; -.
DR PATRIC; fig|285473.5.peg.2316; -.
DR OrthoDB; 9759796at2; -.
DR Proteomes; UP000095349; 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 CDD; cd03747; Ntn_PGA_like; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 3.
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; IPR023343; Penicillin_amidase_dom1.
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:0000313|EMBL:AOT59384.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001227-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000095349}.
FT REGION 241..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 333
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 411
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 414
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ SEQUENCE 940 AA; 102635 MW; 80A35615C2ED2EE8 CRC64;
MPANTTVSSP KKKGRRARLL VIALVLALVA GVGYGAYWSV STVRAPFPQT TGTLTLPGLT
GPVDVKRDAR GIPQIYASTD ADLFRAQGYV QAQDRFWEMD VRRHMTAGRL SEMLGKEAVD
TDAFLRTLGW HRVAQEEYDK VLSDETKKNL QAYADGVNAY LKDKTPREVS VEYSVLEFSH
DYAIEPWTPV DSIAWLKAMA WDLRGNMQDE IDRSLMTSRL SAEQIKDLYP AYPFKTHRPV
VEGFKPEGAG GDDEDGNGNG DGTGNGTGQG AGLGGGSGSG TGTGGGLQNG QSGSQGGIGS
GSQGGLQSQL AALSDALDSV PALLGPNGPG IGSNSWVVSG KHTTTGKPLL ANDPHLAPQL
PSVWYQMGLH CRAVSDKCRY DVAGYTFAGM PGVIIGHNQD IAWGFTNLGA DVTDLYLQKV
TDRGYLRGTK EVPFETREEV IKIAGGGSRT ITVRTTNNGP LISDRSDELE KVGQKAPVAN
AAPDRADGYA VSLRWTALTP GKSMDAVFKL NQARDFEEFR DAARDFEVPS QNLVYADAKG
AEGHIGYQAP GRIPVRAKGH DGTLPAPGWD PSYDWKDEYV PFDELPYEED PKRGYIVTAN
QAVVDDAYPH HLTADWGYGS RSQRINDLIE SKIKDGGKIS TDDMRTMQMD NSSEIAKQLT
PLLLKVDISD PYVREAQKLL EGWDYTQEAD SAAAAYFNAV WRNVLKLAFG DKLPKELRVK
GECLNVPSVD PNVPDDQRGR LVRECGQRDA DDAQPDGGDR WYEVVRPLLQ DEDNAWWKTP
ANRLDEATQT RDQLLARAMK DARWELTAQL GKDISTWSWG RLHQLTLRNQ TLGKGGPDPV
KYLLNRGPWN LAGGEAAVNA TGWNAAGGYG VVWVPSMRMV VNVGEWDKSR WINLTGASGH
AYHPNYTDQT DAWARGELLA WPFSDKAVDA AKADHLVLKP
//
