ID A0A1X6Y5M7_9RHOB Unreviewed; 820 AA.
AC A0A1X6Y5M7;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Acyl-homoserine lactone acylase QuiP {ECO:0000313|EMBL:SLN11273.1};
DE EC=3.5.1.97 {ECO:0000313|EMBL:SLN11273.1};
GN Name=quiP {ECO:0000313|EMBL:SLN11273.1};
GN ORFNames=RUM8411_00138 {ECO:0000313|EMBL:SLN11273.1};
OS Ruegeria meonggei.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=1446476 {ECO:0000313|EMBL:SLN11273.1, ECO:0000313|Proteomes:UP000193778};
RN [1] {ECO:0000313|EMBL:SLN11273.1, ECO:0000313|Proteomes:UP000193778}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8411 {ECO:0000313|EMBL:SLN11273.1,
RC ECO:0000313|Proteomes:UP000193778};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-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}.
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DR EMBL; FWFP01000001; SLN11273.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X6Y5M7; -.
DR OrthoDB; 9760084at2; -.
DR Proteomes; UP000193778; 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, ECO:0000313|EMBL:SLN11273.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001227-2};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT TRANSMEM 7..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 262
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT BINDING 195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 334
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 337
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ SEQUENCE 820 AA; 90312 MW; 465EC2C4A52FAC0E CRC64;
MGFVFRWLVR ITSGLILLTL AAVALVYFLA SQSLPDYDQT VEVNGLSAPV EIIRDTANVP
HILAGNDPDV FFGLGYAHAQ DRLWQMTMMR RTAQGRLSEV FGARTVSIDK LLRRLDLYGL
AHRSVEEQDD YTKAALRAYS AGVNARLDEI NEAALGRGAP EMFLFNAPVS PWQPGDSIAV
IKLMSLQLSG HLQDEVLRAR TSLMLNNPAR LVDILPDVPG PGITALPEYA ALFPNVPRYA
RGTPMPDTPL SPVSKRGLAG ASNAWTAAPS RSASGGTLLA NDPHLGFTAP GVWYLARLEL
SKGGVIGATI PGIPAVMTGR SDRLGWGLTS SYLDDQDIHI ERLNPDNSEE YLTPDGFKRF
RTRPSIIEIK DEAPITLTLR WTENGPVLPG SRYDLDTITP PGHVASLSWT ALSARDTSMT
ASMALMNADN VEQAIDVAEL FTAPSQNLSL VDKTAIGMKL IGAMPKRDLR NQSRGRIPTP
GWLAENMWQG RLPYADNPEF VAPVGGILGN TNNKIIDRPF PEHVSYEWGD TQRIHRWERL
MQSREVHTRD SFIEAQLDTV SFTARSLLPL IGADLWFTGA SAPEGTPDRQ RRIALSLLAE
WNGEMNEHLP EPLIYAAWLR ALQARLISDE LGPLAAEYNH VEPLFIERVY RDIDGASVWC
DVRQSAPTET CTDMARLALD DALIWISENY GGALQSLRWG DAHQATHDHP VLGKVPVLRF
FVNIRQSTSG GDNTLLRGRT SGEGPDPFQN VHGAGYRGVY DFADPDSSVF ITATGQSGHF
LSRYYDDQAQ LWRRGEYIPM SLDLDLARAA AVGVTNLIPR
//