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Database: UniProt
Entry: A0A1X6Y5M7_9RHOB
LinkDB: A0A1X6Y5M7_9RHOB
Original site: A0A1X6Y5M7_9RHOB 
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
//
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