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Database: UniProt
Entry: A0A101CZH1_9RHOB
LinkDB: A0A101CZH1_9RHOB
Original site: A0A101CZH1_9RHOB 
ID   A0A101CZH1_9RHOB        Unreviewed;       820 AA.
AC   A0A101CZH1;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Penicillin acylase {ECO:0000313|EMBL:KUJ86079.1};
GN   ORFNames=AVO45_03705 {ECO:0000313|EMBL:KUJ86079.1};
OS   Ruegeria marisrubri.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=1685379 {ECO:0000313|EMBL:KUJ86079.1, ECO:0000313|Proteomes:UP000053791};
RN   [1] {ECO:0000313|EMBL:KUJ86079.1, ECO:0000313|Proteomes:UP000053791}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZGT118 {ECO:0000313|EMBL:KUJ86079.1,
RC   ECO:0000313|Proteomes:UP000053791};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-2015) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUJ86079.1}.
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DR   EMBL; LQBQ01000001; KUJ86079.1; -; Genomic_DNA.
DR   RefSeq; WP_068344530.1; NZ_LQBQ01000001.1.
DR   AlphaFoldDB; A0A101CZH1; -.
DR   STRING; 1685379.AVO45_03705; -.
DR   OrthoDB; 9760084at2; -.
DR   Proteomes; UP000053791; 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:UP000053791};
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;  90686 MW;  46D9875303562FC2 CRC64;
     MSLLFRWLLR IAAGLVAMVV AAVALVYFLA SQSLPDYDQT LEVDGLSAPV EIVRDNANVP
     HIFGASDPDV FFGLGYAHAQ DRLWQMTMLR RTVQGRLSEV FGKRTVTVDK LLRRLDLYRL
     ALQSVEAQDD YTKAALKAYA AGVNARLAEV NEEALGRGAP EMFLFNAPVA PWQPGDSIAI
     IKLMGLQLSG HLEEEVLRAR TSLMLEDPAR LSDILPDDPG SGIAALPEYA SLFPDLPRYA
     ETIPMPEDPL SPFPRRGLAG ASNAWTAAPS RSASGGTLLA NDPHMGFSAP AAWYLARLEL
     ANGGVIGASI PGVPTILTGR SDRLGWGLTS SYLDDQDLFV EKLNPDDPEE YLTPDGYKRF
     QTRPSIIEIK DAPPITLTLR WTENGPVLPG TFYNLGTITP RGHVMSLSWT LLSPRDTSMS
     ASMALMNASN VREAIAATEG FIAPSQNLSL ADRSTIAMKT IGAMPKRDPR HHSKGRLPSQ
     GWLPENRWQG RLPYSSNPEF VSPAGGLLGN TNNKIIDRAF PEHVSFAWGD TQRVHRWEKL
     MQDREVHTRD SFIEAQLDTV SFTARSLLPL IGADLWYTGE SAPEGTPERQ RQIALALLAE
     WNGEMNEYMP EPLIYAAWIR ALQKRLIEDD LGPLADEFKH VEPLFIERVY RDIDGASAWC
     DVRQSAPVET CTDMARMALD DALIWIAERY GSQLESLRWG DAHQAAHDHQ VLGEVPLLRY
     FVNIRQSTSG GDNTLQRGRT SGEDPNPFLN IHGAGYRGVY DFADPDSSVF ITSTGQSGHF
     LSRYYDDQAQ LWRRGEYVPM SLDAELARAA AVGVTHLIPR
//
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