ID Q165Q9_ROSDO Unreviewed; 821 AA.
AC Q165Q9;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Penicillin acylase, putative {ECO:0000313|EMBL:ABG32284.1};
DE EC=3.5.1.11 {ECO:0000313|EMBL:ABG32284.1};
GN Name=acy {ECO:0000313|EMBL:ABG32284.1};
GN OrderedLocusNames=RD1_2752 {ECO:0000313|EMBL:ABG32284.1};
OS Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp.
OS (strain OCh 114)) (Roseobacter denitrificans).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseobacter.
OX NCBI_TaxID=375451 {ECO:0000313|EMBL:ABG32284.1, ECO:0000313|Proteomes:UP000007029};
RN [1] {ECO:0000313|EMBL:ABG32284.1, ECO:0000313|Proteomes:UP000007029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33942 / OCh 114 {ECO:0000313|Proteomes:UP000007029};
RX PubMed=17098896; DOI=10.1128/JB.01390-06;
RA Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H.,
RA Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K.,
RA O'huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T.,
RA Touchman J.W.;
RT "The complete genome sequence of Roseobacter denitrificans reveals a
RT mixotrophic rather than photosynthetic metabolism.";
RL J. Bacteriol. 189:683-690(2007).
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; CP000362; ABG32284.1; -; Genomic_DNA.
DR RefSeq; WP_011568901.1; NZ_FOOO01000002.1.
DR AlphaFoldDB; Q165Q9; -.
DR STRING; 375451.RD1_2752; -.
DR MEROPS; S45.003; -.
DR KEGG; rde:RD1_2752; -.
DR eggNOG; COG2366; Bacteria.
DR HOGENOM; CLU_011790_0_1_5; -.
DR OrthoDB; 9760084at2; -.
DR Proteomes; UP000007029; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008953; F:penicillin amidase activity; IEA:UniProtKB-EC.
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:ABG32284.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001227-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000007029};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT TRANSMEM 7..29
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 821 AA; 91229 MW; 97870BB27F8CABFA CRC64;
MAQVFTWLLR IAGTLVALIV LAIVMMYYLG TRSLPDYDDV LDVPYLNAPV EIVRDNANVP
HIFGSNDEDV FYALGYAHAQ DRLWQMTLMR RTAQGRLSEV FGRETLDIDN IMRRLDIYPL
AVASLEAQDE RTMRILRAYA TGVNARLDQV NDEALGRGAP EMFLFNAPVA PWRPADSMAI
IKLMGVRLAR HLDTEVMRAR MIKALPNPER IIDILPDAPG TGTAALPEYA HLLGPPAHFA
GRSDIHTHPL SPFAPAEMAG ASNVWAAAPS RSASGGTLLA NDPHLGFSAP GIWYLARLEL
QSGGVIGGTI PGMPIVLTGR SDRLGWGLTS AGMDDQDLYL EELHPENKDE YRTPSGFKKL
TSRKSIINIK DEPPVTITMH WTDNGPVLPG RLYNLGDVMQ PGHAISLSWT LLSPNDTSMM
AALRLMEAQS VEEGFALMED YIAPAQNLML VDAENIGMKM IGAMPRRDAR HETQGRLPSY
GWKEENRWQG TFPYASNPEF IAPAGGILGN TNNKVVERPF PNHVSFDWGD TQRVKRWQRL
MQAREVHTRD SFIEAQLDAV STSARTLLAL IGTELWFTGE AAEEGTPLRR RQRALSLLAE
WSGEMNEHMP EPLIYSAWVR SLQLRMVQDE LGPLAVELTH VEPLFIERAF RDVEGASVWC
DVIQSQPIET CADMARLALD DALIWIGENW GQSLETLRWG DAHQATHDHP VLGDVPLLRY
FVNIRQSTNG GDNTLQRGLT RGYGDNPFAN VHGAGYRGVY DFADPDSSVF VTSTGQSGHF
LSRHYDDMAQ LWRRGEYIPM SLDEDLARAG AVGVTTLRPA P
//
