ID A0A1F1Q3E5_9PSED Unreviewed; 769 AA.
AC A0A1F1Q3E5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Acyl-homoserine lactone acylase subunit beta {ECO:0000313|EMBL:OFS71841.1};
GN ORFNames=HMPREF3173_16495 {ECO:0000313|EMBL:OFS71841.1};
OS Pseudomonas sp. HMSC08G10.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1581141 {ECO:0000313|EMBL:OFS71841.1, ECO:0000313|Proteomes:UP000179079};
RN [1] {ECO:0000313|EMBL:OFS71841.1, ECO:0000313|Proteomes:UP000179079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMSC08G10 {ECO:0000313|EMBL:OFS71841.1,
RC ECO:0000313|Proteomes:UP000179079};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
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:OFS71841.1}.
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DR EMBL; LWMZ01000070; OFS71841.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F1Q3E5; -.
DR Proteomes; UP000179079; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:InterPro.
DR CDD; cd01936; Ntn_CA; 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; 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:SF3; ACYL-HOMOSERINE LACTONE ACYLASE PVDQ; 1.
DR PANTHER; PTHR34218; PEPTIDASE S45 PENICILLIN AMIDASE; 1.
DR Pfam; PF01804; Penicil_amidase; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..769
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009471889"
SQ SEQUENCE 769 AA; 83179 MW; C79CC50026078AA3 CRC64;
MLPRHLTHLG LAAVLLSSGL AAQALEATGE ASAQIRRTSF GVPHILAKDE RSLGYGIGYA
YAQDNLCLLA NEVLTVNGER ARYFGARGKT IEQRENLDSD TFFAWLNTDS VVNAFLQAQP
DPVRQRLEGY AAGYNRALAE RRGQGLPIEC GNGDWVRPIT SLDLAKLTRR LLAEGGIGQF
VEALVAASPP QAAERGEGRD FSAALARQAQ FASARGSNAV AVGAERSSTG GGLLLANPHF
PWEGGMRFYQ MQLTIPGQLD VMGAALPGLP LINIGFNRHL AWTHTVDTSK HFTLYRLQLD
PKDPTRYLLD GKSVPLTRQT LSVTVKGEDG QLQRVQRHVY TSSFGPVVQW PGRLDWDRQH
AYSLRDANLE NTRVLQQWDA INRADSLDRL KQAVGQIQGV PWVNTLAVDA EGRAAYLNQS
VVPYVDQALL ARCGDPAAIE PLVVLDGSRS VCQWKTDAQA AQPGIFPARL LPSLERRDFV
QNSNDPAWLA NPAQPLTGYS PLVSREGQPL GLRSRFALQR LQGAGKLGMA ELQRMVLDDE
VYAANLVLPD LLAWCQAAPS DVQAVCASLG AWNGKADLDS GVGLLHFANI VEAMAEHPES
WRVAFDPVDP QHTPRGLAVE QASVSKRVHE AALASLARLD EAGVSLDRQW GQIQQSADGT
PVPGGPQELG VYNAMHSVPA GAGKQQVVSG TSYLQLVSFT RQGPQAFGLL AFSQSSEAAS
PYASDQTRAF SAKQLAPIPF TEAQIKADPQ YRQYVIREGD KAVVAGAGH
//
