ID A0A132BXL2_9RHOB Unreviewed; 823 AA.
AC A0A132BXL2;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Penicillin acylase 2 {ECO:0000313|EMBL:KUP92557.1};
DE EC=3.5.1.11 {ECO:0000313|EMBL:KUP92557.1};
GN Name=acyII {ECO:0000313|EMBL:KUP92557.1};
GN ORFNames=TRIHO_25270 {ECO:0000313|EMBL:KUP92557.1};
OS Tritonibacter horizontis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Tritonibacter.
OX NCBI_TaxID=1768241 {ECO:0000313|EMBL:KUP92557.1, ECO:0000313|Proteomes:UP000068382};
RN [1] {ECO:0000313|EMBL:KUP92557.1, ECO:0000313|Proteomes:UP000068382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O3.65 {ECO:0000313|EMBL:KUP92557.1,
RC ECO:0000313|Proteomes:UP000068382};
RA Poehlein A., Giebel H.A., Voget S., Brinkhoff T.;
RT "Genome sequence of the marine Rhodobacteraceae strain O3.65, Candidatus
RT Tritonibacter horizontis.";
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:KUP92557.1}.
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DR EMBL; LPUY01000074; KUP92557.1; -; Genomic_DNA.
DR RefSeq; WP_068244066.1; NZ_LPUY01000074.1.
DR AlphaFoldDB; A0A132BXL2; -.
DR PATRIC; fig|1768241.3.peg.2648; -.
DR OrthoDB; 9760084at2; -.
DR Proteomes; UP000068382; Unassembled WGS sequence.
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:SF3; ACYL-HOMOSERINE LACTONE ACYLASE PVDQ; 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:KUP92557.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001227-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000068382};
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 264
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT BINDING 198
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 336
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 339
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ SEQUENCE 823 AA; 90639 MW; 8FA92C5A713D6447 CRC64;
MARLFRWLLR LTAGSILLGL LGGILVYFLA SQSLPNYDKE ITLPGPTAPV EIVRDHANVP
HIFGSFGASD EDVFFGLGYA HAQDRLWQMA VMRRTAQGRL SEVFGARTVK TDSFLRRLDL
YRLARSSVSA QSPETLRALE AYSAGVNARL QEINERALGR GAPEMFLFNM PIAPWQPADS
IALVKLMALQ LSPHMQEEIL RAQTSIALDD PARLRDILPD APGAGTATLP EYTNLFPQLQ
DRPQNRTELA SMMPVAERGL AGASNAWAAA PSRSATGGTL LANDPHLKLT APGTWYLARL
ELGTGGVIGG TIPGIPAVLT GRSQHLGWGI TSSYLDDQDL FIEKVNPDNS QQYLSPNGYK
DFVSRPSIVQ IKGAEPLTLT LRWTENGPVL PGSLFNLAAI TPPGHVVSLG WTALSETDTS
MTAALELMRA DSISQAIEIG EGFVAPSQNL TLADGQTVAM KTVGTMPDRA LGNQSQGRLP
NQGWRRENKW QGRLPYTANP EFIDPRGGIV GNTNNKLLDR PFPNHVSFEW GDTQRINRWR
RLMQMREVHT RDSFIEAQLD TVSYSARTLL PLIGANLWFT GEAAPSGTPA RQRQIALSLL
AEWNGEMNEH LPEPLIYASW VRALQKRLID DELGALADAF SRVDPLFLER VFRDVDGAAI
WCDVRRSTPV ETCSDMARLA LDDALVDIDE NYGNALEALR WGDAHQATHD HEVLGEVPLL
RYFVNIRQST SGGDNTLQRG LTSAAAIRPF ENVHAAGYRG VYDFADPDSS LFIIATGQSG
HFLSRFYDDM AQFWRRGEYL PMSLDEDLAR AAAVGVTRIL PRN
//
