ID A0A1W2BNW3_9RHOB Unreviewed; 819 AA.
AC A0A1W2BNW3;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Penicillin amidase {ECO:0000313|EMBL:SMC74649.1};
GN ORFNames=SAMN06295998_104219 {ECO:0000313|EMBL:SMC74649.1};
OS Primorskyibacter flagellatus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Primorskyibacter.
OX NCBI_TaxID=1387277 {ECO:0000313|EMBL:SMC74649.1, ECO:0000313|Proteomes:UP000192330};
RN [1] {ECO:0000313|EMBL:SMC74649.1, ECO:0000313|Proteomes:UP000192330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12644 {ECO:0000313|EMBL:SMC74649.1,
RC ECO:0000313|Proteomes:UP000192330};
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 (APR-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; FWYD01000004; SMC74649.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W2BNW3; -.
DR STRING; 1387277.SAMN06295998_104219; -.
DR OrthoDB; 9760084at2; -.
DR Proteomes; UP000192330; 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:UP000192330};
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 REGION 467..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 819 AA; 90354 MW; 8507E462A708EE09 CRC64;
MVTVFRWLVR ITGAVLVLSC LVIALVYYLA SQSLPDYDKT LKVDGTTTEI EIVRDHANVP
HIFAGADRDV FFGLGYAHAQ DRLWQMMMLR RTVQGRLSEM FGARTVNIDK LLRRLDFYPL
ATRSVEAQDP RTIRALEGYA AGVNARIAEI NRDSLGRGAP EFFLFDTAIP PWRPADSVAI
VKLMALQLSG QLSTEVLRAR TSLLLPDENR LADILPDMPG PGIAALPDYA TLVPGVPRYA
KANPRDDTLL NPVKRRGFAG ASNGWAAAPS RSASGGTLLA NDPHLEFTAP STWYLARLEL
SAGGVIGATI PGIPAVLTGR SDRLGWGLTS AYVDDQDVRI EALNPDNPEE YRTPDGFKTF
ETRKSIISIK DDTPITMTLR WTDNGPVLPG THYDLDTITP PGHVASLSWT ALSPRDTSMT
AAINLMYAGS VDEALGVSED FIAPAQNLTL ADQNNVALVM VGAMPNRNEG HQSKGRLPTQ
GWRPENRWNG RLPFSDNPRF ISPAGGIVGN TNNKIVDRPF PQHVSYDWGD SQRIQRWERL
MQGREVHTRD SFIEAQLDTV STTARTLLPL IGADLWFTTE AAPEGTPERR RQDALNLLAG
WNGEMNEHLP EPLLYAAWLR ALQERLIRDD LGPLADEYDH VEPLFIERVF RDVDGASAWC
DIIRSAAIET CTDISRLALD DALVWVAETY GTALESLRWG DAHEATHDHP VLGKVAVLNY
FVNIRQSTSG GDNTLMRGRT RGTGPDPFQN THGAGYRGVY DFADPDSSVF VTATGQSGHF
LSRHYDDLGQ LWRRGEYTPM SLDTDLARAA AVGITRLTP
//
