ID A0A239E8M8_9RHOB Unreviewed; 820 AA.
AC A0A239E8M8;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Penicillin amidase {ECO:0000313|EMBL:SNS40976.1};
GN ORFNames=SAMN05421757_10229 {ECO:0000313|EMBL:SNS40976.1};
OS Tropicimonas sediminicola.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Tropicimonas.
OX NCBI_TaxID=1031541 {ECO:0000313|EMBL:SNS40976.1, ECO:0000313|Proteomes:UP000198426};
RN [1] {ECO:0000313|EMBL:SNS40976.1, ECO:0000313|Proteomes:UP000198426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29339 {ECO:0000313|EMBL:SNS40976.1,
RC ECO:0000313|Proteomes:UP000198426};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-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; FZOY01000002; SNS40976.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239E8M8; -.
DR OrthoDB; 9760084at2; -.
DR Proteomes; UP000198426; 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:UP000198426};
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 494..513
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"
FT BINDING 522
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ SEQUENCE 820 AA; 90572 MW; A5E181900D1AD7F7 CRC64;
MEGLFRWTLR LFMVLVVLIT GAASLAYYFA AGSLPDYSAT YRLRGLSAPV EIVRDNANVP
HILGQTDEDS FFGLGFVHAQ DRLWQMTLLR RTAQGRLSEL FGARTVQTDE LMRRLDIYRL
ASASVEAQDA ETQSALRAYA AGVNAWIETV NSEALGRGAP EFFLFSPEIA PWQPADSIAI
AKLMALDMTA HMQNEILRAR ASLVLPSERL IDLMPDVPAG LEGTLPADYG ALFPDLPRHA
RASTWQPDPL SPVGRAAFAG ASNVWAAAPE RAAAGAALLA NDPHMQLTAP SIWYLARLEL
SSGGVIGGTI PGMPIVLSGR SDRLAWGIAV AYADDQDLHM EELNPANTQQ YRTPNGWKDF
RTERSIIRVA EEAPVTITLR WSDNGPVLPR SHFDLDQVTP ANHVASLSWT GLDAADTSLS
AAIRMMRANS VAEAVEAGRD FIVPALNVVL ADGETIGMQV FGAIPDRDPA HYSQGRMPSL
GWMPENVWRG RKPYESNPRR LSPASGIVGN TNNRTTEAPF PDHVSFVWGD TQRIQRWRKL
MAEREVHTRE SFIAAQLDTV SVTARSLLPL IARELWYTGE AAEDGTPERQ RQVALELLAN
WNGEMNEHLP EPLIYAAWLR QLQHKLIVDE IGQLENEFPH PDPIFIERVF RDIDGASAWC
DIQQSTITET CADTARIALD EALLWIGERY GTALESLRWG DAHQARHDHL ILGEIPVLQW
FVNIHQSTSG GDNTMQRALT VGTGPDPFDN VHAAGYRGVY DFADPDASVF VTATGQSGHP
LSRHYDDLGE RWRRGEYIPM SLNPELARAG AVGTTMLEPR
//
