ID A0A1Q4VIX8_9ACTN Unreviewed; 963 AA.
AC A0A1Q4VIX8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Penicillin amidase {ECO:0000313|EMBL:OKH97780.1};
GN ORFNames=A6A06_31940 {ECO:0000313|EMBL:OKH97780.1};
OS Streptomyces sp. CB02923.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1718985 {ECO:0000313|EMBL:OKH97780.1, ECO:0000313|Proteomes:UP000185893};
RN [1] {ECO:0000313|EMBL:OKH97780.1, ECO:0000313|Proteomes:UP000185893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB02923 {ECO:0000313|EMBL:OKH97780.1,
RC ECO:0000313|Proteomes:UP000185893};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKH97780.1}.
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DR EMBL; LWKZ01000028; OKH97780.1; -; Genomic_DNA.
DR RefSeq; WP_073768800.1; NZ_LWKZ01000028.1.
DR AlphaFoldDB; A0A1Q4VIX8; -.
DR STRING; 1718985.A6A06_31940; -.
DR OrthoDB; 9759796at2; -.
DR Proteomes; UP000185893; 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; 2.
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:UP000185893};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT TRANSMEM 26..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..777
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 359
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT BINDING 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 437
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 440
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ SEQUENCE 963 AA; 104830 MW; 8172DF64B9FD8C8E CRC64;
MPANKSAPAP DKAAKKPKKK GRRGRLVAIT VVLLLVAGIG YGAFWGVSTV RASYPQTTGS
LKLAGLTAPV DVSRDGNGIP QIYADTDEDL FRAQGFVQAQ DRFWEMDVRR HMTAGRLSEM
FGQSQVDTDA FLRTLGWHDV AQREYDTKLS PETKKYLQAY SDGVNAYLKD HEGSALSLEY
AALGFQNDYK PHKWTPVDSV AWLKAMAWDL RGNMQDEIDR ALMTSRFSPT QIDQLYPKYP
AKRNRPIVEG GAVDPATKEF DAKATPSGGS QNNSGQSNSG QSNSGLNSGT GTGTGSGTGT
GGGAGTRTGQ GTGTGTGTGT SLHSASSATQ GVKSQLASVS KSLEQIPALL GPNGNGIGSN
SWVVSGAHTT TGKPLLANDP HLAPQMPSLW YQMGLHCRTT SAKCNYDVSG YTFSGMPGVV
IGHNQDISWG MTNLGADVTD LYLEKINANG YLSKDKLQPY KTRKETIKVA GGADREITVR
STDNGPLISD RDDEMSRVGK QAPVGNAAPD RGDGYGVSLR WTALEPGKSM DAVFELNRAK
NWTDFRKAAA DFEVPSQNLI YADTKGNIGY QAPGRIPIRG KGYDGTLPAP GWDPKARWDG
YVPQKALPNE YNPARGYIVT ANQAVVDPDK YPYLLTKDWG YGARSQRIND LIQSKIKDGG
KVSTDDMQTM QMDNSSEIAK LLTPYLLKIN VDDAYVREAQ KLLEGWDYTQ EPDSAAAAYF
NAVWRNTLKL AFGNKMPKEL RVEGQCLNVR AADDTGPADD QDRPVRECGE RAPDQAQPDG
GDRWYEVVRS IIEDPKNDWW KTESRPGRVQ DANRDQLLGH AMRDARYELT SKLGKNVDNW
SWGRLHQMFL KNQTLGTSGP GILQGLFNRG PWNLGGGEAA VDATGWNAAG GYGVTWVPSM
RMVVNLADLD KSRWINLTGA SGHAYSSHYY DQTDKWAKGE LLPWAFSQKA VKAAAKDTLT
LSP
//
