ID A0A2B8AZR5_9ACTN Unreviewed; 950 AA.
AC A0A2B8AZR5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Penicillin acylase {ECO:0000313|EMBL:PGH51201.1};
GN ORFNames=CRI70_08070 {ECO:0000313|EMBL:PGH51201.1};
OS Streptomyces sp. Ru87.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2044307 {ECO:0000313|EMBL:PGH51201.1, ECO:0000313|Proteomes:UP000222409};
RN [1] {ECO:0000313|EMBL:PGH51201.1, ECO:0000313|Proteomes:UP000222409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ru87 {ECO:0000313|EMBL:PGH51201.1,
RC ECO:0000313|Proteomes:UP000222409};
RA Amin D.H., Borsetto C., Abolmaaty A., Tolba S., Abdallah N.A.,
RA Wellington E.M.H.;
RT "Draft genome sequence of Streptomyces sp. Ru87 isolated from Egyptian
RT soil.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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:PGH51201.1}.
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DR EMBL; PDIX01000107; PGH51201.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B8AZR5; -.
DR OrthoDB; 5240333at2; -.
DR Proteomes; UP000222409; Unassembled WGS sequence.
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 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 InterPro; IPR006311; TAT_signal.
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 SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000222409};
KW Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..40
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 41..950
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039508289"
SQ SEQUENCE 950 AA; 102187 MW; 0745FE428AA98E7F CRC64;
MRRSLPLPAT RRTSRPRRAL TATALLALAA GLLSPLPRAA AAESTAPSAS TAAPVTDHCE
GQCSDILPPG SNGNTTLAEI LAHRTLGTRP AHSSDQLGPY NDLVAGHTSL TDGKLADFFN
DASFGVPEDQ VESVTRPRDD VTITRDKKTG VPHIKGTTRE GTEFGAGYAA AQDRLWLMDL
FRHIGRGELT PFAGGAEGNQ GLEQQFWPQA PYTEEDLQSQ IDRIAASGER GELAMADAQA
YIDGINAYAQ KAKKGRYFPG EYVLTGHIGP ITNIGEIEPF KLTDMVALAS VVGALFGGGG
GGEVQAALSL LAAQEKYGTQ KGTEVWESFR QRNDPEAVLT LHDGSSFPYA GKPDKARGTA
MPDPGSVTPE QLVFDREGAA KKDAEAAVKV PSHLKPLRNM HDDGVLPADL FGKPHGMSNA
LMVSGKHTAA GNPVAVFGPQ TGYFAPQLLM LQELQGPGIS ARGASFAGVG MYVQLGRGQD
YAWSATSANQ DIIDTYAVEL CEPDGSAPAK ESLHYVNHGS CEPMEKLERR NAWKPSIADS
TAEGSYRMQV YRTDYGMVTH RATVDGKPVA YTSLRSTYRH EADSIIGFQM FNDPGYVKDA
ESFQRAAEHI GYTFNWFYAD SRDTAYFNSG DNPVRAEGVD ASLPVRAEPA YEWQDFSPEH
NTAAYTPAAE HPQSVNQDYY VSWNNKQARD YTSAGFGFGS VHRGDLLDTR VKKLVEQGGV
TRASLTRVMA DAGLTDLRGE AVLPSLLKVL RSESITDPAA AEAVQQLESW LDAGAKRRET
SAGSKTYAHA EAIRTMDAWW ARLIEGQFKP GLGDGLYDAL RANLAVDEPP SAGHGPTGGH
AGSAFLAGWW SYADKDLRKV LGEPVEGALG DTYCGGGELS ACRDVLLDTL TRAAATPATE
VYPGDENCEP GDQWCADAVI HRPVGGLTHD AAHWQNRPTY QQVVEFPSHR
//
