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Database: UniProt
Entry: A0A291Q1Q8_9ACTN
LinkDB: A0A291Q1Q8_9ACTN
Original site: A0A291Q1Q8_9ACTN 
ID   A0A291Q1Q8_9ACTN        Unreviewed;       816 AA.
AC   A0A291Q1Q8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Peptidase S45, penicillin amidase {ECO:0000313|EMBL:ATL25671.1};
GN   ORFNames=KY5_0653c {ECO:0000313|EMBL:ATL25671.1};
OS   Streptomyces formicae.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1616117 {ECO:0000313|EMBL:ATL25671.1, ECO:0000313|Proteomes:UP000221011};
RN   [1] {ECO:0000313|EMBL:ATL25671.1, ECO:0000313|Proteomes:UP000221011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KY5 {ECO:0000313|EMBL:ATL25671.1,
RC   ECO:0000313|Proteomes:UP000221011};
RA   Holmes N.A., Devine R., Qin Z., Seipke R.F., Wilkinson B., Hutchings M.I.;
RT   "Complete Genome Sequence of Streptomyces formicae KY5, the formicamycin
RT   producer.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S45 family.
CC       {ECO:0000256|ARBA:ARBA00006586}.
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DR   EMBL; CP022685; ATL25671.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A291Q1Q8; -.
DR   KEGG; sfk:KY5_0653c; -.
DR   Proteomes; UP000221011; Chromosome.
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   PANTHER; PTHR34218:SF3; ACYL-HOMOSERINE LACTONE ACYLASE PVDQ; 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.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000221011};
KW   Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..816
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038697998"
SQ   SEQUENCE   816 AA;  87033 MW;  1B06DC1EE47BD547 CRC64;
     MPRVTRLPAR IRGAVSSLVA GITLVGLTAL PASTTPTHTA AGSDRRAVIQ YTEYGVPHIT
     ADDYPGLGYG YGYASAKDNV CVLADAYVTV NAERSRYFGA DAPANAGVGV AADSLTSDLY
     FQRLKDSGTV ERLVDKPPPL GPEPEVAQLV RGYVQGYNRY VAEADARGGI TDPACRGKEW
     VKPIAAMDVY RQIHAVTTMS GSGTFMDGIA GARPPARAAA APRRSADPAA GLAAAVRAAR
     GDGELGSNAL AIGAEGTRGS RGVLLANPHF PWQGMRRMWQ SQLTIPGRLD VSGASLLGFP
     AVLIGHNRDV AWTHTVATAS TYGLYEVPLV PGDPTRYLVD GTPEQMKSHR VRVRVKEKDG
     TTGTVERTLW DTRYGPVLGA GPGGFPLPWG KDTAYTLRDA NSTNLRALNS WLGLGRTTST
     EDVRRSQART QGLPWINTLA VDRKGSAYYA DMQVVPHVTD ELAKRCSTPL GERLLATSGV
     PVLDGGRGAC AWGTDKDAVE PGLLGPGRLP RLIRDDYVTN SNNSPWLANP RSPLTGYPRV
     VGDIGTPRSL RTQEGLLSVQ RRIAGTDGLP GKGFSRATME RMLFRDHSRA AELAGADTAT
     MCRSFPGGTA PSTHGPVDVS SACRALADWD GRYSSDSRGS LLFARFVAKA AGVKDGPWKV
     PFDPSDPLRT PRTLAADKPE VQQAFGDAAA ELRAADIPLD ARLGDHQYVV RDGKRLPIHG
     GPHEAGVLNV ITPRALGAGT PDVATGSSFL QVTEFPAKGA PRTSSLLTYG QSADPTSPHH
     ADQTRLYAKG RWVRERFTQR EILDSPQLRT HILTGK
//
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