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
//