ID A0A2U9P808_STRAS Unreviewed; 509 AA.
AC A0A2U9P808;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Peptidase {ECO:0000313|EMBL:AWT45354.1};
GN ORFNames=DMT42_25775 {ECO:0000313|EMBL:AWT45354.1};
OS Streptomyces actuosus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1885 {ECO:0000313|EMBL:AWT45354.1, ECO:0000313|Proteomes:UP000247634};
RN [1] {ECO:0000313|EMBL:AWT45354.1, ECO:0000313|Proteomes:UP000247634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25421 {ECO:0000313|EMBL:AWT45354.1,
RC ECO:0000313|Proteomes:UP000247634};
RA Liu W., Sun F., Hu Y.;
RT "The complete genome sequence of a nosiheptide producer Streptomyces
RT actuosus ATCC 25421: deducing the ability of producing a new class III
RT lantibiotics.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088}.
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DR EMBL; CP029788; AWT45354.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9P808; -.
DR KEGG; sact:DMT42_25775; -.
DR OrthoDB; 4498590at2; -.
DR Proteomes; UP000247634; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013595; Pept_S33_TAP-like_C.
DR PANTHER; PTHR43248; 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE; 1.
DR PANTHER; PTHR43248:SF29; AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF08386; Abhydrolase_4; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000247634};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..509
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038729478"
FT DOMAIN 403..508
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
FT REGION 22..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 509 AA; 53529 MW; 4AC3E343A84967C9 CRC64;
MARVARWTVL GTAAALLVAG CSGGSSSDDG KKGTESTAAG SPSNLPASLA SQKLDWGRCR
ATADAPAPGS DWQCATLKAP LDWSDPGGKT IRLALIRSKA RGDDRIGSLL FNFGGPGGSG
VSGMPSYAST VSALHERYDL VSWDPRGVGG SQGVRCRSDK EIQASEVLDA TPDTPAEETA
YLKDATDFGK GCRQAAGKLM EHVSTTDTAR DMDLMRQVLG DAKTHYFGIS YGTELGGVYA
HLFPKNVGRL VLDAVVDPSA DTVGHAENQA RGFQRALDDY LKSTGQDPKK GSREIADLLK
RLDAEPLPTG SGRKLTQTLA VTGIVLPLYS KDSWPTLTSA LEAAQEGDGS ELLALADGYN
ERDASGHYGT TTHSQRVISC LDDKERPTPE ETKRRLPAFE KISPVFGAFL GWDTAGWCHD
WPVAGQHETP EVSAPGAAPV LVVGNTGDPA TPYEGARRMA DELGKGVGVV LTWKGEGHGA
YGSGSDCVDS TVNAYLLEGT VPDDGKVCS
//
