ID A0A1E5P436_9ACTN Unreviewed; 530 AA.
AC A0A1E5P436;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Peptidase {ECO:0000313|EMBL:OEJ24237.1};
GN ORFNames=AS594_06805 {ECO:0000313|EMBL:OEJ24237.1};
OS Streptomyces agglomeratus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=285458 {ECO:0000313|EMBL:OEJ24237.1, ECO:0000313|Proteomes:UP000095759};
RN [1] {ECO:0000313|EMBL:OEJ24237.1, ECO:0000313|Proteomes:UP000095759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6-3-2 {ECO:0000313|EMBL:OEJ24237.1,
RC ECO:0000313|Proteomes:UP000095759};
RA Chen X.;
RT "Complete genome sequence of Streptomyces agglomeratus strain 6-3-2, a
RT novel anti-MRSA actinomycete isolated from Wuli of Tebit, China.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088}.
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:OEJ24237.1}.
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DR EMBL; MEHJ01000001; OEJ24237.1; -; Genomic_DNA.
DR RefSeq; WP_069933280.1; NZ_MEHN01000001.1.
DR AlphaFoldDB; A0A1E5P436; -.
DR STRING; 285458.BGM19_29990; -.
DR Proteomes; UP000095759; Unassembled WGS sequence.
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; IPR000073; AB_hydrolase_1.
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; PF00561; Abhydrolase_1; 1.
DR Pfam; PF08386; Abhydrolase_4; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000095759};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..530
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009182928"
FT DOMAIN 92..268
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT DOMAIN 393..489
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
SQ SEQUENCE 530 AA; 56286 MW; 59938427921C48D3 CRC64;
MKKRAGVLIA AGVTMAALVA TVPPAVSADA GAAPGPDAGR TALVWKGCGT KTYPKLQCAS
VEVPLDHVDP RGEKITLALS RIRHTAKTFQ GPLLVNPGGP GGSGRSLAGF VAAALPGKVA
AQYDVIGFDP RGVGASEPAL DCRPGHFAAV RPDSVPRDER DERAGLDRAR AFAKACGDKY
GAVLPHIGTV SAARDLDVVR RALGARQISY FGYSYGTYLG AVYAKLHPRR VRRIVLDSVV
DPSGAWYANN LAQDHAFDAR HKAFAAWVAK HDPVYRLGGD PAEVEAKWYA MREAVRRSPA
GGKVGPAELE DTFLPGGYFN GYWPHLAEAF ASYVNEKDAA PLVAAYKQFG ATDAAGHNGY
SVYTSVQCRD AAWPRDWDTW REDNWDVHEK APFSTWNNAW YNAPCAFWPT PSLTPPDVSN
EELPPALLFQ ATEDAATPYD GGVALHRMLS RSALVVETGG GNHGVTLSGN ACLDLHLAHY
LATGEVPRRA AGGDADAVCD APADPKPLPA ERAAVPSRGG TLHGLLGFRG
//
