ID A0A069JWC9_9ACTN Unreviewed; 530 AA.
AC A0A069JWC9;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Peptidase {ECO:0000313|EMBL:KDQ69369.1};
GN ORFNames=DT87_19915 {ECO:0000313|EMBL:KDQ69369.1};
OS Streptomyces sp. NTK 937.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1487711 {ECO:0000313|EMBL:KDQ69369.1, ECO:0000313|Proteomes:UP000027475};
RN [1] {ECO:0000313|EMBL:KDQ69369.1, ECO:0000313|Proteomes:UP000027475}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NTK 937 {ECO:0000313|EMBL:KDQ69369.1,
RC ECO:0000313|Proteomes:UP000027475};
RA Olano C., Cano-Prieto C., Losada A., Mendez C., Salas J.A.;
RT "Draft genome sequence of marine actinomycete Streptomyces sp. NTK 937,
RT producer of the benzoxazol antibiotic caboxamycin.";
RL Submitted (APR-2014) 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:KDQ69369.1}.
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DR EMBL; JJOB01000001; KDQ69369.1; -; Genomic_DNA.
DR RefSeq; WP_037879271.1; NZ_JJOB01000001.1.
DR AlphaFoldDB; A0A069JWC9; -.
DR OrthoDB; 4498590at2; -.
DR Proteomes; UP000027475; 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; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..530
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001666219"
FT DOMAIN 425..529
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
FT REGION 29..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 530 AA; 55290 MW; 179820CB6CE78BAB CRC64;
MRTTPALRAA ALAATATVLL PLAACSDDGG GTDRGTPSAA STASPTTTPG DLSSQKLDWK
RCPAPSNAQG SGTAPSPLPG GTPWECSFMN VPLDYGDPDG RTIELALVRA RAKDQDRRIG
SLVFNFGGPG ASGVATLPAF GTAYDTLRGR YDLVSFDPRG VGRSEGVECA DDAALDARYE
MDGTPDNAKE EKAFVDDLKS YIADCEENSG EELPYVGTTN AARDMDLLRS VLGDDKLHYF
GISYGTELGG VYAHLFPKKV GRAVLDAVVD PTEDAEKSAL GQAKGFQLAL DNFTADCAER
EDCKLPGSRA QEVQDWIADL LEKLEKKPVP GLGERELTQT QATTGIASAL YSKETWPLLE
QGLDEADGQN GGLLLALADS LNGRTQNGHY DNSGAANTAI NCADSKQRFT LEQTKAALPL
FRKASPVFGD YLGWGLMSCT GWPVAGAWDT PDVSAPGAAP VLVIGNTGDP ATPYAGAKAM
AGELGKGVGV ELTYKGEGHG AYNGGSTCVQ KAVDGYLLDG KVPASGTVCA
//
