ID A0A101N8V2_9ACTN Unreviewed; 513 AA.
AC A0A101N8V2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Peptidase {ECO:0000313|EMBL:KUM88604.1};
GN ORFNames=AQI94_08545 {ECO:0000313|EMBL:KUM88604.1};
OS Streptomyces pseudovenezuelae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX NCBI_TaxID=67350 {ECO:0000313|EMBL:KUM88604.1, ECO:0000313|Proteomes:UP000053039};
RN [1] {ECO:0000313|EMBL:KUM88604.1, ECO:0000313|Proteomes:UP000053039}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40212 {ECO:0000313|EMBL:KUM88604.1,
RC ECO:0000313|Proteomes:UP000053039};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces pseudovenezuelae DSM 40212, type
RT strain for the species Streptomyces pseudovenezuelae.";
RL Submitted (OCT-2015) 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:KUM88604.1}.
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DR EMBL; LMWM01000009; KUM88604.1; -; Genomic_DNA.
DR RefSeq; WP_031058886.1; NZ_KQ948145.1.
DR AlphaFoldDB; A0A101N8V2; -.
DR OrthoDB; 4498590at2; -.
DR Proteomes; UP000053039; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..513
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007101231"
FT DOMAIN 408..512
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
FT REGION 45..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 513 AA; 54522 MW; 6FAF73ACEE02AF4B CRC64;
MPTPSRLRVA ALTATALLLA CALAGCADSQ EEDLSAQKLS WKDCPAPSPA EGGGDAPSPL
PGGEEWQCAT LKAPLDWAKP KGDTIGIALI RARTSGPENR RIGSLVFNFG GPGGSGVSTL
PAFGSDYAKL RTRYDLVSFD PRGVGRSAPV ECLNDLQLDV YFEQDGTPDD SAERAKLLDN
TKEFNAACEE NSQKMLPHVR TTDAARDMDL MRQVLGDDKL HYFGISYGTE LGGVYAHLFP
KHVGRAVFDG VVDPTQNSEQ GSLGQARGFQ LALDNFAEDC TSQPTDCPVG DTAQDVKDRI
AKLLADLDRK PIPGIGQRVL TQTAATNGIA QALYSKDFWE YLTEGLEQAY DGDGRVLMVL
SDSMNGRSEN GEYSNITAAN ISINCADDKP RYTTAAVERR LPEFRAASPL FGDFLAWSLL
TCTDWAVAGA ADHPDVSAAG SAPILVVGNT GDPATPYEGA RKMVEALGRG VGVELTYKGQ
GHGAYDSKNK CVQDAVNGYL LTGKVPAAGT VCS
//
