ID A0A101MZP0_9ACTN Unreviewed; 517 AA.
AC A0A101MZP0;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Protease {ECO:0000313|EMBL:KUM83877.1};
GN ORFNames=AQI94_33550 {ECO:0000313|EMBL:KUM83877.1};
OS Streptomyces pseudovenezuelae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX NCBI_TaxID=67350 {ECO:0000313|EMBL:KUM83877.1, ECO:0000313|Proteomes:UP000053039};
RN [1] {ECO:0000313|EMBL:KUM83877.1, ECO:0000313|Proteomes:UP000053039}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40212 {ECO:0000313|EMBL:KUM83877.1,
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:KUM83877.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMWM01000040; KUM83877.1; -; Genomic_DNA.
DR RefSeq; WP_031055640.1; NZ_KQ948151.1.
DR AlphaFoldDB; A0A101MZP0; -.
DR OrthoDB; 3930956at2; -.
DR Proteomes; UP000053039; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; 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 Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:KUM83877.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 124..279
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT DOMAIN 409..512
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
FT REGION 355..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 517 AA; 54996 MW; D6EBD185D6960A1C CRC64;
MSDAHPIRSR RQGFSVGARI LAVFVLAVFG GVYAWLQYDA HGPSAEPRTE FTANNPPAGL
PTALTVGQHL HWSRCTSPPI ARTGYDCAVM KAPLDYRKPR GRTIDVALIR RKATGPNARR
IGSLVLNFGG PGVSGVSGLP QRLNQYRPLL DRYDLVSFDP RGVGATIPVR CGKTADDTGF
DGADACAEHS GAVLPYISTA HTARDLDLMR YLLGDERLHY FGVSYGTALG AVYAHLHPSN
VGRLVLEASV DPTEDLDEEQ ESQVKAVQAA FDRFAAHCAA RIRHCATGDG PEEAARRMAR
LAGRLEKKPA PAGGGRTLDA DDLAYAVSDH LALGTDGWPT LAKALTALID HNDGRPLSEG
ADNIGSADRA APPRDNSRAA LTAITCADSS LRPGFERLAK DAARVKAASP VFGAAWSTGV
YLCYDWPFDG ERPTLQVNAE GAAPVLVVGG TGDPTTPYPG ARHMARALGD RVGVLLTAEE
EGHGTYPQNR CVSETVDQYL RTGRTPAPGT VCRGSMS
//
