ID S5V990_STRC3 Unreviewed; 521 AA.
AC S5V990;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Protease {ECO:0000313|EMBL:AGS71689.1};
GN ORFNames=B446_24390 {ECO:0000313|EMBL:AGS71689.1};
OS Streptomyces collinus (strain DSM 40733 / Tue 365).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1214242 {ECO:0000313|EMBL:AGS71689.1, ECO:0000313|Proteomes:UP000015423};
RN [1] {ECO:0000313|Proteomes:UP000015423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40733 / Tue 365 {ECO:0000313|Proteomes:UP000015423};
RA Ruckert C., Szczepanowski R., Goesmann A., Pross E.K., Musiol E.M.,
RA Blin K., Wohlleben W., Puhler A., Weber T., Kalinowski J.;
RT "The complete genome sequence of Streptomyces collinus Tu 365.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AGS71689.1, ECO:0000313|Proteomes:UP000015423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40733 / Tue 365 {ECO:0000313|Proteomes:UP000015423};
RX PubMed=24140291; DOI=10.1016/j.jbiotec.2013.10.004;
RA Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Iftime D.,
RA Musiol E.M., Blin K., Wohlleben W., Puhler A., Kalinowski J., Weber T.;
RT "Complete genome sequence of the kirromycin producer Streptomyces collinus
RT Tu 365 consisting of a linear chromosome and two linear plasmids.";
RL J. Biotechnol. 168:739-740(2013).
CC -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088}.
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DR EMBL; CP006259; AGS71689.1; -; Genomic_DNA.
DR RefSeq; WP_020942119.1; NC_021985.1.
DR AlphaFoldDB; S5V990; -.
DR STRING; 1214242.B446_24390; -.
DR KEGG; sci:B446_24390; -.
DR PATRIC; fig|1214242.5.peg.4995; -.
DR eggNOG; COG0596; Bacteria.
DR HOGENOM; CLU_013364_3_1_11; -.
DR Proteomes; UP000015423; Chromosome.
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; 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 Protease {ECO:0000313|EMBL:AGS71689.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000015423};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..521
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004532881"
FT DOMAIN 415..520
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
FT REGION 22..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 521 AA; 55049 MW; A2F166D70EFDF953 CRC64;
MSRFLRWTAA VAAALLVAGC GGSSGGGQEE GKGAAGGPGP ARKGTGSSPP ASPPPALPSS
LTSQRPDWHT CKATEGSAAP GDAWRCATLR VPLDWSKPGG TTIGLALMRS RATGSGRIGS
LLFNFGGPGG SGLSMMPYYA ATVPKLHERY DLVSWDPRGV GASEGVRCRG DRAIEKAEQV
DATPDTPAEE RAYLRDAADF GQGCRRAAGA LLAHVSTTDT ARDMDLMRQV LGDRTTHYFG
ISYGTELGGV YAHLFPQRVG RLILDAVVDP TADAVGHAEN QTRGFQRALD DYLKSTGQDP
RQGSRKIADL LRRLDSEPLR TSSGRRLTQT LAVTGIVVPL YTEAAWPRLT SALAAAEKGD
GSPLLALADQ YDERDSSGHY GTTSHAQRVI SCLDDRQRPT LAETKRLLPG FERISPVFGD
FLGWDTAGWC HDWPVPGQYD TPEVSAPGAA PVLLVGNTGD PATPYEGTRR MADELGKGVG
IELTWKGEGH GAYGSGSDCV DNAVNTYLLE GRAPRDGTVC S
//
