ID A0A0B5I7P2_9ACTN Unreviewed; 1100 AA.
AC A0A0B5I7P2;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Tricorn protease homolog {ECO:0000256|PIRNR:PIRNR036421};
DE EC=3.4.21.- {ECO:0000256|PIRNR:PIRNR036421};
GN ORFNames=SVTN_15755 {ECO:0000313|EMBL:AJF65648.1};
OS Streptomyces vietnamensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=362257 {ECO:0000313|EMBL:AJF65648.1, ECO:0000313|Proteomes:UP000031774};
RN [1] {ECO:0000313|EMBL:AJF65648.1, ECO:0000313|Proteomes:UP000031774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GIMV4.0001 {ECO:0000313|Proteomes:UP000031774};
RA Deng M.R., Guo J., Ma L.Y., Feng G.D., Mo C.Y., Zhu H.H.;
RT "Complete genome sequence of Streptomyces vietnamensis strain GIMV4.0001, a
RT genetic manipulable producer of the benzoisochromanequinone antibiotic
RT granaticin.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Degrades oligopeptides. {ECO:0000256|PIRNR:PIRNR036421}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|PIRNR:PIRNR036421}.
CC -!- SIMILARITY: Belongs to the peptidase S41B family.
CC {ECO:0000256|ARBA:ARBA00008524, ECO:0000256|PIRNR:PIRNR036421}.
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DR EMBL; CP010407; AJF65648.1; -; Genomic_DNA.
DR RefSeq; WP_041129675.1; NZ_CP010407.1.
DR AlphaFoldDB; A0A0B5I7P2; -.
DR STRING; 362257.SVTN_15755; -.
DR KEGG; svt:SVTN_15755; -.
DR HOGENOM; CLU_005503_1_0_11; -.
DR Proteomes; UP000031774; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR CDD; cd00988; PDZ_CTP_protease; 1.
DR CDD; cd07562; Peptidase_S41_TRI; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.30.750.44; -; 1.
DR Gene3D; 2.120.10.60; Tricorn protease N-terminal domain; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011659; PD40.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR005151; Tail-specific_protease.
DR InterPro; IPR028204; Tricorn_C1.
DR InterPro; IPR029414; Tricorn_PDZ.
DR InterPro; IPR012393; Tricorn_protease.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR43253; TRICORN PROTEASE HOMOLOG 2-RELATED; 1.
DR PANTHER; PTHR43253:SF1; TRICORN PROTEASE HOMOLOG 2-RELATED; 1.
DR Pfam; PF07676; PD40; 2.
DR Pfam; PF03572; Peptidase_S41; 1.
DR Pfam; PF14684; Tricorn_C1; 1.
DR Pfam; PF14685; Tricorn_PDZ; 1.
DR PIRSF; PIRSF036421; Tricorn_protease; 1.
DR SMART; SM00245; TSPc; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF69322; Tricorn protease domain 2; 1.
DR SUPFAM; SSF69304; Tricorn protease N-terminal domain; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR036421};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR036421};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PIRNR:PIRNR036421};
KW Reference proteome {ECO:0000313|Proteomes:UP000031774};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR036421}.
FT DOMAIN 855..1047
FT /note="Tail specific protease"
FT /evidence="ECO:0000259|SMART:SM00245"
FT REGION 1077..1100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 755
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 978
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 1036
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT SITE 979
FT /note="Transition state stabilizer; via amide nitrogen"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-3"
SQ SEQUENCE 1100 AA; 119768 MW; 686F883EA1826D27 CRC64;
MSDDVAYLRF PHLHDDLLCF AAEDDLWLAP LAPEGERPDR AWRLTVDRTR VGHPRFSPDG
RHIAYTNWRS LDPEIHLVPI DGGTARRLTY WGSTDTRVCG WTPPDKDGRS DILAVSSHGQ
PFSYYSWAYT VPTDGSPGLR LPWGPVSDIA VTDDTAITGN DGERRSLLLT GKPPHEPAAW
KRYLGGATGR LWLHGERLLP DLGGHIDAPM TVGGRIAFLS DHEGIGNLYS CRPDGTDLRR
HTDHDDFYAR HASSDGRRVV YQCAGELWIV DALTADSRPR KLEVRLGGQR VGRRCYQVPA
AHHIDALSVD ETGRASAVSV RGSLYWLTHR DGPARTIIDS PGVRVRLPEM LGSGGQVAYV
TDAEGEDAVE VAYLPRASGD RPPRRLASGD LGRVEELVSD PDGERLAIAS HDGRLLLLDA
TEESNGEVTE LIRSVNGPVR DLAFSPDGDW LTWSHPGIGR SLRSIKMARI SGPGARTVVD
VTNGRFEDEN PVFTRDGRYL AFLSWRGFDP VYDVHTGDLS FPLGCRPYLV PLSSATPSPF
ALLPDGRPAA GGLDPTDEDA ETADGTVTVE IEGLPDRVTP FPVAASKYSA LHPVSGGGLV
WLRWPISGAL GETFANPADT SGKPTLEHFS ITKARKSELA KDLDWFAVSG DGTRLVVADD
GELRAVPATE SGDGDSTVYL DLRRILHEID PGAEWRQAFD EAGRIVRAYF WEPDMGGVDW
TAVLDQYRPL VERVASPDEF ADLLREVMGE LGTSHAYVTP ARRNEGPPHY QRPMGLLGAN
LVPREAGWTV KRILPGESSD SKARSPLAGT GIREGAVLTH VDGRPVDPVT GPYPLLSGTG
GTTVELTFTP AEGEGRARRV AVVPLIDERP LRYHDWVAKR RAVVRELSGG RCGYLHIPDM
GGSGWAQFNR DLRWEVSRPA LIVDVRGNAG GNISELVVEK LTRKILGWDL TRNAQPVSYA
SNAPRGPVVA LADEATSSDG DMITAAFKIL GLGPVVGQRT WGGVVGMTGR HRLGDGTQIT
VPMNAAWFPE YGWSLENHGV EPDLAVLRTP LDWAEGRHAQ LDDAVHIALA LLDETPAASP
PGYESLPDRS RPKLPPRPDA
//
