ID A6EBZ5_9SPHI Unreviewed; 1073 AA.
AC A6EBZ5;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 22-FEB-2023, entry version 65.
DE RecName: Full=Tricorn protease homolog {ECO:0000256|PIRNR:PIRNR036421};
DE EC=3.4.21.- {ECO:0000256|PIRNR:PIRNR036421};
GN ORFNames=PBAL39_05578 {ECO:0000313|EMBL:EDM37244.1};
OS Pedobacter sp. BAL39.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=391596 {ECO:0000313|EMBL:EDM37244.1, ECO:0000313|Proteomes:UP000003664};
RN [1] {ECO:0000313|EMBL:EDM37244.1, ECO:0000313|Proteomes:UP000003664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAL39 {ECO:0000313|EMBL:EDM37244.1,
RC ECO:0000313|Proteomes:UP000003664};
RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUN-2007) 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}.
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:EDM37244.1}.
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DR EMBL; ABCM01000005; EDM37244.1; -; Genomic_DNA.
DR RefSeq; WP_008240661.1; NZ_ABCM01000005.1.
DR AlphaFoldDB; A6EBZ5; -.
DR STRING; 391596.PBAL39_05578; -.
DR eggNOG; COG0793; Bacteria.
DR eggNOG; COG4946; Bacteria.
DR OrthoDB; 9815657at2; -.
DR Proteomes; UP000003664; Unassembled WGS sequence.
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; 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; IPR018910; Lipoprotein_LpqB_C.
DR InterPro; IPR011659; PD40.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR005151; Tail-specific_protease.
DR InterPro; IPR028204; Tricorn_C1.
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; PF10647; Gmad1; 1.
DR Pfam; PF07676; PD40; 3.
DR Pfam; PF03572; Peptidase_S41; 1.
DR Pfam; PF14684; Tricorn_C1; 1.
DR PIRSF; PIRSF036421; Tricorn_protease; 1.
DR SMART; SM00245; TSPc; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS50106; PDZ; 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:UP000003664};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR036421}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1073
FT /note="Tricorn protease homolog"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002694953"
FT DOMAIN 748..852
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 545..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 762
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 979
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 1035
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT SITE 980
FT /note="Transition state stabilizer; via amide nitrogen"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-3"
SQ SEQUENCE 1073 AA; 122092 MW; A83993B0FD55D6DA CRC64;
MKRTFFAITT ALLLSGTVTQ AQNETYFTAY PALTPDAQTV VFSFEGDLWK VPATGGAATR
LTAMPGEEIN PRVSPDGKWL AFSSNQFGNY DVYVMPMAGG TVKQLTFNDT ADEVDNWSWD
SKTIYFSSGR YNMYTTYTVG ANGGTAKRLF PNFFNTIHNV AEAPSGELFF NDTWESKNFA
NRKRYKGAFN PDIQSYNPKT KAYKQYTDYK GKDLWATVAK SGKVYYASDE GNDEYNLYTF
EGDKKLRLTD FPSAIKRPFV AANGASIVFE RDYQLYLYNV SSKTSRKINI EVSRNTVLSK
DQEFDVRGSI TDFDASPDGK KLAFVSRGEL FVSDAEGKFI RKINRGLENG INERVMEVKW
LSDNRTLVFN QTFKGYPNWF SIAADGKGKT KQLTSENRSN RAIAFNKDRT QAVYLSGRDE
VRVMDLKSLE SKTIVKDEIW AFQNANPSFS PDGAYVLFTA YRNFEQDIFV HHLKQNKTIN
LTNTGVTETS PSWSPDGKYI FFTSLRTKPS YPFGMQNGHV YRMALDDYDE PYRLDKFDEL
FNEKKKDKTA PADNKTDKDK KKPSKSEKEK AKADSLKKAE DKSKEASMFV INTQNLMDRI
TLVSPNFGTQ SGAEILEKGD KTYAFYSSDH EGGGASFYRT VIENFENNKT EKVTDGYASI
QQSGDKYYIL SRGTIHKYNI DMNRLDRLDI GYKFNRNLNE EFNQMFYESW AGLEENFYSE
DFHGVDWMKM RQQYARFLPY LNNRSDLRVL LNDMLGELNS SHLGFSTYGA DERKSLNYAT
NETGIVFDDE NPFKVSRVVA QSNGRHKGVG LRAGDVITAV NGVPLDASID RDYYFTTPSL
EQEMELTLTR EGKIVTTKVH PQSTGTLKGN LYDEWITENR ERVKTLGNNR IAYSYMKNMG
GDELERFLLD MVAQENNKEG IILDLRYNTG GNVHDEVLRF LSQRPYLQWK YRGGKLSPQS
NFAPAAKPIV LLINEQSLSD AEMTAAGFKA LKLGKIIGTE TYRWIIFTSG KGLVDGSFYR
LPSWGCFTLD GKNLEKEGVA PDIYVKNTFV DRLEDKDPQL ERAVAEILQD LKK
//
