ID A0A2S9JKT9_9SPHI Unreviewed; 1092 AA.
AC A0A2S9JKT9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Tricorn protease homolog {ECO:0000256|PIRNR:PIRNR036421};
DE EC=3.4.21.- {ECO:0000256|PIRNR:PIRNR036421};
GN ORFNames=C5749_09615 {ECO:0000313|EMBL:PRD53770.1};
OS Sphingobacterium gobiense.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=1382456 {ECO:0000313|EMBL:PRD53770.1, ECO:0000313|Proteomes:UP000238642};
RN [1] {ECO:0000313|EMBL:PRD53770.1, ECO:0000313|Proteomes:UP000238642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACCC 05757 {ECO:0000313|EMBL:PRD53770.1,
RC ECO:0000313|Proteomes:UP000238642};
RA Li L., Liu L., Zhang X., Wang T., Liang L.;
RT "The draft genome of Sphingobacterium gobiense H7.";
RL Submitted (FEB-2018) 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:PRD53770.1}.
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DR EMBL; PVBS01000002; PRD53770.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S9JKT9; -.
DR OrthoDB; 9815657at2; -.
DR Proteomes; UP000238642; 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; 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; 3.
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; SSF82171; DPP6 N-terminal domain-like; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 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:UP000238642};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR036421}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1092
FT /note="Tricorn protease homolog"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015648493"
FT DOMAIN 855..1049
FT /note="Tail specific protease"
FT /evidence="ECO:0000259|SMART:SM00245"
FT REGION 548..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 756
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 980
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 1038
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
SQ SEQUENCE 1092 AA; 124150 MW; 51145D2C4544BC4D CRC64;
MKNKFSKALH ALFLSGFLFL GAKAQQETLL LRNPDISDKH ITFVYAGDVW IANKNGENAR
RLTVNPGVEQ NPIFSPDGQQ IAFTGNYDGN TDVYVVSIQG GAPQRVTFHP TSDILRGWLN
NNEVYFTSTR EFTYSLGPRL YKTSVNGELA SPLLMPEAYQ GSPSPDGRYW AYIKNTDPTE
RDRVAFKRYR GGGMPSIWIF DTQTKEVEII PGENSNDVKP IWLGNKVYFL SDRDKIVNIF
SYDTKTKSVE KLTNYKDYDV RTLSGKGDEL TFEYAGRLHI LHTATKNVER LVINVNADAM
YKRQHYIDVG KDIRSYTISP TGQRVLFENR GEIFTIPKEK GDARNISKAP ASHERFPAWS
PNGKWISFIS DKNGKYELVL RDQMAKNEPI YIPLGETAFY YQPSWSPDSK KLFYNDAHLN
LYYVDIETKK ITLVDDDRLS STTGRVSNHF QPSWSFDSDW IAYVKSLRNG IRTLFMYNLQ
TRQSTQITDG MSAVNQPTFS RDGKYLFFSA STNTGLTNSG LHMTAYERNV NYNVYAFILS
KETPSLFKNE SDEEEITDDK TKNKKEENKE KEDKSEEKPK EDKSKKSATK VDLEDISRRI
VALPLSPGRY SLNGTTENML IYMRGNTIGA YDLKKLEDNK LVENASGFAI SADGKKMLYR
SNRDFFIVNA GQKPAPGKGK IEIKNVKQLV DPVAEWKQIF HEVWAMQKEF FYVENMHGVD
WNAMRTKYEK FLPYVGHRSD LGYLLNEMMG EMVVGHNYIY PGDEPATPAV HTGTLGADFD
VVEEGYKINK IYTTLDWNPS LRAPLAEPGL KVKEGEYIVA VNGIALNQSI NIFQLLENTV
DKQVTLKIND TPSWSGAREI VVKPISFGQE TSLRRMDWVE SNRKKVDELS KGQIAYVYMP
NTGPEGYTYF NRYYFSQMDK KALLLDERNN GGGWVADYVI DLLSRELISG WRIRDGRSFT
TPGNGIYGPK AMIINENAGS GGDMMPYMFR FKGLGKLVGR TTMGILVGIS GYPPLLDGGR
ITSPNFGIFD LDSNYIIENK GVAPDIFVEQ MPKDLLEGRD PQLEKTIAIL LEEMKTYPYQ
ELKDPKDPVR VK
//
