ID A0A1Q3H4D8_9BACT Unreviewed; 1070 AA.
AC A0A1Q3H4D8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Tricorn protease homolog {ECO:0000256|PIRNR:PIRNR036421};
DE EC=3.4.21.- {ECO:0000256|PIRNR:PIRNR036421};
GN ORFNames=BKI52_05355 {ECO:0000313|EMBL:OJJ23778.1};
OS marine bacterium AO1-C.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae.
OX NCBI_TaxID=1905359 {ECO:0000313|EMBL:OJJ23778.1, ECO:0000313|Proteomes:UP000186474};
RN [1] {ECO:0000313|EMBL:OJJ23778.1, ECO:0000313|Proteomes:UP000186474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AO1-C {ECO:0000313|EMBL:OJJ23778.1};
RA Buerger P., Wood-Charlson E.M., Weynberg K.D., Willis B., Van Oppen M.J.;
RT "CRISPR-Cas defence system in Roseofilum reptotaenium: evidence of a
RT bacteriophage-cyanobacterium arms race in the coral black band disease.";
RL Submitted (OCT-2016) 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:OJJ23778.1}.
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DR EMBL; MLAY01000001; OJJ23778.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3H4D8; -.
DR STRING; 1905359.BKI52_05355; -.
DR Proteomes; UP000186474; 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; 2.120.10.30; TolB, C-terminal domain; 3.
DR Gene3D; 2.120.10.60; Tricorn protease N-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
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; IPR029414; Tricorn_PDZ.
DR InterPro; IPR012393; Tricorn_protease.
DR PANTHER; PTHR43253; TRICORN PROTEASE HOMOLOG 2-RELATED; 1.
DR PANTHER; PTHR43253:SF1; TRICORN PROTEASE HOMOLOG 2-RELATED; 1.
DR Pfam; PF07676; PD40; 6.
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; SM00228; PDZ; 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.
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:UP000186474};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR036421}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1070
FT /note="Tricorn protease homolog"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012817790"
FT DOMAIN 752..839
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 739
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 967
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 1024
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
SQ SEQUENCE 1070 AA; 120617 MW; 747D9D558BAFAC4C CRC64;
MKKFYLLICV IVAISSITQA QTNPIFATKP SISPDGSQVA FSYQGDIWVM AANGGTARRL
TIHPAYETNP IWSPDGKSIA FNSNRLSNQD IFTIPAQGGQ VKRITYHSTT DAVGSWVNNQ
IVFNSARRAF KQIEWASEIQ AVNAKGGTPS RIMDALGYMP VQSPNGNLIA FVKGACRISR
EAYQGPANKN IWIYNTKTRK YTQISQSKFN EYQPVWGNDN TLYYIGAATG RYNIYSQKIN
ADGSANGQPA QITKFKDDGV RYIGASQNGK LVFERQVSLY TMNASGGTPQ RLNIQATSDS
RFDPMEHKTY RNNVSSYELS PSGKYIAMEI RGEIFIKPTK RDKRRAVNIS KHAYRDRYPT
WLNDSTVIFV SDRDGQYDLY LARSADKKQG NLYQTLKTEV VRLTNTKVDE SEPIMSPNRK
KIAFQRGRGD LVVANISTAG KLSAEKTLVK GWDAPGGVAW SPDSRWVAYA LSDLNFNREV
YIHAADNSKP AVNISMHPRR DQSPVWSPDG SKLGFISNRI NDYDIWFVWL NKKDWELSRK
DREEGNYYDN PDAKKKKKRK KSKAVKIDFD NIHDRMVRVT SKPGDEFDFA FNQKGDKLYF
TANSPTNRRR DLYQAKWDGT KMRTITKNGK NPAGLNLAPK GRQLYFVTRG MVQQMSTKGN
RVAPLPHEAK MVINHPQERA QIFEEAWRNL NAGFYDPNFH GQNFEALRKK YKPWALQAST
VQDFREIYNL MLGQLNASHM GLRGRSIPER TQRERTGFLG IEVEPAKGGV KVTHVIANSP
ADKTESKINK GEVITAVNGQ SIGANTNFYS LLTNTNNERI MLNVQGKGGN REVIIRPANS
LGNLLYEEWI SDKKALVEKY SNGRLGYIHI RGMNMPSFER FERELMASGY GKEGIVIDVR
FNGGGWTTDY LMAVLNVQQH AYTIPRGAAK SLNENKKFRS YYPFSERLPL SSWTKPSVAM
CNQNSYSNAE IFSHAYKHLG IGKLVGQPTF GAVISTGGAR LIDGSLVRMP FRAWYVKATG
ENMEHGPAVP DFLIENAPDN RGKKEDAQLK KSVEVLLKQI GDKKNSTEKR
//
