ID K6ZFA0_9ALTE Unreviewed; 1135 AA.
AC K6ZFA0;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Tricorn protease homolog {ECO:0000256|PIRNR:PIRNR036421};
DE EC=3.4.21.- {ECO:0000256|PIRNR:PIRNR036421};
GN Name=tri {ECO:0000313|EMBL:GAC29027.1};
GN ORFNames=GPAL_2166 {ECO:0000313|EMBL:GAC29027.1};
OS Glaciecola pallidula DSM 14239 = ACAM 615.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Glaciecola.
OX NCBI_TaxID=1121922 {ECO:0000313|EMBL:GAC29027.1, ECO:0000313|Proteomes:UP000006251};
RN [1] {ECO:0000313|EMBL:GAC29027.1, ECO:0000313|Proteomes:UP000006251}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACAM 615 {ECO:0000313|EMBL:GAC29027.1,
RC ECO:0000313|Proteomes:UP000006251};
RX PubMed=25009843;
RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT high degree of genomic diversity and genomic characteristic for cold
RT adaptation.";
RL Environ. Microbiol. 16:1642-1653(2014).
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:GAC29027.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BAEQ01000040; GAC29027.1; -; Genomic_DNA.
DR RefSeq; WP_006011538.1; NZ_KE386817.1.
DR AlphaFoldDB; K6ZFA0; -.
DR STRING; 1121922.GCA_000428905_01892; -.
DR OrthoDB; 9758793at2; -.
DR Proteomes; UP000006251; 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; 2.
DR Pfam; PF03572; Peptidase_S41; 1.
DR Pfam; PF14684; Tricorn_C1; 1.
DR Pfam; PF14685; Tricorn_PDZ; 1.
DR PIRSF; PIRSF036421; Tricorn_protease; 2.
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 Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR036421}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1135
FT /note="Tricorn protease homolog"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003900867"
FT DOMAIN 892..1086
FT /note="Tail specific protease"
FT /evidence="ECO:0000259|SMART:SM00245"
FT REGION 580..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..610
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 796
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 1017
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 1075
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT SITE 1018
FT /note="Transition state stabilizer; via amide nitrogen"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-3"
SQ SEQUENCE 1135 AA; 126055 MW; 7ECAABE0B956CE31 CRC64;
MIPICRYSLS KLALFSIGLS ILSSQAIASI DVSNAGYFRT PSIHDNTIVF AAEGDLWRVN
HQSGLVKNEA VRLTTHSAEE ITPFISPSGQ QVAFSANYEG TIEVYLTSVT GGAPKRITFE
NSRAMVKGWT QSGDIVYATS TTITGPANSW VLKTVDPKTL VVNNIQVSDA VEGVIDDKTN
TLYFVQHGLQ ISTDNANQYK GGATGELWQY NLDNVEEATK LTEAHTGSVK NPMLFNQHLY
FISNQSGIDN LWRMSLNGEN AEPVTKYIEW GVRSASMHNG TIAYQLGADI IILDLVQNSS
EKVSIALTSD FPHLRERWIE KPLERLSHVS LSPKGNKVVV TARGRIAVAG TDTKRLVEIN
TKPTSRSRNA ILNIDNKSVF TFNDDSGESE VWQFWLDGQT PPKKLTNDGK TSRLNMWLSP
DGSKLAHDTK QGELFLLDIA SGENTLLLNN IASGVSSFNW FKDNDTIALA YVKAGNERTS
VILHSLSQEK SETLTSQKYE SYSPTFSADG KWLYFLSDRN FNANPNSPWG DRNMGPAFDR
KAEIYAIALN AASKFPFAQP QERIGLLSKT DDEDVDKIEE NEDDAFPSDE QDESDKLQDQ
MSSKKNADAD QKTSIEITWQ GIQKRLWKVP VSAGNYSQLS ANSRFLYVID QVNEPNSRPD
LKSIGIKYDP SLKTYTSAIS AYELSKDGES ILIQKGRRAA TSMYVVSAGS IFPSNARDNM
VQTQGWKIRI EPRNEWRQIF KDAWLMHRDS LFETDMRGVD WLATKAKYEP LLKRLTDRRE
LNDIFKQMMG ELNALHSQVR GGDIIDNDET ASSSSLGAAF LDSVDGVLVS HIYLHDPELP
DEASPLASPG VNAMNGDIVK AINNTAITTV ADLVKQLKFQ SGKQVLLTLE RNGEQINTIV
KPESSGNEGR YRYRNWVYSN ASKVAEQDQD IGYLHLYAMT GSDLSTFAKE FYAQYKKQGL
IIDVRRNRGG NIDSIIIEKL LRRAWSFWQS TNGQRSTNMQ QAFRGHLVVL ADEFTYSDGE
TFTAGIKALD LGTVIGKQTA GAGVWLSGGN SVVDGGMARV AEFPVFAMDG RWITEGRGIS
PDIEVNNMPH ATYKGIDAQL NKGIAYLQEK IKEQPIPEYK AKPFPPIDAT ADDIK
//
