ID Q085Y2_SHEFN Unreviewed; 1094 AA.
AC Q085Y2;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=Tricorn protease homolog {ECO:0000256|PIRNR:PIRNR036421};
DE EC=3.4.21.- {ECO:0000256|PIRNR:PIRNR036421};
DE Flags: Precursor;
GN OrderedLocusNames=Sfri_1080 {ECO:0000313|EMBL:ABI70933.1};
OS Shewanella frigidimarina (strain NCIMB 400).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=318167 {ECO:0000313|EMBL:ABI70933.1, ECO:0000313|Proteomes:UP000000684};
RN [1] {ECO:0000313|EMBL:ABI70933.1, ECO:0000313|Proteomes:UP000000684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 400 {ECO:0000313|EMBL:ABI70933.1,
RC ECO:0000313|Proteomes:UP000000684};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL Submitted (AUG-2006) 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; CP000447; ABI70933.1; -; Genomic_DNA.
DR RefSeq; WP_011636554.1; NC_008345.1.
DR AlphaFoldDB; Q085Y2; -.
DR STRING; 318167.Sfri_1080; -.
DR KEGG; sfr:Sfri_1080; -.
DR eggNOG; COG0793; Bacteria.
DR eggNOG; COG4946; Bacteria.
DR HOGENOM; CLU_005503_0_0_6; -.
DR OrthoDB; 9758793at2; -.
DR Proteomes; UP000000684; 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; 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; 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; PS51257; PROKAR_LIPOPROTEIN; 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:UP000000684};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR036421}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1094
FT /note="Tricorn protease homolog"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004166392"
FT DOMAIN 839..1044
FT /note="Tail specific protease"
FT /evidence="ECO:0000259|SMART:SM00245"
FT ACT_SITE 753
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 975
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 1033
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT SITE 976
FT /note="Transition state stabilizer; via amide nitrogen"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-3"
SQ SEQUENCE 1094 AA; 121313 MW; A878EDACAA1B5444 CRC64;
MKLRRSVAHC MLALGTLACS SMIFANASNQ GYYRAPALND QTLVFTAEGD LWTKQLNQTK
ASRLTSLAAE ELDATISKDG KWVAYTANYE GATEVYVMPI AGGVAKRVSF ENSRVRLQGW
TASGEVLYST DNAFGPANFW VLKTVDPQSL TITDLPLADA VEGTIDDKGE YVYFTQFGLQ
VSGDNVKVYR GGAKGEIWRY KLGSKQEAQQ LTSAHEGSVK QPMLWNQRVY FVSDQSGNDN
IWSMTLDGKD IKQLTQYSDW QVRDAQLNNG RIIFQQGADI KLLNLADLAE STVAIELTSD
FTHRREQWVN DPMDYATSTV FSHQGDNVVI TARSHVAIAS NDGRRLVQID SPADSRVRDA
LLSDDGKWVY GISDASGEQE IWQYPADGSA GAKQLTKDGS TLRTSLSLSP NGRYLVHDDY
MGNVWLLDLS RYNNQKIIQN GEGLGPYQDI KWSGDSQFIA LTKAEIGKQR PQIVLYSINE
SKSQTLTTDK YESFSPSFSH DGKWLYFLSN REFKANPGSP WGDRNMGPIF DKRTQVFALA
LDAKASFPFA KPTELTVNKD AKKADSKDQD IPAKVKVEWD GLNQRLWQVP VDAGNYNSLT
AAKDKLYLLD GSQDKSELKL IKFDPLNIKV DAFSEDVGQY SLSKDGSKIM LRKQSDPKSL
MIVDAGDKLP SDVSRAKVST DQWQLSISPQ QEWQQIFEDA WLMHRDSFFD PKMRGVDWQA
AKAKYQPLVD RLTDRNELND IFTQMMGELN SLHSQVRGGD IAQDADAAKA AALGARLTQT
DRGVVISHIY QTDPELPLSA SPLARIEVDA KEGDVIASIN GKKITNIADV TQLLRNQGNK
QVLLGLVRGK TAINTIVTPH DIGTDAKLRY LDWVEHNGDK VAKASKGNIG YLHLYAMGSG
DVESFAREFY TNYDKEGLII DVRRNRGGNI DSWIIEKLLR RAWAFWQPTH GSTNANMQQT
FRGHLVVLAD QMTYSDGETF SAGIRALNIA PIIGKQTAGA GVWLSGRNSV TDKGMARVAE
YPQYAIDGRW VVEGHGVEPD IEVDNLPYAT FSGKDAQLDA AISYLKDELV QQPIAPLQGL
PMPDIGPAAD IKAK
//
