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Database: UniProt
Entry: A4Y917_SHEPC
LinkDB: A4Y917_SHEPC
Original site: A4Y917_SHEPC 
ID   A4Y917_SHEPC            Unreviewed;      1094 AA.
AC   A4Y917;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   RecName: Full=Tricorn protease homolog {ECO:0000256|PIRNR:PIRNR036421};
DE            EC=3.4.21.- {ECO:0000256|PIRNR:PIRNR036421};
DE   Flags: Precursor;
GN   OrderedLocusNames=Sputcn32_2731 {ECO:0000313|EMBL:ABP76450.1};
OS   Shewanella putrefaciens (strain CN-32 / ATCC BAA-453).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=319224 {ECO:0000313|EMBL:ABP76450.1};
RN   [1] {ECO:0000313|EMBL:ABP76450.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CN-32 {ECO:0000313|EMBL:ABP76450.1};
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   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Fredrickson J.,
RA   Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella putrefaciens CN-32.";
RL   Submitted (APR-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}.
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DR   EMBL; CP000681; ABP76450.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4Y917; -.
DR   STRING; 319224.Sputcn32_2731; -.
DR   KEGG; spc:Sputcn32_2731; -.
DR   eggNOG; COG0793; Bacteria.
DR   eggNOG; COG4946; Bacteria.
DR   HOGENOM; CLU_005503_0_0_6; -.
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; 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   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; 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   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..1094
FT                   /note="Tricorn protease homolog"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002677343"
FT   DOMAIN          758..849
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
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;  121131 MW;  8F9A1DD2A9431711 CRC64;
     MKLRHSVACC MLALGTLTAF QTIAADAVSN QGYYRAPALH NQTLVFTAEG DLWTQTLGQK
     AATRLTSLPA EELGATISAD GKWVAYVANY EGASEVYVIP ITGGVAKRVS FENSRVRVQG
     WTAKGDILYS TDTGFGPANN WMLRSVDPQT LTTTDLPLAD AVEGVIDDRN EYVYFTRFGL
     QVTGDNAKVY RGGAKGELWR FKLGSKTEAQ LLSGQHDGSV RQPMLWQDRL YFISDSDGND
     NLWSSALDGS DAKQLTQFKD WQVRGARMDQ GKVVFQLGAD IHVFDIAAAK DSLLNIELTS
     DFAERREHWV KDPMDYASST NLAPAGDKVV ITARSHVAIA GIDGSRLVQV ALPGTYRVRE
     AVLSQDGKSV YAISDMTGQQ EIWQFPADGS SGAKQLTKDG HTLRMSLNLS SDGRFIAHDD
     NDGNVWLLDL KKNTNQKIIT NGEGLGPYAD ICWSSDSRFI ALTKSEIGKQ RPQIVLYSVD
     ENKAETLTSD KYESYSPTFS SDGQWLYFLS NRQFSATPSS PWGDRNMGPV FDKRSQIFAI
     ALVKNAKFPF SKPNELESNQ VEKNDAKDKP SPVKIDWAGI SQRLWQVPVD SGNYSKLRVV
     DDRLYLLDQA IGDDVAPNLM TIKFDRLSPK AEVFAEDIGQ YEVSADGKKL MLRKHSNDKS
     LLIVDGGDKL GDTDNAKVQT EQWQLAISPQ LEWQQMFEDA WLMHRESFFD KKMRGLDWQA
     TKAKYQPLLD RLTDRNELND IFMQMMGELD SLHSQVRGGD LPKDPDAAKA ASLGARLQQT
     ADGVKIAHIY SNDPELPANA SPLNRIEVDA KAGDMLLAIN GTPVANVADV TRLLRNQQDK
     QVLLQLKRGS QTHKTIVMPV SAMVDSQLRY LDWVSHNAAV VEDASQGKMG YLHLYAMGGG
     DIESFAREFY ANYDKEGLII DVRRNRGGNI DSWIIEKLLR RAWAFWQPTH GTPNTNMQQT
     FRGHLVVLTD ELTYSDGETF SAGIKALGIA PLIGKQTAGA GVWLSGRNAL TDKGMARVAE
     YPQYAMDGRW VLEGHGVTPD IEVDNLPFAT FNGKDAQLEA AISYLKDELV KQPIPALKAQ
     PMPVKGMAQD INAN
//
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