ID A0A1M4XWI3_9BACT Unreviewed; 1097 AA.
AC A0A1M4XWI3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Tricorn protease homolog {ECO:0000256|PIRNR:PIRNR036421};
DE EC=3.4.21.- {ECO:0000256|PIRNR:PIRNR036421};
GN ORFNames=SAMN05444274_103148 {ECO:0000313|EMBL:SHE97788.1};
OS Mariniphaga anaerophila.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Prolixibacteraceae;
OC Mariniphaga.
OX NCBI_TaxID=1484053 {ECO:0000313|EMBL:SHE97788.1, ECO:0000313|Proteomes:UP000184164};
RN [1] {ECO:0000313|EMBL:SHE97788.1, ECO:0000313|Proteomes:UP000184164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26910 {ECO:0000313|EMBL:SHE97788.1,
RC ECO:0000313|Proteomes:UP000184164};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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}.
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DR EMBL; FQUM01000003; SHE97788.1; -; Genomic_DNA.
DR RefSeq; WP_073000158.1; NZ_FQUM01000003.1.
DR AlphaFoldDB; A0A1M4XWI3; -.
DR STRING; 1484053.SAMN05444274_103148; -.
DR OrthoDB; 9815657at2; -.
DR Proteomes; UP000184164; 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; 5.
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; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF69304; Tricorn protease N-terminal domain; 2.
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:UP000184164};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR036421}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1097
FT /note="Tricorn protease homolog"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012431737"
FT DOMAIN 856..1048
FT /note="Tail specific protease"
FT /evidence="ECO:0000259|SMART:SM00245"
FT REGION 543..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1078..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 755
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 979
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 1037
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
SQ SEQUENCE 1097 AA; 123493 MW; C726FB1E059D9890 CRC64;
MKNLFLLSAA LFLMFSANGQ INAKLMRYTD VSESQIAFVY GGDIWLVDKN GGTAIQLTNS
PGEESWPRFS PDGTHLAFTA NYNGNSDVFV MPVTGGIPTR ITFNVFPDRM VDWHPDGKKL
FFASARENGI SRLNQFYLTS KDGGFPEKVQ IPYGELASFS PDGNKLAYIT KITENYPFKR
YLGGLASDIT IFDLKNNTAE RITDYPGNDG QPAWAGNKIY FLSDRDENMR LNIWEYDTKT
KEMRQITNYK NFDISFMSAG PDDLVYEMGG DLYLMDLASL KPRQIKVNVI SDLSVEMPHS
KDVSSRISNV TASPGGKRVI FEARGELFNA PTEEGFTLNM TRSSGSFDQN PAWSPDGKTI
AFWSDKSGEY EMYLQDSNGK NPAKQLTQRG KGFGYKLFWS PNSKKIAFID ETNTIQIIDA
ESGEITEAGN YRWNLGHGQR FNFPLSWSPD SKWLAFTQGL DNSNAAICIF NTDDNQLHQV
TSGFYDDSFP VFSTDGKYLF YLTNRNMSAA YSSLGDGTWI YPNSTEIAAL SLKKDTPSLL
APKNDEVEIK AENKEKDDDE KKKKDQEKDE NKEKENDNKV EIDFENLETR LSILPPKAGN
ISALIPFEGK LVYLRRPNTG SGERHSSLHF YDLKEREEKE MMGQVSRAAA TADGKSLIVS
SQNKYGIIKP AAGQKIEKPI PTDGLVMDLI PKEEWRQIFM DTWRRHRDFF YDPNMHGLDW
EALRDRYGEL LDDARTRWDV TNLQLNLVAE ISAGHTYAGG GDTERASSRS NGFLGVDWEP
DGKQYRIKKI VKPAEWDTEV RSPFDKPGVE VNEGDYILSV NGISLDPTKE PYAAFEGLSG
KTVKLQVSTT GKEADARDVV VKCLSAGQEN NLRYLEWIEN NRKMVDELSD GQLGYIYMSN
TSSRGQLELV RMFYGQLHKK GFILDERFNG GGQLADRFLE LLQRPVTYNL HWRHGKDHTN
PIKTNTGPVG MLINGWAGSG GDGLPWAFQE LKAGPIVGER TLGILVGPAS QHQLIDGGYI
TVPGARLYDN DGHWFWEGEG VSPDFEVWDD PNMLIKGRDP QMEKVVKEVL KLTKENKHLM
TPAPPLEDRT AKGLRKE
//
