ID A0A345UNC8_9BACT Unreviewed; 1080 AA.
AC A0A345UNC8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Tricorn protease homolog {ECO:0000256|PIRNR:PIRNR036421};
DE EC=3.4.21.- {ECO:0000256|PIRNR:PIRNR036421};
GN ORFNames=CYPRO_2741 {ECO:0000313|EMBL:AXJ01980.1};
OS Cyclonatronum proteinivorum.
OC Bacteria; Balneolota; Balneolia; Balneolales; Cyclonatronaceae;
OC Cyclonatronum.
OX NCBI_TaxID=1457365 {ECO:0000313|EMBL:AXJ01980.1, ECO:0000313|Proteomes:UP000254808};
RN [1] {ECO:0000313|EMBL:AXJ01980.1, ECO:0000313|Proteomes:UP000254808}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Omega {ECO:0000313|EMBL:AXJ01980.1,
RC ECO:0000313|Proteomes:UP000254808};
RA Toshchakov S.V., Korzhenkov A., Samarov N.I., Kublanov I.V., Muntyan M.S.,
RA Sorokin D.Y.;
RT "Phenotypic and genomic properties of Cyclonatronum proteinivorum gen.
RT nov., sp. nov., a haloalkaliphilic bacteroidete from soda lakes possessing
RT Na+-translocating rhodopsin.";
RL Submitted (MAR-2018) 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; CP027806; AXJ01980.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345UNC8; -.
DR KEGG; cprv:CYPRO_2741; -.
DR Proteomes; UP000254808; 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; cd00988; PDZ_CTP_protease; 1.
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; 1.
DR Gene3D; 2.120.10.60; Tricorn protease N-terminal domain; 2.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
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; 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; 3.
DR Pfam; PF03572; Peptidase_S41; 1.
DR Pfam; PF14684; Tricorn_C1; 1.
DR PIRSF; PIRSF036421; Tricorn_protease; 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.
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:UP000254808};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR036421}.
FT DOMAIN 702..769
FT /note="Tricorn protease C1"
FT /evidence="ECO:0000259|Pfam:PF14684"
FT DOMAIN 894..1046
FT /note="Tail specific protease"
FT /evidence="ECO:0000259|Pfam:PF03572"
FT ACT_SITE 764
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 982
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT ACT_SITE 1038
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-1"
FT SITE 983
FT /note="Transition state stabilizer; via amide nitrogen"
FT /evidence="ECO:0000256|PIRSR:PIRSR036421-3"
SQ SEQUENCE 1080 AA; 122363 MW; AF3C2B0EC50B1F46 CRC64;
MKYTLRLFFS LLFIAATVIE LRAQDIVPQW IRYQTISPDG QHIAFTYMGN LYRVPVEGGE
ARQLTFHEAH DFIPVWSNDG SQIAFASDRY GNFNVYVMDA MGGTASRLTF HSNDEFPYSF
SHDDQHVIFG AVRQDRAEHR QFPSPSQPEL YQVPVEGGRV GQIFTIPAEY VQVSTDGSRM
LYHDKKGGEN EWRKHQKSAI ARDIWIYESE SDTHRQLTFV EGEDRQPVFN TDESAFYFLS
ERNGSFNVHK MSLTGSEPAE QITFFELHPV RFLSYAQGTL AFGWDGELYT MQEGEEPQKV
DVRIRTQDTR NTDSIITING GVQEMAVSPN GKEIAFIARG EVFVTSTDGA FTKRITNTPQ
RERFVTWNHD GSAVVYASER DGQWHIFETR RVRSEEPFFY ASTLLEEQIV VSDSVDAYLP
SFSPDGKHLA YIAGRRTLRV MNLETRETHD LLGPEDLFHM QDGDQSFSWS PDSQWILVSW
RKLLHNAEVL LLAADGSERH NLTESGFMDY SPKWVGDGDR ILFFTNRDGL RSFATSGRNE
LDAYGIFLTG EAWDTFNLSE DDYKLMQAVQ GALNGDGDGD DSNDNGDSDT TLTFELDNIR
DRMARFTIHS SSISDAVLSK DGETLYYLTR FEDNANLWET NLRTRETRQA IRLNVPGGSL
MWDNNMENLY LLARGSISRL NPSAGTQTPI RIAGEMTFDA AAEREHMFEH VYIRTKNVFY
EPTFHGVDWS MLHEEYKKYV SHLGNSYEFA EMISEMIGEL NVSHAGARFS RNIPNGDATA
SLGIFKDFDF EDDGIRIVEI MEGGPLDRAA LRHIRAGMII EKIDGELVSA DRDVASFLNR
KAGEFVLLDI VDPETGERHQ VTTKPITLGQ ERQLLYRRFV RINEREVDEL SGGRLGYVHI
PGMSDGPFRS VIHDMLGRFA DREAVIVDAR FNGGGDLVAD LAMFFTGVEF NRYATEDRVV
GGEPTSRWTK PTLSMHNEAM YSDGHCYASA YTELELGLTV GMPVPGTCSF AGWSALPDGT
RWGVVPISAR NKSGEWMENN QTEPIIRVKN MPGFIDQGTD QQLMRSVEAL LEQLDGEAYE
//
