ID I3TNV6_TISMK Unreviewed; 490 AA.
AC I3TNV6;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Probable periplasmic serine endoprotease DegP-like {ECO:0000256|ARBA:ARBA00013958};
DE EC=3.4.21.107 {ECO:0000256|ARBA:ARBA00013035};
DE AltName: Full=Protease Do {ECO:0000256|ARBA:ARBA00032850};
GN Name=degP {ECO:0000313|EMBL:AFK54444.1};
GN OrderedLocusNames=TMO_2606 {ECO:0000313|EMBL:AFK54444.1};
OS Tistrella mobilis (strain KA081020-065).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC Geminicoccaceae; Tistrella.
OX NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK54444.1, ECO:0000313|Proteomes:UP000005258};
RN [1] {ECO:0000313|EMBL:AFK54444.1, ECO:0000313|Proteomes:UP000005258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA081020-065 {ECO:0000313|EMBL:AFK54444.1,
RC ECO:0000313|Proteomes:UP000005258};
RX PubMed=22458477; DOI=10.1021/ja301735a;
RA Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H.,
RA Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.;
RT "Bacterial biosynthesis and maturation of the didemnin anti-cancer
RT agents.";
RL J. Am. Chem. Soc. 134:8625-8632(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Acts on substrates that are at least partially unfolded. The
CC cleavage site P1 residue is normally between a pair of hydrophobic
CC residues, such as Val-|-Val.; EC=3.4.21.107;
CC Evidence={ECO:0000256|ARBA:ARBA00001772};
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DR EMBL; CP003236; AFK54444.1; -; Genomic_DNA.
DR AlphaFoldDB; I3TNV6; -.
DR STRING; 1110502.TMO_2606; -.
DR MEROPS; S01.442; -.
DR KEGG; tmo:TMO_2606; -.
DR PATRIC; fig|1110502.3.peg.2671; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_1_1_5; -.
DR Proteomes; UP000005258; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00987; PDZ_serine_protease; 2.
DR Gene3D; 2.30.42.10; -; 2.
DR Gene3D; 2.40.10.120; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011782; Pept_S1C_Do.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR001940; Peptidase_S1C.
DR NCBIfam; TIGR02037; degP_htrA_DO; 1.
DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 1.
DR Pfam; PF13180; PDZ_2; 2.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 2.
DR SUPFAM; SSF50156; PDZ domain-like; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50106; PDZ; 2.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:AFK54444.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005258};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 306..345
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 404..455
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 130
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 160
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 236
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 490 AA; 51915 MW; 2A42068A97BC1E34 CRC64;
MNRLPERDAD LAAAIRGGLR SRMLALVLAL AALQVPPAVA ADAERRVPES RSEMQLSFAP
VVRQAAPAVV NIYTRRTVVV QQRSPFFDDP FFRRFFGDRM GIGKPSERVQ NALGSGVIVD
GRGYIVTNNH VIDGADQITV VLNDRREFAA EVVRLDPQTD LAVLKIDTEG QTLPALSFGD
SDSIEVGDLV LAIGNPFGVG QTVTSGIVSA LARTMVGVSD FQSFIQTDAA INPGNSGGAL
VTVNGELIGV NTAIFSRSGG SNGIGFAIPA TLVKTVVQAA IEGRPVARAW LGARGQPVTQ
EIAESLGMPR PTGVLVSDVH PEGPAKGVLK RGDVILEIGG KPVDDPRALR FRLAAAGIGG
ETAVTIWREG RRQTVSLPLV AAPETVARDE REITGSNPLA GARIANLSPA LAEELGIDGF
EEGVIVVDIT RNSAAASIGL KPGDMVLAVN GKRLSRTADV ETTLKQMQGQ RRWQLTLRRE
GRELTLDLMG
//
