ID K2JGW6_9PROT Unreviewed; 504 AA.
AC K2JGW6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 38.
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 ORFNames=P24_12587 {ECO:0000313|EMBL:EKE73802.1};
OS Oceanibaculum indicum P24.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Oceanibaculaceae; Oceanibaculum.
OX NCBI_TaxID=1207063 {ECO:0000313|EMBL:EKE73802.1, ECO:0000313|Proteomes:UP000006746};
RN [1] {ECO:0000313|EMBL:EKE73802.1, ECO:0000313|Proteomes:UP000006746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P24 {ECO:0000313|EMBL:EKE73802.1,
RC ECO:0000313|Proteomes:UP000006746};
RX PubMed=23209207; DOI=10.1128/JB.01859-12;
RA Lai Q., Shao Z.;
RT "Genome Sequence of Oceanibaculum indicum Type Strain P24.";
RL J. Bacteriol. 194:6942-6942(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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKE73802.1}.
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DR EMBL; AMRL01000016; EKE73802.1; -; Genomic_DNA.
DR RefSeq; WP_008945123.1; NZ_AMRL01000016.1.
DR AlphaFoldDB; K2JGW6; -.
DR STRING; 1207063.P24_12587; -.
DR PATRIC; fig|1207063.3.peg.2543; -.
DR eggNOG; COG0265; Bacteria.
DR Proteomes; UP000006746; Unassembled WGS sequence.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000006746};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 280..371
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 410..492
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 131
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 161
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 504 AA; 53693 MW; 1F3EB1BC0864F561 CRC64;
MSNRLAFLPG TSAQADGSSR RLSANRFFAT LLALAVLVQA VPALARPAPD SFADMAEKLL
PAVVNVSTTQ TVQSSPQDVP EMPQFPPGSP FEEFFRDFFD RQQRPNQPRR ATSLGSGFVI
DASGFIVTNN HVIADADKVT IRMHDDAEFE AEIVGRDPKT DLALLKINPG DYKLTAVGWG
DSDASRVGDW VLAIGNPFGL GGTVTAGIVS ARARDINAGP YDDFLQTDAS INRGNSGGPM
FNMSGEVVGI NTAIYSPSGG SIGIGFAVPS ALAKPVIEQL KEYGRTRRGW LGVRIQMVTD
EIAESLGLDK ARGALIASVT ETGPADKGGI KAGDIVLKFN GQNVPDMRRL PRIVAATKID
EDVPVEIWRD GKKLTVQVKV GELEEAEQAG LLDPTKPADS GAVNRTVDSL GLSLTGVTPE
LRQRFGLADT AKGVLVTEVK PNSPAAEKAI QPGDMIVEVS QEEVNSPAEL VEKVQSAQKA
GRKSVLLLVN RKGEMRFVAV RIEG
//
