ID A0A225NG98_9RHOB Unreviewed; 489 AA.
AC A0A225NG98;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=ATO3_16125 {ECO:0000313|EMBL:OWU72598.1};
OS Marinibacterium profundimaris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Marinibacterium.
OX NCBI_TaxID=1679460 {ECO:0000313|EMBL:OWU72598.1, ECO:0000313|Proteomes:UP000215377};
RN [1] {ECO:0000313|EMBL:OWU72598.1, ECO:0000313|Proteomes:UP000215377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22II1-22F33 {ECO:0000313|EMBL:OWU72598.1,
RC ECO:0000313|Proteomes:UP000215377};
RA Lai Q., Li G., Shao Z.;
RT "Oceanicola sp. 22II1-22F33 Genome Sequencing.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
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:OWU72598.1}.
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DR EMBL; AQQR01000006; OWU72598.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A225NG98; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000215377; 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, ECO:0000313|EMBL:OWU72598.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000215377};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 268..333
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 364..476
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 121
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 151
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 224
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 489 AA; 52224 MW; 2DC7088C0FCCF741 CRC64;
MQLQTSTLTR WTPQRAFNAL GFVVLAMALM LAQAVSSQTR PDSLAPLADQ VSPAVVNITT
STVVEGRTGP QGIVPEGSPF EDFFREFQDR NGGEGRRPRR SSALGSGFVI SEDGYVVTNN
HVIESADEIT IEFFDGDELQ ATVVGTDPNT DIALLKVETD EPLPFVNFGD SDTARVGDWV
IAMGNPLGQG FSLSVGIVSA RNRALSGSYD DYIQTDAAIN RGNSGGPLFN MDGEVVGVNT
AILSPNGGSI GIGFSMASNV VTRVVDQLRE YGETRRGWLG VRIQDVTDEI AEAMGLEQAS
GALITDVPEG PAKEAGLLAG DVIMTFDGKD VEDTRGLVRQ VGNTDIGKSV RVVVFRDGGT
ETVLVTLGRR EEAERTVPAA MEQMEDAPAE REILGLTLST LTEEMRAELG IPEGQDGLVV
VDVDETSEAY EKGLRAGDLI TEAGQQKVET LAALDERIEE ATEAGRKSLL LLVRRGGDPR
FVAISLEDS
//
