ID A0A437GXS4_9SPHN Unreviewed; 475 AA.
AC A0A437GXS4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=EKN06_08760 {ECO:0000313|EMBL:RVQ67208.1};
OS Croceicoccus ponticola.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Croceicoccus.
OX NCBI_TaxID=2217664 {ECO:0000313|EMBL:RVQ67208.1, ECO:0000313|Proteomes:UP000283003};
RN [1] {ECO:0000313|EMBL:RVQ67208.1, ECO:0000313|Proteomes:UP000283003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM-16 {ECO:0000313|EMBL:RVQ67208.1,
RC ECO:0000313|Proteomes:UP000283003};
RA Yoon J.-H.;
RT "Croceicoccus ponticola sp. nov., a lipolytic bacterium isolated from
RT seawater.";
RL Submitted (DEC-2018) 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:RVQ67208.1}.
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DR EMBL; RXOL01000003; RVQ67208.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A437GXS4; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000283003; 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; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000283003};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 242..315
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 347..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 87
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 123
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 198
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 475 AA; 49635 MW; 46DDBD408898DA81 CRC64;
MARVVPRGGA PASFADLTEQ LQPAVVNIST RQRVQVQAGG NPFAGTPFEG LFGGPSGPGG
QPTTREAQSL GSGFIMSADG YVVTNNHVVA AQGRNGTIEA ITVTTTDGTE YEAELVGTDA
QSDLAVLKIK RSKPFPFVNF GDSRQARVGD WIIAIGNPFG LGGTVTSGII SAVYRATGGG
GAYDRYLQTD AAINRGNSGG PMFDMQGNVI GINNAIFSPT GGSVGIGFAI PAETAEPIVR
KLIAGERIER GYLGVQIQPV SEDLAASLGI PHNRGEFVQS VVPDGAAAKA GLRAGDVVVK
VAGKDVTPEQ TLSYIVANTA PGTRIPVELI RNGKRVTINA TVAARPSEDE LTQSYANPEE
EQDGFANPRT DGDQSYVAEK LGLSVTPLTA TIARQLGVSE DTKGLVIAAV DASSDAAGKG
LRRGDIVLSA NYREVATLAE LEAVIRSVQA EKREAILLRV QRRGQPAIYV PLRMR
//
