ID A0A257F024_9RHOB Unreviewed; 481 AA.
AC A0A257F024;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, 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=CFE34_04875 {ECO:0000313|EMBL:OYU19497.1};
OS Rhodobacteraceae bacterium PARR1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=2015578 {ECO:0000313|EMBL:OYU19497.1, ECO:0000313|Proteomes:UP000216502};
RN [1] {ECO:0000313|EMBL:OYU19497.1, ECO:0000313|Proteomes:UP000216502}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PARR1 {ECO:0000313|EMBL:OYU19497.1};
RA Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT formosa and its bacterial cohort.";
RL Submitted (JUN-2017) 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:OYU19497.1}.
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DR EMBL; NKIT01000019; OYU19497.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257F024; -.
DR Proteomes; UP000216502; 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:OYU19497.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000216502};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..481
FT /note="Probable periplasmic serine endoprotease DegP-like"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039661417"
FT DOMAIN 261..336
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 357..469
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 114
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 144
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 217
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 481 AA; 50288 MW; A44D943A60BC7E54 CRC64;
MVMPAFQPGR ALTAAVLGLS LALSAPIMSE ARGAPESFAD LAEQISPSVV NITTSSVVAA
STEDGPMVPE GSPFEDFFKE FQDRNGAPQE PRRSEALGSG FVISADGYIV TNNHVIDGAD
EIKIEFFSGK TLDAKLVGTD PKTDIALLKV ESEEALPFVQ FGNSDMMRVG DWVMAMGNPL
GQGFSVSAGI VSARGRELQG TYDDFIQTDA AINRGNSGGP LFNMEGQVIG VNTAILSPNG
GSIGIGFSMA SNVVSKVVDQ LKEFGQTRRG WLGVKIQDVT PDVAEAMGLV EAKGALVTDV
PDGPAKDAGM ASGDVITTFN GTAIDDARAL TRTVGDSPIG AAVPVLVMRD GKEVELQVTL
GRREDAEAAD VLPAAANPAV PEEKQMMGLT LQPLTTENAE QLGMPAGSEG LVVTAVDEAS
DAFEKGLRAG DVITEAGQQA VVSLKDLEDR VAEAKDGGRK SILLLVRREG NPRFVALPLD
Q
//
