ID A0A1Y5SC28_9RHOB Unreviewed; 467 AA.
AC A0A1Y5SC28;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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:SLN37210.1};
GN ORFNames=PEL8287_01779 {ECO:0000313|EMBL:SLN37210.1};
OS Roseovarius litorisediminis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=1312363 {ECO:0000313|EMBL:SLN37210.1, ECO:0000313|Proteomes:UP000193827};
RN [1] {ECO:0000313|EMBL:SLN37210.1, ECO:0000313|Proteomes:UP000193827}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8287 {ECO:0000313|EMBL:SLN37210.1,
RC ECO:0000313|Proteomes:UP000193827};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-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 -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
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DR EMBL; FWFL01000004; SLN37210.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5SC28; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000193827; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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; IPR041489; PDZ_6.
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; 1.
DR Pfam; PF17820; PDZ_6; 1.
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, ECO:0000313|EMBL:SLN37210.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:SLN37210.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000193827};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..467
FT /note="Probable periplasmic serine endoprotease DegP-like"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038807070"
FT DOMAIN 265..356
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 362..459
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT ACT_SITE 117
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 147
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 221
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 467 AA; 49028 MW; 67AD605B42E4CE87 CRC64;
MAKVVSRLGQ TLAAILVFSM TFAAPGMSQT ADRPLYLNED GLPTLAPLLA EVTPAVVNIS
VESSRSVEMN PLFNDPFFRR FFDLQPPPQQ PQRRQQMSAG SGVIIDAEKG YVLTNHHVVE
NGDRITVTLK DRRQFDAELV GSDPGTDVAL VKIDAENLTA LDLGDSDRLQ VGDYVLAIGN
PFGLGQTVTS GIVSALGRSG LNIEGYEDFI QTDASINPGN SGGALVTLDG RLVGVNTAII
APSGGNVGIG FAVPANMAKA VVDQLIEFGE VQRGLLGVTI QDFTPDLGQA LGIEAGAGAV
VTQVEPDSAA EAAGLQPGDL IVSVDGRPVA GSADLRSQIG LKRTGRSIEI GIIRNGERQT
VVATLRRGPQ GGPQAGGHGL EWLSGADLRN LEPGDPLYGE MPGVLVVRLE SDSRAARSGL
EAGDIILAVN RVPVASVAEL REQLAKVDRA LALTIQRGSA RIFLIMR
//