ID W0ALZ9_9SPHN Unreviewed; 508 AA.
AC W0ALZ9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=NX02_28995 {ECO:0000313|EMBL:AHE57368.1};
OS Sphingomonas sanxanigenens DSM 19645 = NX02.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1123269 {ECO:0000313|EMBL:AHE57368.1, ECO:0000313|Proteomes:UP000018851};
RN [1] {ECO:0000313|EMBL:AHE57368.1, ECO:0000313|Proteomes:UP000018851}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NX02 {ECO:0000313|EMBL:AHE57368.1,
RC ECO:0000313|Proteomes:UP000018851};
RA Ma T., Huang H., Wu M., Li X., Li G.;
RT "Completed genome of Sphingomonas sanxanigenens NX02.";
RL Submitted (JUL-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 -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
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DR EMBL; CP006644; AHE57368.1; -; Genomic_DNA.
DR RefSeq; WP_025295458.1; NZ_CP006644.1.
DR AlphaFoldDB; W0ALZ9; -.
DR STRING; 1123269.NX02_28995; -.
DR KEGG; ssan:NX02_28995; -.
DR PATRIC; fig|1123269.5.peg.5688; -.
DR eggNOG; COG0265; Bacteria.
DR HOGENOM; CLU_020120_1_0_5; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000018851; Chromosome.
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};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000018851};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..508
FT /note="Probable periplasmic serine endoprotease DegP-like"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039337839"
FT DOMAIN 285..337
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 404..496
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 375..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 118
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 155
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT ACT_SITE 229
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ SEQUENCE 508 AA; 52633 MW; 21EDB921E48D8170 CRC64;
MRYAYALTTA LLLGGTAATL VTNPLGAQVA QNDPQALASA PRAGAPLSFA DLAAKLQPAV
VNISTTQRVQ VATNPFEGTP FGNLFGGLQG GRPVTRQATS LGSGFIVSPD GYIVTNNHVI
SPDRRGNGTV EAITVIMPDR KEYKARLIGR DPQSDLAVLK IEAANLPFVR FGDSTRTRVG
DWVMAIGNPF GLGGTVTAGI VSALHRNTGS GGAYDRYIQT DASINQGNSG GPMFDLAGNV
IGINTAIFSP TGGNVGIGFA IPAEQAKPIV DTLMKGGSVE RGYLGVEIQQ LDDDSAGALG
LNKNEGELIA RTVPGEAADK AGIRQGDVIV KVNGRTVNPD QTLSFIVANL PVGTRVPIEL
IRDGKRMTLT ATVGKRPPED QLAGFARGED DEGFGDDSAP GDSEQATRGA LGIAVMPLTP
VIARQLGLDP AMQGVVVSSV DPSSEAAAKG LRRGDVISAV NSVTRVAVRT PADLDNAISA
ARRAGRNSVL LLVTRGNQST YVGVPIKQ
//
