ID A0A0Q8QAE7_9SPHN Unreviewed; 428 AA.
AC A0A0Q8QAE7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:KRB82751.1};
GN ORFNames=ASE00_12040 {ECO:0000313|EMBL:KRB82751.1};
OS Sphingomonas sp. Root710.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736594 {ECO:0000313|EMBL:KRB82751.1, ECO:0000313|Proteomes:UP000051854};
RN [1] {ECO:0000313|EMBL:KRB82751.1, ECO:0000313|Proteomes:UP000051854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root710 {ECO:0000313|EMBL:KRB82751.1,
RC ECO:0000313|Proteomes:UP000051854};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB82751.1, ECO:0000313|Proteomes:UP000051854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root710 {ECO:0000313|EMBL:KRB82751.1,
RC ECO:0000313|Proteomes:UP000051854};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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:KRB82751.1}.
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DR EMBL; LMIB01000012; KRB82751.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q8QAE7; -.
DR STRING; 1736594.ASE00_12040; -.
DR OrthoDB; 5405281at2; -.
DR Proteomes; UP000051854; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05561; Peptidases_S8_4; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000051854};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..428
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006353123"
FT DOMAIN 188..419
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 196
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 224
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 375
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 428 AA; 42286 MW; B2CF0956A9B35B7D CRC64;
MPVPMLKGGR YLLLAALLTL SGATAAQLLP PLGRGLGEVT QGVDRLGDSV GATVSDTAAG
LGGIVDRLAR TRLDRLGALV RQNPQALEFD ARGDPAVKGE LIALDAPAPA LAAAAAEGFT
IVEQGEIEGL GIGSATLRAP NGVSLAKAEK QLARLIPGAT IQSNPIYQPS GVAAKGSGRP
VAVAASGPGA TIGLIDGGVA QHPALPGNIV QRGFAQGSPF PGDHGTAIAS ILVGQGAVRG
VSPQSRLLAA DIYGRDPRGG NALAIARALG WLAGSGAAVI NISLAGPPNP LLARAVAATD
KRGVLMVAAV GNDGAAAPPA FPASYPQVIA VTGIDERGRA LIEAGWATHL DFSAPGADLI
AAKAAGGVGK VRGTSFAAPF VAGRLARLSA GGMLSRARAV ALLSGEAAKG GSARLYGRGI
VCGPCATR
//
