ID A0A0Q9EMU3_9GAMM Unreviewed; 545 AA.
AC A0A0Q9EMU3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Peptidase S8 {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASE45_09725 {ECO:0000313|EMBL:KRD69421.1};
OS Lysobacter sp. Root96.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1736612 {ECO:0000313|EMBL:KRD69421.1, ECO:0000313|Proteomes:UP000050805};
RN [1] {ECO:0000313|EMBL:KRD69421.1, ECO:0000313|Proteomes:UP000050805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root96 {ECO:0000313|EMBL:KRD69421.1,
RC ECO:0000313|Proteomes:UP000050805};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRD69421.1, ECO:0000313|Proteomes:UP000050805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root96 {ECO:0000313|EMBL:KRD69421.1,
RC ECO:0000313|Proteomes:UP000050805};
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 ECO:0000256|RuleBase:RU003355}.
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:KRD69421.1}.
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DR EMBL; LMJN01000002; KRD69421.1; -; Genomic_DNA.
DR RefSeq; WP_056305519.1; NZ_LMJN01000002.1.
DR AlphaFoldDB; A0A0Q9EMU3; -.
DR STRING; 1736612.ASE45_09725; -.
DR OrthoDB; 9790784at2; -.
DR Proteomes; UP000050805; 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 Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 2.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 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:UP000050805};
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..545
FT /note="Peptidase S8"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006371015"
FT DOMAIN 152..363
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 379..454
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 466..531
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 161
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 190
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 483
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 545 AA; 55509 MW; AAC3393AF34866F6 CRC64;
MKQSKLMYAL GLGLATMVAA TAAAAQEQPN PNRVWVKFKA GTASAAAGKS AGASTQSLGQ
RIQALRGKLS AARGGDAVLN YQFDRLNSAV MTLSSPEDIK ALRGNPDVES VEIDQPRYLQ
AQSVPYGIDQ VQARNVWDAN QDGVLDAGAA TGAGIKVCVI DSGLNKNHED FAGMTITGYP
AGWDTDTCGH GTHVAGTIAA ANNNTGVVGV SPGKVSLHIV KIFGSNGTNG GQHGQCSWTY
SSTLVDAANR CDAAGAKIIS MSLGGASSSV TEQNAFQTLA NNGVLSIAAA GNAGDASLSY
PASYPSVVSV AAVDSANVKA AFSQFNAAVD VAAPGVDTLS TYPMKNDPLV VGASSFAAIP
VAGSKQTTAS AGWVNGGLCQ ASSSTWRNKI VVCQRGTNTF VDKITKAKTG RALGVVIYNN
VAGDLRIGMY DANSNPVTTT LPAVGISKAD GETIVANLAG QTATVDATPS VSNTAYETMS
GTSMATPHVS GVAAVVWSSK PTATAAQVRD ALYTTAKDID AAGFDNNTGW GLVQTQAAIT
ELQSQ
//
