ID A0A0Q6VCW6_9ACTN Unreviewed; 426 AA.
AC A0A0Q6VCW6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Peptidase S8/S53 domain-containing protein {ECO:0000259|Pfam:PF00082};
GN ORFNames=ASC64_19530 {ECO:0000313|EMBL:KQV72835.1};
OS Nocardioides sp. Root122.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736431 {ECO:0000313|EMBL:KQV72835.1, ECO:0000313|Proteomes:UP000051395};
RN [1] {ECO:0000313|EMBL:KQV72835.1, ECO:0000313|Proteomes:UP000051395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root122 {ECO:0000313|EMBL:KQV72835.1,
RC ECO:0000313|Proteomes:UP000051395};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV72835.1, ECO:0000313|Proteomes:UP000051395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root122 {ECO:0000313|EMBL:KQV72835.1,
RC ECO:0000313|Proteomes:UP000051395};
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:KQV72835.1}.
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DR EMBL; LMDE01000003; KQV72835.1; -; Genomic_DNA.
DR RefSeq; WP_056906505.1; NZ_LMDE01000003.1.
DR AlphaFoldDB; A0A0Q6VCW6; -.
DR STRING; 1736431.ASC64_19530; -.
DR OrthoDB; 5177045at2; -.
DR Proteomes; UP000051395; 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; cd00306; Peptidases_S8_S53; 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:UP000051395};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 162..391
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 169
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 205
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 426 AA; 46626 MW; 317B9D7CD6A42052 CRC64;
MSDWMIGDDR RRRTTDQLRA FRRANPEQVA WNTEAPADFT YLYHPDRVLV RRADVDEFEE
TARQVGDRLL KGQPQRDETT LLGGALVRYL LPERTSGESV PEVLDQLEAA GLTRGRATPD
HWVHVSPGGP GGSLCPAIEP QETGLKEPWP PQAPDTTDKR HDVRVVVVDT GWNPTSATDG
RTPWLDGVTG DDEQNGARLR RYAGHGTFIA GVIRCLVPHA TVHVDGFCIG GVGGGGILES
DMVDQLEEAM KRDPQVINLS AGCRTRMDYP SVAFQTFYDE HLEGRDCVLV AAAGNDSTAA
PFWPAAFDWA VGVGSLDRNG RISDFSNYGV SADVYALGRN HVNAFPDGSY KCRETPDKGD
IREFRTGMAR WSGTSFAAPI VAGLIAREIA EHGIPAADAR DHVLARAVYD SDPTVGPHME
LRHPHA
//
