ID A0A099J2J1_9MICO Unreviewed; 488 AA.
AC A0A099J2J1;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Peptidase S8 {ECO:0000313|EMBL:KGJ72521.1};
GN ORFNames=GY21_14850 {ECO:0000313|EMBL:KGJ72521.1};
OS Cryobacterium roopkundense.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Cryobacterium.
OX NCBI_TaxID=1001240 {ECO:0000313|EMBL:KGJ72521.1, ECO:0000313|Proteomes:UP000029864};
RN [1] {ECO:0000313|EMBL:KGJ72521.1, ECO:0000313|Proteomes:UP000029864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RuG17 {ECO:0000313|EMBL:KGJ72521.1,
RC ECO:0000313|Proteomes:UP000029864};
RA Sisinthy S.;
RL Submitted (AUG-2014) 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:KGJ72521.1}.
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DR EMBL; JPXF01000068; KGJ72521.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099J2J1; -.
DR STRING; 1001240.GY21_14850; -.
DR eggNOG; COG1404; Bacteria.
DR Proteomes; UP000029864; 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; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; 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 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; 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:UP000029864};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..488
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001956327"
FT DOMAIN 180..478
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 188
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 229
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 420
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 488 AA; 49260 MW; F233C11BED580AF6 CRC64;
MSKTAGRRRG TAAGIALTAA LSAAFLAPGI ANAAPKPPPQ AEIIHGDVMN YAINVTKANN
GQTQKAERAV EQAGGEVVAS YAEIGVVIAQ SDNTVFADTL RLDKAVESVG ATRTAPVDTA
DATYRGDAAT TAPERRSAAV TKDMGVEAAG DVVADPRESE QWDMSLIGAD AAHQITDGDR
NVLVAVLDSG IEATHPDLAA NVDATVSAGC NSGVPNTAPE AWQPSTSSHG THVAGTIAAA
RNGVGIVGVA PDVRLSSVKV VNDDGFIYPE AAICGFMYAT STGADVTNNS YYIDPWMFWC
DNDADQAAVK TAVDRAVQYS QSKGVVNVAA AGNSNIDLAN KTTDASSPND TTPLLRAIDT
GCADIPAELD GVVTVSSTTN TSAKSGFSNY GLDVVDVAAP GSAILSTVTG GGYALYSGTS
MASPHAAGVA ALIKSTHPDM SGQALAGLLS GQATDVPCPV GSVQCVGSPA DNGFFGAGMV
NALAAVQK
//
