ID A0A0A8X529_9BACI Unreviewed; 444 AA.
AC A0A0A8X529;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Probable secreted peptidase {ECO:0000313|EMBL:GAM14147.1};
GN ORFNames=SAMD00020551_2295 {ECO:0000313|EMBL:GAM14147.1};
OS Mesobacillus selenatarsenatis SF-1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX NCBI_TaxID=1321606 {ECO:0000313|EMBL:GAM14147.1, ECO:0000313|Proteomes:UP000031014};
RN [1] {ECO:0000313|EMBL:GAM14147.1, ECO:0000313|Proteomes:UP000031014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SF-1 {ECO:0000313|EMBL:GAM14147.1,
RC ECO:0000313|Proteomes:UP000031014};
RA Kuroda M., Sei K., Yamashita M., Ike M.;
RT "Whole genome shotgun sequence of Bacillus selenatarsenatis SF-1.";
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240, 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:GAM14147.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BASE01000046; GAM14147.1; -; Genomic_DNA.
DR RefSeq; WP_041965928.1; NZ_BASE01000046.1.
DR AlphaFoldDB; A0A0A8X529; -.
DR STRING; 1321606.SAMD00020551_2295; -.
DR MEROPS; S08.141; -.
DR Proteomes; UP000031014; 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; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 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:UP000031014};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 137..429
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 146
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 193
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 382
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 444 AA; 47143 MW; DE706D07DC4CA849 CRC64;
MKKINIFAVA LVLFSFILSP SFSSPKASLL SVELDPKLES LLANPLSNEE VELIITYKDM
PLLSDIKLLK LLGFEVNPFS ELPMVAVKGK IGLVNELLLT ATNILSIYAN DDLEYFLRDS
RALIGAEAVW NALGYTGKGV TVAVIDSGID ATHPDLQYGE KVIQNVKFIV GDLFGNQPLY
LENQLNTDTT SGHGTHVAGT IAGSGTSSDG LYKGVAPDAK LVGLGVGEAI NILWSLEAFD
YAIKNQEKYG IDIISNSWGS TGEYSPDHPI NIASKKAHDA GMTVVFAAGN EGPDDNTLNP
YSAAPWVISV AAGTKDKQLA DFSSRGVAGD EYLHPDITAP GVDIVATRSS TGIVMNLLGT
VTDVSYIDGV HLPYYTTSSG TSMAAPHISG VVALMKEANP SLNPDLALDL MIQTADPMPE
YQLHEVGAGY VNAYEAVQAA SSSK
//
