ID A0A0K9GAS6_9BACI Unreviewed; 418 AA.
AC A0A0K9GAS6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Peptidase S8 {ECO:0000313|EMBL:KMY43870.1};
GN ORFNames=AC622_06070 {ECO:0000313|EMBL:KMY43870.1};
OS Bacillus sp. FJAT-27916.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1679169 {ECO:0000313|EMBL:KMY43870.1, ECO:0000313|Proteomes:UP000036953};
RN [1] {ECO:0000313|Proteomes:UP000036953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-27916 {ECO:0000313|Proteomes:UP000036953};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Che J., Ge C., Shi H.,
RA Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (JUL-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:KMY43870.1}.
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DR EMBL; LFZV01000001; KMY43870.1; -; Genomic_DNA.
DR RefSeq; WP_049670249.1; NZ_LFZV01000001.1.
DR AlphaFoldDB; A0A0K9GAS6; -.
DR STRING; 1679169.AC622_06070; -.
DR PATRIC; fig|1679169.3.peg.1287; -.
DR OrthoDB; 9798386at2; -.
DR Proteomes; UP000036953; 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; EXTRACELLULAR PROTEASE; 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:UP000036953};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..418
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005524369"
FT DOMAIN 134..394
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 143
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 180
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 358
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 418 AA; 43170 MW; 2977753D6A793538 CRC64;
MKSKRLISTV VLSLAMVFSG ASFSSAAEMG KAPKESVQKE TIRVLIKGSQ SERAQAKKDM
GVHHDFNGQG FTVDVSEKEY EKLVKNNDIE VKKVPEFKIA ATNQLKATSS PTTRVPWGIK
AIYNNSSLTS TSGGSGIKVA VLDTGVLKTH KDLSSNVEQC KDFTTSSTYV NNSCADRNGH
GTHVAGTVLG NGGGGTGVYG VAPQAKLWAY KVLTDSGSGY SDDIAAAIRH AADQATSTGS
KLIISMSLGS SANDSLISSA VTYAQGKGVL IIAAAGNSGS AANTIGYPGA LANVVAVAAL
ENVQANGTYR VANYSSRGNP NTDGDYVIGV KDIEVSAPGS AVESTWYTGG YNTISGTSMA
TPHVSGLAAK IWASNTGYTA NQVRTVLQNR AKANDILGGV GAAVGDDYAS GFGFPRVQ
//