ID A0A2C1KVL2_9BACI Unreviewed; 740 AA.
AC A0A2C1KVL2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Peptidase S8 {ECO:0000313|EMBL:PGT89668.1};
GN ORFNames=COD11_03950 {ECO:0000313|EMBL:PGT89668.1};
OS Bacillus sp. AFS040349.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=2033502 {ECO:0000313|EMBL:PGT89668.1, ECO:0000313|Proteomes:UP000222674};
RN [1] {ECO:0000313|EMBL:PGT89668.1, ECO:0000313|Proteomes:UP000222674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AFS040349 {ECO:0000313|EMBL:PGT89668.1,
RC ECO:0000313|Proteomes:UP000222674};
RG Agbiome Team Llc;
RA Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA Shank E.A., Bowers A.;
RT "Large-scale bioinformatics analysis of Bacillus genomes uncovers conserved
RT roles of natural products in bacterial physiology.";
RL Submitted (SEP-2017) 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:PGT89668.1}.
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DR EMBL; NUMC01000014; PGT89668.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C1KVL2; -.
DR OrthoDB; 9798386at2; -.
DR Proteomes; UP000222674; 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; cd02133; PA_C5a_like; 1.
DR CDD; cd07474; Peptidases_S8_subtilisin_Vpr-like; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR046450; PA_dom_sf.
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; IPR034213; S8_Vpr-like.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52025; PA domain; 1.
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 Cell wall {ECO:0000256|ARBA:ARBA00022512};
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:UP000222674};
KW Secreted {ECO:0000256|ARBA:ARBA00022512};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..740
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039188019"
FT DOMAIN 134..523
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 342..410
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT ACT_SITE 143
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 183
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 472
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 740 AA; 80902 MW; 640E8CD93EBC35BF CRC64;
MGIKKVLYIM LITTICFPNM AIGETFPNRP PLPKESQEEN QKMMMIVKEE DFDYFKKRLE
SYPHITINQT YQNVFYGFSI EGQTNDIMTL KNDPAVIHSS PVVSYASQID ESVPFIGGDD
VRGLFDRSDH RLTGEGVKVA VIDTGVDYNH PDLRRSYLGG FDVIDGDQDP METMAKDGSE
TIHGTHVAGI IAANGKLKGV APEAEIIAYR ALGPGGMGTS DQVIAAIDRA IKDKVDIINL
SLGNNVNGPD WPTSLALDRA VEAGIVAVTS SGNSGPGLWT VGSPGTSSKA ISVGASSPPL
QMPYLKVGGI KEDISIHSLQ GAKSWQLKGL EEIVDAGLGY KNDIKDSVRG KVVLVERGKI
SFTEKVLNAK EKGAKAVLIS NNVKGNFAGA LEIPLDMPVA SISKEAGAAI RKQLKHHPSI
RTEYRKEQDQ LADFSSRGPV TSTWAIKPDV VAPGVAIEST VPDGYLALHG TSMAAPHVAG
ACALIKQAHP DWNPEQIKAS LMNTATKLTN DNEKVLKPNE QGAGRINIKE AVEAKVLVYP
GSLTFGQYET NHPRTKKTVK ITIDNQSNKE EHIYFDMPKN KPGVRWELPK NINIKPGEKK
QVEISLDLTP SQLTPGIHQG WLKLQQDGND IDVPYAYVVD EPNYPRIMGF EFAYSDEPEV
YKYRMYLPGG ADEVGIALYD LDTLAFVGYL DWFHDAPRGL VEKEVKLEET DIPEGNYKGV
IFANKSGKED FVETDILLGE
//
