ID A0A073JYX1_9BACI Unreviewed; 915 AA.
AC A0A073JYX1;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Peptidase S8 {ECO:0000313|EMBL:KEK19446.1};
GN ORFNames=BAMA_21880 {ECO:0000313|EMBL:KEK19446.1};
OS Bacillus manliponensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=574376 {ECO:0000313|EMBL:KEK19446.1, ECO:0000313|Proteomes:UP000027822};
RN [1] {ECO:0000313|EMBL:KEK19446.1, ECO:0000313|Proteomes:UP000027822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 15802 {ECO:0000313|EMBL:KEK19446.1,
RC ECO:0000313|Proteomes:UP000027822};
RA Lai Q., Liu Y., Shao Z.;
RT "Draft genome sequence of Bacillus manliponensis JCM 15802 (MCCC
RT 1A00708).";
RL Submitted (JUN-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:KEK19446.1}.
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DR EMBL; JOTN01000007; KEK19446.1; -; Genomic_DNA.
DR RefSeq; WP_034638746.1; NZ_JOTN01000007.1.
DR AlphaFoldDB; A0A073JYX1; -.
DR STRING; 574376.BAMA_21880; -.
DR eggNOG; COG1404; Bacteria.
DR OrthoDB; 9798386at2; -.
DR Proteomes; UP000027822; 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; cd07474; Peptidases_S8_subtilisin_Vpr-like; 1.
DR Gene3D; 2.60.40.4070; -; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR025965; FlgD/Vpr_Ig-like.
DR InterPro; IPR013783; Ig-like_fold.
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 InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF13860; FlgD_ig; 1.
DR Pfam; PF05922; Inhibitor_I9; 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:UP000027822};
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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..915
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001690688"
FT DOMAIN 65..158
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 195..571
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 383..467
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT DOMAIN 766..800
FT /note="FlgD/Vpr Ig-like"
FT /evidence="ECO:0000259|Pfam:PF13860"
FT REGION 88..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 204
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 237
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 531
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 915 AA; 99267 MW; 08F930F96DE50C95 CRC64;
MKKVTSGLLS MALVFSNFGV LSAHAEKKAQ EKQLSPQLET NMKQWGGNKI STEVDTQTSK
EISVIVELHH APMASMENIQ HAPDLQNNDA KSQEEQLKQA QENATKKIKE KVPQAKITET
YHTLFSGFAL SIPGNQITVL ASLPDVKAVY PNLTYKLHDT TQSAPSTENP NIGGPTIGAP
EAWNLQDLSG KALDGKGMKV AVIDSGVDYT HPDLQANYIG GYDTVDEDDD PMDGNVHGTH
VAGIIAANGK IKGIAPNASI LAYRVMNDMG FGTTEDIIEG IERAIQDDAD ILNLSLGQDL
NVPDQAVTRT LERAAKLGVT AVVSNGNDGP KPWSVDAPAN TSSVISVGAS TTSIPFPTFQ
VNGSKTIYQG LPLSTSDLTS KTSAPLVYVG YGSPSDYTKQ DVKGKFVLVD QGNSSTLVKA
EQAKQAGALG IFLVSSEQEI SIMPEYFYRQ NNAIPVVQLS NQHGEQLKAA VKKRAKTITI
GQPNMKELIG NFSSRGPSQG SWLVKPDFVA PGVQITSTVP NGGYESHNGT SMATPQVAGA
LALLRQMYPD WSTEQLKAAL SNTAKSLQDV NENTYPVMTQ GAGLINIPKA LQTETLVTPN
NVSFGFIKPD SGKIKLTQNI SLQNRSNKKK TYSTRVELLD SAKGIHTSFP SSISVKENSA
MEKPFTISIN RSLPQGVYTG ALYVKERGSD YEIRIPFTFS VDPKDYKRID GLEIINSTFS
PNGDDILDDN LIHYHLLSAV DDVTLHANLV TKEHVSYEGI IYQGQNESPG YKPFKWNGTR
ANGTELPDGL YQIEAVASNT GGETKQTGAV FIDRHAPQLS AEVDNENLFI KGKVDDILLD
WMTESGWIAP GLPVTMKYKI NGNGIWELPF VNTWEKSFDI YFDRTQLQEG NNTIHIVATD
AAGNTSELNV QLEVK
//
