ID A0A150L1G7_9BACI Unreviewed; 664 AA.
AC A0A150L1G7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Cell wall-associated serine proteinase {ECO:0000313|EMBL:KYD05939.1};
DE EC=3.4.21.96 {ECO:0000313|EMBL:KYD05939.1};
GN ORFNames=B4102_3112 {ECO:0000313|EMBL:KYD05939.1};
OS Heyndrickxia sporothermodurans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Heyndrickxia.
OX NCBI_TaxID=46224 {ECO:0000313|EMBL:KYD05939.1, ECO:0000313|Proteomes:UP000075666};
RN [1] {ECO:0000313|EMBL:KYD05939.1, ECO:0000313|Proteomes:UP000075666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4102 {ECO:0000313|EMBL:KYD05939.1,
RC ECO:0000313|Proteomes:UP000075666};
RA Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., Holsappel S.,
RA Eijlander R.T., Kuipers O.P.;
RT "Genome Sequences of Twelve Sporeforming Bacillus Species Isolated from
RT Foods.";
RL Submitted (JAN-2016) 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:KYD05939.1}.
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DR EMBL; LQYN01000053; KYD05939.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150L1G7; -.
DR STRING; 46224.B4102_3112; -.
DR PATRIC; fig|46224.3.peg.3081; -.
DR Proteomes; UP000075666; 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; cd07475; Peptidases_S8_C5a_Peptidase; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR034216; C5a_Peptidase.
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 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:UP000075666};
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..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..664
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007564096"
FT DOMAIN 198..650
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 449..533
FT /note="PA"
FT /evidence="ECO:0000259|Pfam:PF02225"
FT REGION 643..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 207
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 272
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 602
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 664 AA; 72814 MW; 189F30C336D03BD5 CRC64;
MKRRSRRSIP YKIISMGILA ALLISGSNYS FAKTEQTSNQ SKVNVESIVQ KGQEILREQK
QKANLDAKNK LGITKADINK ATNKPFAPKE KVRLIVELTD EPLMDIKTSV FEEKKKLKTH
DQVINQITKK RIKTKLRHQF VRGFNGFSIE TEFRNMETIK KIDGVANVSI AKTYSEAMKS
SKSIVQAQQV WEELGLKGEG MLVGVVDSGV DYRHKDMVMS DEGKEKAKLT KENIQNKLDE
TKVDDRWYTD KVPTGYDWAD KDDDVLPYES SHGMHVSGTI GANGDEENNG VKGIAPNVQI
LAEKVFSDNG GGAYEDDIVA GINHAVEMGA DVINLSLGSD GGFVGEEDDT VQKAIRLATN
NGVLVVAAGG NAYYSTKNDK LSSSKKPYAE NPDIGILGSP GVSPFALQVA SYENNVVHKP
SLKLTTGDEI AFYEPSYLKL KKAMEKGKEY PLVFAGKGSA NDYKNIDVKD KIAVVQPDID
LGINSHLQFN VQDKGAKAVI IAPTPKWGDY KESDFSPYSI PAVVTSVKDG KKLINELQNG
QSVSAQLSGG LWVQNPNHDE MSDFSSIGAP HTLDFKPEIT SPGGGIYSTV FDNQYDVYSG
TSMATPHVVG GATLVLQSFY EKGLPKSMNT VLKTKTALMN TSKIEYDPNS NNKIPYSPRK
QGQE
//
