ID A0A0J6FYF0_9BACI Unreviewed; 391 AA.
AC A0A0J6FYF0;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Alkaline serine protease {ECO:0000313|EMBL:KMM39392.1};
GN ORFNames=AB986_09375 {ECO:0000313|EMBL:KMM39392.1};
OS Alkalihalobacillus macyae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=157733 {ECO:0000313|EMBL:KMM39392.1, ECO:0000313|Proteomes:UP000035996};
RN [1] {ECO:0000313|EMBL:KMM39392.1, ECO:0000313|Proteomes:UP000035996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16346 {ECO:0000313|EMBL:KMM39392.1,
RC ECO:0000313|Proteomes:UP000035996};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Zheng C., Che J., Ge C., Shi H.,
RA Pan Z., Liu X.;
RL Submitted (JUN-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:KMM39392.1}.
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DR EMBL; LELK01000001; KMM39392.1; -; Genomic_DNA.
DR RefSeq; WP_048310562.1; NZ_LELK01000001.1.
DR AlphaFoldDB; A0A0J6FYF0; -.
DR STRING; 157733.AB986_09375; -.
DR OrthoDB; 9798386at2; -.
DR Proteomes; UP000035996; 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; cd07484; Peptidases_S8_Thermitase_like; 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; 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; IPR037045; S8pro/Inhibitor_I9_sf.
DR InterPro; IPR034084; Thermitase-like_dom.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 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:UP000035996};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..391
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005271657"
FT DOMAIN 142..377
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 150
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 183
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 337
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 391 AA; 41168 MW; 8AEE662037296303 CRC64;
MFKRLAAFAT SATLLMSVAL PASATNLEGK EAPSYANEQQ LAPQELIVHF NDSTKSTYAK
ELVSKHGGKV IETTDEFMVV KVNGSVTEAI KVLEENSSVE YAEPNSMFHA NHVPNDPFYK
TKQYAPQKVK AEQAWDVTQS NSSIKIAVID TGVDYNHPDL AGKVVKGYDF ADNDNDPMDE
HYHGTHVSGI AAANTNNGIG IAGLSPNASI LAVRVLDESG SGSLDDVAQG IRYAADQGAQ
VINLSLGGIL GSQTLKDAVN YAWNKGSVVV AAAGNESSPK PSYPAYYSNA IAVAATDQND
TIAYYSNYGT WVDIAAPGSS VYSTMPGNSY DNLSGTSMAS PVVAGVAGLL AAQGRSASEI
RTALEETADY ITGTGALFQN GRVNAANAVQ Y
//
