ELYA_ALKCL
ID ELYA_ALKCL Reviewed; 380 AA.
AC P41362;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Alkaline protease;
DE EC=3.4.21.-;
DE Flags: Precursor;
OS Alkalihalobacillus clausii (Bacillus clausii).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=79880;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 21522 / DSM 2512 / JCM 9139 / LMG 18518 / 221;
RX PubMed=1368952; DOI=10.1271/bbb.56.1455;
RA Takami H., Kobayashi T., Kobayashi M., Yamamoto M., Nakamura S., Aono R.,
RA Horikoshi K.;
RT "Molecular cloning, nucleotide sequence, and expression of the structural
RT gene for alkaline serine protease from alkaliphilic Bacillus sp. 221.";
RL Biosci. Biotechnol. Biochem. 56:1455-1460(1992).
RN [2]
RP PROTEIN SEQUENCE OF 112-129.
RC STRAIN=ATCC 21522 / DSM 2512 / JCM 9139 / LMG 18518 / 221;
RA Horikoshi K.;
RL (In) Horikoshi K. (eds.);
RL Microorganisms in alkaline evironments, pp.187-194, VCH, Weinheim (1991).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; S48754; AAC60420.1; -; Genomic_DNA.
DR EMBL; D13157; BAA02442.1; -; Genomic_DNA.
DR AlphaFoldDB; P41362; -.
DR SMR; P41362; -.
DR MEROPS; S08.003; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07477; Peptidases_S8_Subtilisin_subset; 1.
DR Gene3D; 3.30.70.80; -; 1.
DR Gene3D; 3.40.50.200; -; 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; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR InterPro; IPR034202; Subtilisin_Carlsberg-like.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 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 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Hydrolase; Metal-binding; Protease;
KW Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT PROPEP 28..111
FT /evidence="ECO:0000269|Ref.2"
FT /id="PRO_0000027010"
FT CHAIN 112..380
FT /note="Alkaline protease"
FT /id="PRO_0000027011"
FT DOMAIN 34..111
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 116..379
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 143
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 173
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 326
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT BINDING 113
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 186
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 274
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 276
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 279
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 380 AA; 38826 MW; 5F73ABC68D5B6831 CRC64;
MKKPLGKIVA STALLISVAF SSSIASAAEE AKEKYLIGFN EQEAVSEFVE QVEANDEVAI
LSEEEEVEIE LLHEFETIPV LSVELSPEDV DALELDPAIS YIEEDAEVTT MAQSVPWGIS
RVQAPAAHNR GLTGSGVKVA VLDTGISTHP DLNIRGGASF VPGEPSTQDG NGHGTHVAGT
IAALNNSIGV LGVAPSAELY AVKVLGASGS GSVSSIAQGL EWAGNNGMHV ANLSLGSPSP
SATLEQAVNS ATSRGVLVVA ASGNSGAGSI SYPARYANAM AVGATDQNNN RASFSQYGAG
LDIVAPGVNV QSTYPGSTYA SLNGTSMATP HVAGAAALVK QKNPSWSNVQ IRNHLKNTAT
SLGSTNLYGS GLVNAEAATR
