ELYA_ALKAL
ID ELYA_ALKAL Reviewed; 380 AA.
AC P27693;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Alkaline protease;
DE EC=3.4.21.-;
DE Flags: Precursor;
OS Alkalihalobacillus alcalophilus (Bacillus alcalophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=1445;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PB92;
RX PubMed=2059048; DOI=10.1128/aem.57.4.901-909.1991;
RA van der Laan J.C., Gerritse G., Mulleners L.J.M., van der Hoek R.A.,
RA Quax W.J.;
RT "Cloning, characterization, and multiple chromosomal integration of a
RT Bacillus alkaline protease gene.";
RL Appl. Environ. Microbiol. 57:901-909(1991).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
RC STRAIN=PB92;
RX PubMed=1518788; DOI=10.1093/protein/5.5.405;
RA van der Laan J.C., Teplyakov A.V., Kelders H., Kalk K.H., Misset O.,
RA Mulleners L.J.M., Dijkstra B.W.;
RT "Crystal structure of the high-alkaline serine protease PB92 from Bacillus
RT alcalophilus.";
RL Protein Eng. 5:405-411(1992).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
RX PubMed=1447775; DOI=10.1016/0022-2836(92)90495-6;
RA Sobek H., Hecht H.-J., Aehle W., Schomburg D.;
RT "X-ray structure determination and comparison of two crystal forms of a
RT variant (Asn115Arg) of the alkaline protease from Bacillus alcalophilus
RT refined at 1.85-A resolution.";
RL J. Mol. Biol. 228:108-117(1992).
RN [4]
RP STRUCTURE BY NMR OF 112-380.
RC STRAIN=PB92;
RX PubMed=9115441; DOI=10.1016/s0969-2126(97)00208-6;
RA Martin J.R., Mulder F.A., Karimi-Nejad Y., van der Zwan J., Mariani M.,
RA Schipper D., Boelens R.;
RT "The solution structure of serine protease PB92 from Bacillus alcalophilus
RT presents a rigid fold with a flexible substrate-binding site.";
RL Structure 5:521-532(1997).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 2 calcium ions per subunit.;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M65086; AAA22212.1; -; Genomic_DNA.
DR PIR; A49778; A49778.
DR PDB; 1AH2; NMR; -; A=112-380.
DR PDBsum; 1AH2; -.
DR AlphaFoldDB; P27693; -.
DR SMR; P27693; -.
DR DrugBank; DB01973; O-Benzylsulfonyl-Serine.
DR MEROPS; S08.038; -.
DR SABIO-RK; P27693; -.
DR EvolutionaryTrace; P27693; -.
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 3D-structure; Calcium; Hydrolase; Metal-binding; Protease; Secreted;
KW Serine protease; Signal; Zymogen.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT PROPEP 28..112
FT /id="PRO_0000027008"
FT CHAIN 113..380
FT /note="Alkaline protease"
FT /id="PRO_0000027009"
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 BINDING 151
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 184
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 186
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 188
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 274
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 276
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 279
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:1AH2"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:1AH2"
FT HELIX 125..130
FT /evidence="ECO:0007829|PDB:1AH2"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:1AH2"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:1AH2"
FT HELIX 173..182
FT /evidence="ECO:0007829|PDB:1AH2"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:1AH2"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:1AH2"
FT HELIX 213..226
FT /evidence="ECO:0007829|PDB:1AH2"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:1AH2"
FT HELIX 242..252
FT /evidence="ECO:0007829|PDB:1AH2"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:1AH2"
FT TURN 272..275
FT /evidence="ECO:0007829|PDB:1AH2"
FT STRAND 276..279
FT /evidence="ECO:0007829|PDB:1AH2"
FT STRAND 282..291
FT /evidence="ECO:0007829|PDB:1AH2"
FT STRAND 303..306
FT /evidence="ECO:0007829|PDB:1AH2"
FT STRAND 310..314
FT /evidence="ECO:0007829|PDB:1AH2"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:1AH2"
FT STRAND 318..322
FT /evidence="ECO:0007829|PDB:1AH2"
FT HELIX 325..342
FT /evidence="ECO:0007829|PDB:1AH2"
FT HELIX 348..358
FT /evidence="ECO:0007829|PDB:1AH2"
FT STRAND 364..370
FT /evidence="ECO:0007829|PDB:1AH2"
FT HELIX 375..379
FT /evidence="ECO:0007829|PDB:1AH2"
SQ SEQUENCE 380 AA; 38853 MW; 539EA72771B6682C CRC64;
MKKPLGKIVA STALLISVAF SSSIASAAEE AKEKYLIGFN EQEAVSEFVE QVEANDEVAI
LSEEEEVEIE LLHEFETIPV LSVELSPEDV DALELDPAIS YIEEDAEVTT MAQSVPWGIS
RVQAPAAHNR GLTGSGVKVA VLDTGISTHP DLNIRGGASF VPGEPSTQDG NGHGTHVAGT
IAALNNSIGV LGVAPNAELY AVKVLGASGS GSVSSIAQGL EWAGNNGMHV ANLSLGSPSP
SATLEQAVNS ATSRGVLVVA ASGNSGAGSI SYPARYANAM AVGATDQNNN RASFSQYGAG
LDIVAPGVNV QSTYPGSTYA SLNGTSMATP HVAGAAALVK QKNPSWSNVQ IRNHLKNTAT
SLGSTNLYGS GLVNAEAATR
