ELYA_ALKHC
ID ELYA_ALKHC Reviewed; 361 AA.
AC P41363; Q53294; Q9KEJ7;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Thermostable alkaline protease;
DE EC=3.4.21.-;
DE Flags: Precursor;
GN OrderedLocusNames=BH0855;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AH-101 / JCM 9161 / FERM 10531;
RX PubMed=1369007; DOI=10.1007/bf00169427;
RA Takami H., Kobayashi T., Aono R., Horikoshi K.;
RT "Molecular cloning, nucleotide sequence and expression of the structural
RT gene for a thermostable alkaline protease from Bacillus sp. no. AH-101.";
RL Appl. Microbiol. Biotechnol. 38:101-108(1992).
RN [2]
RP SEQUENCE REVISION.
RA Takami H., Kobayashi T., Aono R., Horikoshi K.;
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
RN [4]
RP PROTEIN SEQUENCE OF 94-113.
RC STRAIN=AH-101 / JCM 9161 / FERM 10531;
RX PubMed=1370008; DOI=10.1007/bf00172544;
RA Takami H., Akiba T., Horikoshi K.;
RT "Characterization of an alkaline protease from Bacillus sp. no. AH-101.";
RL Appl. Microbiol. Biotechnol. 33:519-523(1990).
CC -!- FUNCTION: Shows keratinolytic activity.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 12-13.;
CC Temperature dependence:
CC Thermostable.;
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; D13158; BAA02443.2; -; Genomic_DNA.
DR EMBL; BA000004; BAB04574.1; -; Genomic_DNA.
DR PIR; G83756; G83756.
DR RefSeq; WP_010897028.1; NC_002570.2.
DR AlphaFoldDB; P41363; -.
DR SMR; P41363; -.
DR MEROPS; S08.046; -.
DR PRIDE; P41363; -.
DR EnsemblBacteria; BAB04574; BAB04574; BAB04574.
DR KEGG; bha:BH0855; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_011263_15_7_9; -.
DR OMA; SGQYSWI; -.
DR OrthoDB; 923655at2; -.
DR Proteomes; UP000001258; Chromosome.
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; IPR037045; S8pro/Inhibitor_I9_sf.
DR InterPro; IPR034202; Subtilisin_Carlsberg-like.
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 Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..93
FT /evidence="ECO:0000269|PubMed:1370008"
FT /id="PRO_0000027012"
FT CHAIN 94..361
FT /note="Thermostable alkaline protease"
FT /id="PRO_0000027013"
FT DOMAIN 97..360
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 124
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 154
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 307
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 255
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 257
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT VARIANT 38
FT /note="E -> D (in strain: AH-101)"
FT VARIANT 69..70
FT /note="KK -> EE (in strain: AH-101)"
FT VARIANT 74..77
FT /note="KLKK -> ELQN (in strain: AH-101)"
FT VARIANT 86
FT /note="K -> E (in strain: AH-101)"
FT VARIANT 104
FT /note="N -> S (in strain: AH-101)"
FT VARIANT 292
FT /note="N -> Y (in strain: AH-101)"
FT VARIANT 346..347
FT /note="PS -> SN (in strain: AH-101)"
SQ SEQUENCE 361 AA; 38116 MW; 24BF004F9E3E8474 CRC64;
MRQSLKVMVL STVALLFMAN PAAASEEKKE YLIVVEPEEV SAQSVEESYD VDVIHEFEEI
PVIHAELTKK ELKKLKKDPN VKAIEKNAEV TISQTVPWGI SFINTQQAHN RGIFGNGARV
AVLDTGIASH PDLRIAGGAS FISSEPSYHD NNGHGTHVAG TIAALNNSIG VLGVAPSADL
YAVKVLDRNG SGSLASVAQG IEWAINNNMH IINMSLGSTS GSSTLELAVN RANNAGILLV
GAAGNTGRQG VNYPARYSGV MAVAAVDQNG QRASFSTYGP EIEISAPGVN VNSTYTGNRY
VSLSGTSMAT PHVAGVAALV KSRYPSYTNN QIRQRINQTA TYLGSPSLYG NGLVHAGRAT
Q
