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ELYA_BACYA
ID   ELYA_BACYA              Reviewed;         378 AA.
AC   P20724;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Alkaline elastase YaB;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=ale;
OS   Bacillus sp. (strain YaB).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=72578;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2670913; DOI=10.1128/jb.171.9.5232-5236.1989;
RA   Kaneko R., Koyama N., Tsai Y.-C., Juang R.-Y., Yoda K., Yamasaki M.;
RT   "Molecular cloning of the structural gene for alkaline elastase YaB, a new
RT   subtilisin produced by an alkalophilic Bacillus strain.";
RL   J. Bacteriol. 171:5232-5236(1989).
RN   [2]
RP   PROTEIN SEQUENCE OF 111-164.
RA   Tsai Y.-C., Lin Y.-T., Li Y.-F., Yamasaki M., Tamura G.;
RT   "Characterization of an alkaline elastase from alkalophilic Bacillus Ya-
RT   B.";
RL   Biochim. Biophys. Acta 883:439-447(1986).
CC   -!- FUNCTION: Digests elastin efficiently, has a substrate preference for
CC       Ala in P1 position.
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; M28537; AAA87324.1; -; Genomic_DNA.
DR   AlphaFoldDB; P20724; -.
DR   SMR; P20724; -.
DR   MEROPS; S08.157; -.
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   Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   PROPEP          28..110
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="PRO_0000027014"
FT   CHAIN           111..378
FT                   /note="Alkaline elastase YaB"
FT                   /id="PRO_0000027015"
FT   DOMAIN          114..377
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        141
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        171
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        324
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   BINDING         111
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         149
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         182
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         272
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
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         277
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   378 AA;  38793 MW;  5A8FD8CC0C62687D CRC64;
     MNKKMGKIVA GTALIISVAF SSSIAQAAEE AKEKYLIGFK EQEVMSQFVD QIDGDEYSIS
     SQAEDVEIDL LHEFDFIPVL SVELDPEDVD ALELDPAIAY IEEDAEVTTM QTVPWGINRV
     QAPIAQSRGF TGTGVRVAVL DTGISNHADL RIRGGASFVP GEPNISDGNG HGTQVAGTIA
     ALNNSIGVLG VAPNVDLYGV KVLGASGSGS ISGIAQGLQW AANNGMHIAN MSLGSSAGSA
     TMEQAVNQAT ASGVLVVAAS GNSGAGNVGF PARYANAMAV GATDQNNNRA TFSQYGAGLD
     IVAPGVGVQS TVPGNGYASF NGTSMATPHV AGVAALVKQK NPSWSNVQIR NHLKNTATNL
     GNTTQFGSGL VNAEAATR
 
 
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