SEPA_STAEP
ID SEPA_STAEP Reviewed; 507 AA.
AC P0C0Q3; P43148;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Extracellular elastase;
DE EC=3.4.24.-;
DE AltName: Full=SEPP1;
DE Flags: Precursor;
GN Name=sepA;
OS Staphylococcus epidermidis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1282;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 208-222.
RC STRAIN=TU 3298 / DSM 3095;
RX PubMed=8320236; DOI=10.1128/jb.175.13.4218-4224.1993;
RA Teufel P.;
RT "Characterization of an extracellular metalloprotease with elastase
RT activity from Staphylococcus epidermidis.";
RL J. Bacteriol. 175:4218-4224(1993).
CC -!- FUNCTION: Protease that has a low substrate specificity. Glucagon is
CC preferentially cleaved between aromatic (Phe) and hydrophobic (Val)
CC amino acids. Hydrolyzes casein and elastin.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 3 Ca(2+) ions per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5-7.;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the peptidase M4 family. {ECO:0000305}.
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DR EMBL; X69957; CAA49579.1; -; Genomic_DNA.
DR PIR; A40659; A40659.
DR AlphaFoldDB; P0C0Q3; -.
DR SMR; P0C0Q3; -.
DR MEROPS; M04.009; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.390.10; -; 1.
DR InterPro; IPR011096; FTP_domain.
DR InterPro; IPR025711; PepSY.
DR InterPro; IPR023612; Peptidase_M4.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR001570; Peptidase_M4_C_domain.
DR InterPro; IPR013856; Peptidase_M4_domain.
DR Pfam; PF07504; FTP; 1.
DR Pfam; PF03413; PepSY; 1.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 1.
DR PRINTS; PR00730; THERMOLYSIN.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT PROPEP 29..207
FT /evidence="ECO:0000269|PubMed:8320236"
FT /id="PRO_0000028620"
FT CHAIN 208..507
FT /note="Extracellular elastase"
FT /id="PRO_0000028621"
FT ACT_SITE 352
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 435
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 347
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 355
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 375
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 386
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 386
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 388
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 389
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 389
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 391
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 394
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 394
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 397
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 398
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 401
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 404
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 507 AA; 55814 MW; 62305238A73A2308 CRC64;
MKNFSKFALT SIAALTVASP LVNTEVDAKD KVSATQNIDA KVTQESQATD ALKELPKSEN
IKKHYKDYKV TDTEKDNKGF THYTLQPKVG NTYAPDKEVK VHTNKEGKVV LVNGDTDAKK
VQPTNKVSIS KESATDKAFE AIKIDRQKAK NLKSDVIKTN KVEIDGEKNK YVYNIEIITT
SPKISHWNVK IDAETGQVVD KLNMIKEAAT TGTGKGVLGD TKQININSVS GGYALQDLTQ
QGTLSAYNYD ANTGQAYLMQ DKDRNFDDDE QRAGVDANYY AKETYDYYKN TFGRESYDNQ
GSPIISLAHV NNFQGQDNRN NAAWIGDKMI YGDGDGRTFT ALSGANDVVA HEITHGVTQQ
TANLVYRSQS GALNESFSDV FGYFVDDEDF LMGEDVYTPG VGGDALRSMS NPERFGQPSH
MNDFVYTNSD NGGVHTNSGI PNKAAYNTIR SIGKQRSEQI YYRALTVYLT SNSDFQDAKA
SLQQAALDLY GEGIAQQVGQ AWDSVGV
