ID Q9FDF2_BACLI Unreviewed; 310 AA. AC Q9FDF2; DT 01-MAR-2001, integrated into UniProtKB/TrEMBL. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 114. DE SubName: Full=KerA {ECO:0000313|EMBL:AAG00494.1}; DE Flags: Fragment; OS Bacillus licheniformis. OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=1402 {ECO:0000313|EMBL:AAG00494.1}; RN [1] {ECO:0000313|EMBL:AAG00494.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=837B {ECO:0000313|EMBL:AAG00494.1}; RA Goldstein G., Wagner E.K., Lee Y.E., Masisak E.S., Oh J.; RT "Nucleotide sequence of kerA gene encoding a keratinolytic protease of RT Bacillus licheniformis OWU 837B."; RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0007829|PDB:4GI3} RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 37-310. RX PubMed=23075397; DOI=10.1111/febs.12033; RA Derache C., Epinette C., Roussel A., Gabant G., Cadene M., Korkmaz B., RA Gauthier F., Kellenberger C.; RT "Crystal structure of greglin, a novel non-classical Kazal inhibitor, in RT complex with subtilisin."; RL FEBS J. 279:4466-4478(2012). RN [3] {ECO:0007829|PDB:4HX2} RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 37-310 IN COMPLEX WITH CALCIUM RP AND ZINC. RX DOI=10.1039/C2SC21712K; RA Trillo-Muyo S., Martinez-Rodriguez S., Arolas J.L., Gomis-Ruth F.X.; RT "Mechanism of action of a Janus-faced single-domain protein inhibitor RT simultaneously targeting two peptidase classes."; RL Chem. Sci. 4:791-797(2013). CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; CC Evidence={ECO:0000256|ARBA:ARBA00001913}; CC -!- SIMILARITY: Belongs to the peptidase S8 family. CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240, CC ECO:0000256|RuleBase:RU003355}. 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; AF282895; AAG00494.1; -; Genomic_DNA. DR PIR; JC1085; JC1085. DR PDB; 4GI3; X-ray; 1.75 A; A=37-310. DR PDB; 4HX2; X-ray; 2.25 A; A/C=37-310. DR PDBsum; 4GI3; -. DR PDBsum; 4HX2; -. DR AlphaFoldDB; Q9FDF2; -. DR SMR; Q9FDF2; -. DR MEROPS; S08.001; -. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR CDD; cd07477; Peptidases_S8_Subtilisin_subset; 1. DR Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1. DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 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 PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1. DR PANTHER; PTHR43806; PEPTIDASE S8; 1. DR Pfam; PF00082; Peptidase_S8; 1. DR PRINTS; PR00723; SUBTILISIN. DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1. DR SUPFAM; SSF52743; Subtilisin-like; 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 {ECO:0007829|PDB:4GI3, ECO:0007829|PDB:4HX2}; KW Calcium {ECO:0007829|PDB:4HX2}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE- KW ProRule:PRU01240}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0007829|PDB:4HX2}; KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE- KW ProRule:PRU01240}; KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE- KW ProRule:PRU01240}; Zinc {ECO:0007829|PDB:4HX2}. FT DOMAIN 59..301 FT /note="Peptidase S8/S53" FT /evidence="ECO:0000259|Pfam:PF00082" FT ACT_SITE 68 FT /note="Charge relay system" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240" FT ACT_SITE 99 FT /note="Charge relay system" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240" FT ACT_SITE 256 FT /note="Charge relay system" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240" FT BINDING 38 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4HX2" FT BINDING 77 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4HX2" FT BINDING 110 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4HX2" FT BINDING 112 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4HX2" FT BINDING 114 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4HX2" FT BINDING 116 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:4HX2" FT BINDING 204 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4HX2" FT BINDING 206 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4HX2" FT BINDING 209 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:4HX2" FT BINDING 273 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0007829|PDB:4HX2" FT BINDING 310 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0007829|PDB:4HX2" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AAG00494.1" SQ SEQUENCE 310 AA; 31285 MW; 740B9816277876EA CRC64; RIINAAKAKL DKEALKEVKN DPDVAYVEED HVAHALAQTV PYGIPLIKAD KVQAQGFKGA NVKVAVLDTG IQASHPDLNV VGGASFVAGE AYNTDGNGHG THVAGTVAAL DNTTGVLGVA PSVSLYAVKV LNSSGSGSYS GIVSGIEWAT TNGMDVINMS LGGASGSTAM KQAVDNAYAR GVVVVAAAGN SGSSGNTNTI GYPAKYDSVI AVGAVDSNSN RASFSSVGAE LEVMAPGAGV YSTYPTNTYA TLNGTSMASP HVAGAAALIL SKHPNLSASQ VRNRLSSTAT YLGSSFYYGK GLINVEAAAQ //