THET_THEVU
ID THET_THEVU Reviewed; 279 AA.
AC P04072;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1986, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Thermitase;
DE EC=3.4.21.66;
OS Thermoactinomyces vulgaris.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Thermoactinomyces.
OX NCBI_TaxID=2026;
RN [1]
RP PROTEIN SEQUENCE.
RA Meloun B., Baudys M., Kostka V., Hausdorf G., Frommel C., Hohne W.E.;
RT "Complete primary structure of thermitase from Thermoactinomyces vulgaris
RT and its structural features related to the subtilisin-type proteinases.";
RL FEBS Lett. 183:195-200(1985).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=2647518; DOI=10.1016/0014-5793(89)81194-9;
RA Teplyakov A.V., Kuranova I.P., Harutyunyan E.H., Frommel C., Hohne W.E.;
RT "Crystal structure of thermitase from Thermoactinomyces vulgaris at 2.2-A
RT resolution.";
RL FEBS Lett. 244:208-212(1989).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS).
RX PubMed=2689655; DOI=10.1016/0022-2836(89)90336-7;
RA Gros P., Betzel C., Dauter Z., Wilson K.S., Hol W.G.J.;
RT "Molecular dynamics refinement of a thermitase-eglin-c complex at 1.98-A
RT resolution and comparison of two crystal forms that differ in calcium
RT content.";
RL J. Mol. Biol. 210:347-367(1989).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
RX PubMed=2196375; DOI=10.1016/0022-2836(90)90160-n;
RA Teplyakov A.V., Kuranova I.P., Harutyunyan E.H., Vainshtein B.K.,
RA Frommel C., Hohne W.E., Wilson K.S.;
RT "Crystal structure of thermitase at 1.4-A resolution.";
RL J. Mol. Biol. 214:261-279(1990).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=1993669; DOI=10.2210/pdb3tec/pdb;
RA Gros P., Kalk K.H., Hol W.G.J.;
RT "Calcium binding to thermitase. Crystallographic studies of thermitase at
RT 0, 5, and 100 mM calcium.";
RL J. Biol. Chem. 266:2953-2961(1991).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins, including collagen.; EC=3.4.21.66;
CC -!- COFACTOR:
CC Note=Binds 3 calcium ions or 2 calcium ions and 1 sodium ion per
CC subunit. The sodium ion is bound at calcium concentrations up to 5 mM.
CC At 100 mM calcium 3 calcium ions are bound.;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR PIR; A00973; SUMYTV.
DR PDB; 1TEC; X-ray; 2.20 A; E=1-279.
DR PDB; 1THM; X-ray; 1.37 A; A=1-279.
DR PDB; 2TEC; X-ray; 1.98 A; E=1-279.
DR PDB; 3TEC; X-ray; 2.00 A; E=1-279.
DR PDBsum; 1TEC; -.
DR PDBsum; 1THM; -.
DR PDBsum; 2TEC; -.
DR PDBsum; 3TEC; -.
DR AlphaFoldDB; P04072; -.
DR SMR; P04072; -.
DR MINT; P04072; -.
DR MEROPS; S08.007; -.
DR BRENDA; 3.4.21.66; 6282.
DR EvolutionaryTrace; P04072; -.
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; cd07484; Peptidases_S8_Thermitase_like; 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; IPR034084; Thermitase-like_dom.
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; Direct protein sequencing; Hydrolase; Metal-binding;
KW Protease; Secreted; Serine protease.
FT CHAIN 1..279
FT /note="Thermitase"
FT /id="PRO_0000076421"
FT DOMAIN 12..277
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 38
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 71
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 225
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT BINDING 5
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 47
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 60
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 62
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 82
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 85
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 87
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 89
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT HELIX 8..11
FT /evidence="ECO:0007829|PDB:1THM"
FT HELIX 14..17
FT /evidence="ECO:0007829|PDB:1THM"
FT HELIX 20..24
FT /evidence="ECO:0007829|PDB:1THM"
FT STRAND 33..39
FT /evidence="ECO:0007829|PDB:1THM"
FT TURN 46..51
FT /evidence="ECO:0007829|PDB:1THM"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:1THM"
FT TURN 58..61
FT /evidence="ECO:0007829|PDB:1THM"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1THM"
FT HELIX 71..80
FT /evidence="ECO:0007829|PDB:1THM"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:1THM"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:1THM"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:2TEC"
FT HELIX 112..124
FT /evidence="ECO:0007829|PDB:1THM"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:1THM"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:1THM"
FT HELIX 141..152
FT /evidence="ECO:0007829|PDB:1THM"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:1THM"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:1THM"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:1THM"
FT STRAND 178..184
FT /evidence="ECO:0007829|PDB:1THM"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:1THM"
FT STRAND 207..213
FT /evidence="ECO:0007829|PDB:1THM"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:1THM"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:1THM"
FT HELIX 224..239
FT /evidence="ECO:0007829|PDB:1THM"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:1THM"
FT HELIX 245..254
FT /evidence="ECO:0007829|PDB:1THM"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:3TEC"
FT TURN 260..264
FT /evidence="ECO:0007829|PDB:1THM"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:1THM"
FT HELIX 273..278
FT /evidence="ECO:0007829|PDB:1THM"
SQ SEQUENCE 279 AA; 28366 MW; 8065049BC8927AC0 CRC64;
YTPNDPYFSS RQYGPQKIQA PQAWDIAEGS GAKIAIVDTG VQSNHPDLAG KVVGGWDFVD
NDSTPQNGNG HGTHCAGIAA AVTNNSTGIA GTAPKASILA VRVLDNSGSG TWTAVANGIT
YAADQGAKVI SLSLGGTVGN SGLQQAVNYA WNKGSVVVAA AGNAGNTAPN YPAYYSNAIA
VASTDQNDNK SSFSTYGSVV DVAAPGSWIY STYPTSTYAS LSGTSMATPH VAGVAGLLAS
QGRSASNIRA AIENTADKIS GTGTYWAKGR VNAYKAVQY
