PRTM_ALKCK
ID PRTM_ALKCK Reviewed; 380 AA.
AC Q99405; Q5WK05;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=M-protease {ECO:0000303|PubMed:15299321};
DE EC=3.4.21.- {ECO:0000269|PubMed:7632397};
DE Flags: Precursor;
GN Name=aprE; OrderedLocusNames=ABC0761;
OS Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=66692;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSM-K16;
RA Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA Kawai S., Ito S., Horikoshi K.;
RT "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT K16.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 112-134, FUNCTION, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC STRAIN=KSM-K16;
RX PubMed=7632397; DOI=10.1007/bf00218452;
RA Kobayashi T., Hakamada Y., Adachi S., Hitomi J., Yoshimatsu T., Koike K.,
RA Kawai S., Ito S.;
RT "Purification and properties of an alkaline protease from alkalophilic
RT Bacillus sp. KSM-K16.";
RL Appl. Microbiol. Biotechnol. 43:473-481(1995).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 112-380 IN COMPLEX WITH CALCIUM,
RP COFACTOR, AND SUBUNIT.
RX PubMed=15299321; DOI=10.1107/s0907444994009960;
RA Yamane T., Kani T., Hatanaka T., Suzuki A., Ashida T., Kobayashi T.,
RA Ito S., Yamashita O.;
RT "Structure of a new alkaline serine protease (M-protease) from Bacillus sp.
RT KSM-K16.";
RL Acta Crystallogr. D 51:199-206(1995).
CC -!- FUNCTION: Alkaline serine protease that cleaves various substrates,
CC including N-succinyl-Ala-Ala-Pro-Phe-pNA, N-succinyl-Ala-Ala-Pro-
CC MetpNA, oxidized insulin B chain, casein, hemoglobin and
CC scleroproteins, such as keratin, alpha-keratin and elastin.
CC {ECO:0000269|PubMed:7632397}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:15299321};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000269|PubMed:15299321};
CC -!- ACTIVITY REGULATION: Activity is inhibited by phenylmethylsulfonyl
CC fluoride and chymostatin. {ECO:0000269|PubMed:7632397}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.8 mM for N-succinyl-Ala-Ala-Pro-Phe-pNA
CC {ECO:0000269|PubMed:7632397};
CC KM=1.01 mM for N-succinyl-Ala-Ala-Pro-Met-pNA
CC {ECO:0000269|PubMed:7632397};
CC pH dependence:
CC Optimum pH is 12.3. {ECO:0000269|PubMed:7632397};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius. CaC1(2) markedly shifts
CC the optimum temperature to 70 degrees Celsius.
CC {ECO:0000269|PubMed:7632397};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15299321}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:7632397}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; AP006627; BAD63300.1; -; Genomic_DNA.
DR RefSeq; WP_011245616.1; NC_006582.1.
DR PDB; 1MPT; X-ray; 2.40 A; A=112-380.
DR PDB; 1WSD; X-ray; 1.50 A; A=112-380.
DR PDBsum; 1MPT; -.
DR PDBsum; 1WSD; -.
DR AlphaFoldDB; Q99405; -.
DR SMR; Q99405; -.
DR MEROPS; S08.010; -.
DR EnsemblBacteria; BAD63300; BAD63300; ABC0761.
DR KEGG; bcl:ABC0761; -.
DR eggNOG; COG1404; Bacteria.
DR HOGENOM; CLU_011263_15_7_9; -.
DR OMA; SGQYSWI; -.
DR OrthoDB; 923655at2; -.
DR EvolutionaryTrace; Q99405; -.
DR Proteomes; UP000001168; 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; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR InterPro; IPR034202; Subtilisin_Carlsberg-like.
DR Pfam; PF05922; Inhibitor_I9; 1.
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; Reference proteome; Secreted; Serine protease; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT PROPEP 28..111
FT /evidence="ECO:0000269|PubMed:7632397"
FT /id="PRO_0000027142"
FT CHAIN 112..380
FT /note="M-protease"
FT /id="PRO_0000027143"
FT DOMAIN 34..111
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 116..379
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 143
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 173
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 326
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT BINDING 113
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15299321,
FT ECO:0007744|PDB:1MPT, ECO:0007744|PDB:1WSD"
FT BINDING 151
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15299321,
FT ECO:0007744|PDB:1MPT, ECO:0007744|PDB:1WSD"
FT BINDING 184
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15299321,
FT ECO:0007744|PDB:1MPT, ECO:0007744|PDB:1WSD"
FT BINDING 186
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15299321,
FT ECO:0007744|PDB:1WSD"
FT BINDING 188
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15299321,
FT ECO:0007744|PDB:1MPT, ECO:0007744|PDB:1WSD"
FT BINDING 190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15299321,
FT ECO:0007744|PDB:1MPT, ECO:0007744|PDB:1WSD"
FT BINDING 274
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15299321,
FT ECO:0007744|PDB:1MPT"
FT BINDING 276
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15299321,
FT ECO:0007744|PDB:1MPT"
FT BINDING 279
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15299321,
FT ECO:0007744|PDB:1MPT"
FT BINDING 302
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15299321,
FT ECO:0007744|PDB:1MPT"
FT HELIX 117..121
FT /evidence="ECO:0007829|PDB:1WSD"
FT HELIX 124..129
FT /evidence="ECO:0007829|PDB:1WSD"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:1WSD"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:1WSD"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:1WSD"
FT HELIX 173..182
FT /evidence="ECO:0007829|PDB:1WSD"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:1WSD"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:1WSD"
FT HELIX 213..225
FT /evidence="ECO:0007829|PDB:1WSD"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:1WSD"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:1WSD"
FT HELIX 242..254
FT /evidence="ECO:0007829|PDB:1WSD"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:1WSD"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:1WSD"
FT STRAND 279..285
FT /evidence="ECO:0007829|PDB:1WSD"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:1WSD"
FT STRAND 301..306
FT /evidence="ECO:0007829|PDB:1WSD"
FT STRAND 308..314
FT /evidence="ECO:0007829|PDB:1WSD"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:1WSD"
FT STRAND 318..322
FT /evidence="ECO:0007829|PDB:1WSD"
FT HELIX 325..342
FT /evidence="ECO:0007829|PDB:1WSD"
FT HELIX 348..358
FT /evidence="ECO:0007829|PDB:1WSD"
FT HELIX 365..368
FT /evidence="ECO:0007829|PDB:1WSD"
FT HELIX 375..378
FT /evidence="ECO:0007829|PDB:1WSD"
SQ SEQUENCE 380 AA; 38881 MW; 9A916CFACD8E43E9 CRC64;
MKKPLGKIVA STALLISVAF SSSIASAAEE AKEKYLIGFN EQEAVSEFVE QIEANDDVAI
LSEEEEVEIE LLHEFETIPV LSVELSPEDV DALELDPTIS YIEEDAEVTT MAQSVPWGIS
RVQAPAAHNR GLTGSGVKVA VLDTGISTHP DLNIRGGASF VPGEPSTQDG NGHGTHVAGT
IAALNNSIGV LGVAPSAELY AVKVLGASGS GSVSSIAQGL EWAGNNGMHV ANLSLGSPSP
SATLEQAVNS ATSRGVLVVA ASGNSGAGSI SYPARYANAM AVGATDQNNN RASFSQYGAG
LDIVAPGVNV QSTYPGSTYA SLNGTSMATP HVAGVAALVK QKNPSWSNVQ IRNHLKNTAT
GLGNTNLYGS GLVNAEAATR
