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Membrane-bound protease PH1510 (EC 3.4.21.-) (NfeD homolog) (Stomatin operon partner protein) (STOPP)

 STOPP_PYRHO             Reviewed;         441 AA.
O59179;
14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
22-NOV-2017, entry version 98.
RecName: Full=Membrane-bound protease PH1510;
EC=3.4.21.-;
AltName: Full=NfeD homolog;
AltName: Full=Stomatin operon partner protein;
Short=STOPP;
Flags: Precursor;
OrderedLocusNames=PH1510;
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 /
NBRC 100139 / OT-3).
Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
Pyrococcus.
NCBI_TaxID=70601;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
PubMed=9679194; DOI=10.1093/dnares/5.2.55;
Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y.,
Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y.,
Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y.,
Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K.,
Masuchi Y., Shizuya H., Kikuchi H.;
"Complete sequence and gene organization of the genome of a hyper-
thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
DNA Res. 5:55-76(1998).
[2]
FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF
THR-62; SER-97; LYS-138 AND ASP-168, AND ENZYME REGULATION.
STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
PubMed=15611110; DOI=10.1074/jbc.M411748200;
Yokoyama H., Matsui I.;
"A novel thermostable membrane protease forming an operon with a
stomatin homolog from the hyperthermophilic archaebacterium Pyrococcus
horikoshii.";
J. Biol. Chem. 280:6588-6594(2005).
[3]
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 16-236, SUBUNIT, AND
FUNCTION.
STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
PubMed=16574150; DOI=10.1016/j.jmb.2006.02.052;
Yokoyama H., Matsui E., Akiba T., Harata K., Matsui I.;
"Molecular structure of a novel membrane protease specific for a
stomatin homolog from the hyperthermophilic archaeon Pyrococcus
horikoshii.";
J. Mol. Biol. 358:1152-1164(2006).
[4]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 16-236 OF MUTANT ALA-138,
AND SUBUNIT.
STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
PubMed=18421152; DOI=10.1107/S0909049507068471;
Yokoyama H., Hamamatsu S., Fujii S., Matsui I.;
"Novel dimer structure of a membrane-bound protease with a catalytic
Ser-Lys dyad and its linkage to stomatin.";
J. Synchrotron Radiat. 15:254-257(2008).
[5]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 16-236 OF MUTANT ALA-138 IN
COMPLEX WITH SUBSTRATE PEPTIDE, AND SUBUNIT.
STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
PubMed=22475127; DOI=10.1021/bi300098k;
Yokoyama H., Takizawa N., Kobayashi D., Matsui I., Fujii S.;
"Crystal structure of a membrane stomatin-specific protease in complex
with a substrate peptide.";
Biochemistry 51:3872-3880(2012).
[6]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 16-236 OF MUTANT ALA-138,
AND FUNCTION.
STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
PubMed=24121343; DOI=10.1107/S0909049513021328;
Yokoyama H., Kobayashi D., Takizawa N., Fujii S., Matsui I.;
"Structural and biochemical analysis of a thermostable membrane-bound
stomatin-specific protease.";
J. Synchrotron Radiat. 20:933-937(2013).
-!- FUNCTION: Protease that cleaves its substrates preferentially near
hydrophobic or aromatic amino acid residues. Can degrade casein
and the stomatin homolog PH1511 (in vitro).
{ECO:0000269|PubMed:15611110, ECO:0000269|PubMed:16574150,
ECO:0000269|PubMed:24121343}.
-!- ENZYME REGULATION: Inhibited by divalent metal cations, including
Mg(2+), Mn(2+), Ca(2+) and Zn(2+). Mildly inhibited by 0.01 % SDS
and 0.1% dodecyl-beta-D-maltoside. Activity is nearly abolished by
1 % SDS. {ECO:0000269|PubMed:15611110}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 5-6. {ECO:0000269|PubMed:15611110};
Temperature dependence:
Optimum temperature is above 90 degrees Celsius.
{ECO:0000269|PubMed:15611110};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15611110,
ECO:0000269|PubMed:16574150, ECO:0000269|PubMed:18421152,
ECO:0000269|PubMed:22475127}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
protein {ECO:0000305}.
-!- SIMILARITY: Belongs to the peptidase S14 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; BA000001; BAA30618.1; -; Genomic_DNA.
PIR; B71027; B71027.
RefSeq; WP_010885587.1; NC_000961.1.
PDB; 2DEO; X-ray; 3.00 A; A/B=16-236.
PDB; 3BPP; X-ray; 2.30 A; A=16-236.
PDB; 3VIV; X-ray; 2.25 A; A/B=16-236.
PDB; 3WG5; X-ray; 2.40 A; A/B=16-236.
PDB; 3WWV; X-ray; 2.40 A; A=371-441.
PDBsum; 2DEO; -.
PDBsum; 3BPP; -.
PDBsum; 3VIV; -.
PDBsum; 3WG5; -.
PDBsum; 3WWV; -.
ProteinModelPortal; O59179; -.
SMR; O59179; -.
STRING; 70601.PH1510; -.
MEROPS; S49.005; -.
TCDB; 8.A.21.2.1; the stomatin/podocin/band 7/nephrosis,2/spfh (stomatin) family.
EnsemblBacteria; BAA30618; BAA30618; BAA30618.
GeneID; 1443826; -.
KEGG; pho:PH1510; -.
eggNOG; arCOG01910; Archaea.
eggNOG; COG1030; LUCA.
HOGENOM; HOG000217027; -.
KO; K07403; -.
OMA; QMDTPGG; -.
OrthoDB; POG093Z040N; -.
BioCyc; PHOR70601:GJWR-1509-MONOMER; -.
BRENDA; 3.4.21.B56; 5244.
EvolutionaryTrace; O59179; -.
Proteomes; UP000000752; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
CDD; cd07015; Clp_protease_NfeD; 1.
InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
InterPro; IPR023562; ClpP/TepA.
InterPro; IPR002810; NfeD-like_C.
InterPro; IPR033853; PH1510-N.
Pfam; PF00574; CLP_protease; 1.
Pfam; PF01957; NfeD; 1.
SUPFAM; SSF52096; SSF52096; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Hydrolase; Membrane; Protease;
Serine protease; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 441 Membrane-bound protease PH1510.
/FTId=PRO_0000429022.
TRANSMEM 239 259 Helical. {ECO:0000255}.
TRANSMEM 271 291 Helical. {ECO:0000255}.
TRANSMEM 307 327 Helical. {ECO:0000255}.
TRANSMEM 344 364 Helical. {ECO:0000255}.
REGION 64 67 Substrate binding.
REGION 119 124 Substrate binding.
ACT_SITE 97 97 Nucleophile.
ACT_SITE 138 138 Proton donor/acceptor.
MUTAGEN 62 62 T->A: Reduces enzyme activity by over
90%. {ECO:0000269|PubMed:15611110}.
MUTAGEN 97 97 S->A: Abolishes enzyme activity.
{ECO:0000269|PubMed:15611110}.
MUTAGEN 138 138 K->A: Reduces enzyme activity by 99%.
{ECO:0000269|PubMed:15611110}.
MUTAGEN 168 168 D->A: Reduces enzyme activity by 97%.
{ECO:0000269|PubMed:15611110}.
STRAND 23 31 {ECO:0000244|PDB:3VIV}.
HELIX 35 50 {ECO:0000244|PDB:3VIV}.
STRAND 54 63 {ECO:0000244|PDB:3VIV}.
HELIX 67 78 {ECO:0000244|PDB:3VIV}.
STRAND 84 88 {ECO:0000244|PDB:3VIV}.
STRAND 94 96 {ECO:0000244|PDB:3VIV}.
HELIX 98 104 {ECO:0000244|PDB:3VIV}.
STRAND 106 111 {ECO:0000244|PDB:3VIV}.
STRAND 116 118 {ECO:0000244|PDB:3VIV}.
STRAND 122 126 {ECO:0000244|PDB:3VIV}.
STRAND 128 130 {ECO:0000244|PDB:3BPP}.
STRAND 132 134 {ECO:0000244|PDB:3VIV}.
HELIX 137 153 {ECO:0000244|PDB:3VIV}.
HELIX 158 166 {ECO:0000244|PDB:3VIV}.
HELIX 173 178 {ECO:0000244|PDB:3VIV}.
STRAND 183 185 {ECO:0000244|PDB:3VIV}.
HELIX 189 196 {ECO:0000244|PDB:3VIV}.
STRAND 218 221 {ECO:0000244|PDB:3VIV}.
HELIX 226 236 {ECO:0000244|PDB:3VIV}.
HELIX 376 379 {ECO:0000244|PDB:3WWV}.
STRAND 383 388 {ECO:0000244|PDB:3WWV}.
STRAND 390 398 {ECO:0000244|PDB:3WWV}.
STRAND 401 409 {ECO:0000244|PDB:3WWV}.
STRAND 418 425 {ECO:0000244|PDB:3WWV}.
STRAND 428 433 {ECO:0000244|PDB:3WWV}.
SEQUENCE 441 AA; 48281 MW; 2E16ECFC4529C4E6 CRC64;
MRRILLSMIV LIFLASPILA KNIVYVAQIK GQITSYTYDQ FDRYITIAEQ DNAEAIIIEL
DTPGGRADAM MNIVQRIQQS KIPVIIYVYP PGASAASAGT YIALGSHLIA MAPGTSIGAC
RPILGYSQNG SIIEAPPKIT NYFIAYIKSL AQESGRNATI AEEFITKDLS LTPEEALKYG
VIEVVARDIN ELLKKSNGMK TKIPVNGRYV TLNFTNVEVR YLAPSFKDKL ISYITDPNVA
YLLLTLGIWA LIIGFLTPGW HVPETVGAIM IILAIIGFGY FGYNSAGILL IIVAMLFFIA
EALTPTFGLF TVAGLITFII GGILLFGGGE EYLVRKEVFS QLRILIITVG AILAAFFAFG
MAAVIRAHKK KARTGKEEMI GLIGTVVEEL NPEGMIKVRG ELWKARSKFN GKIEKGEKVR
VVDMDGLTLI VVRERKEGGE K


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