HTPX1_SACS2
ID HTPX1_SACS2 Reviewed; 311 AA.
AC Q97X95;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Protease HtpX homolog 1 {ECO:0000255|HAMAP-Rule:MF_00188};
DE EC=3.4.24.- {ECO:0000255|HAMAP-Rule:MF_00188};
GN Name=htpX1 {ECO:0000255|HAMAP-Rule:MF_00188}; Synonyms=htpX-1;
GN OrderedLocusNames=SSO1859;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00188};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00188};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00188};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00188}.
CC -!- SIMILARITY: Belongs to the peptidase M48B family. {ECO:0000255|HAMAP-
CC Rule:MF_00188}.
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DR EMBL; AE006641; AAK42047.1; -; Genomic_DNA.
DR PIR; H90348; H90348.
DR RefSeq; WP_009988523.1; NC_002754.1.
DR AlphaFoldDB; Q97X95; -.
DR STRING; 273057.SSO1859; -.
DR EnsemblBacteria; AAK42047; AAK42047; SSO1859.
DR GeneID; 44130609; -.
DR KEGG; sso:SSO1859; -.
DR PATRIC; fig|273057.12.peg.1909; -.
DR eggNOG; arCOG01331; Archaea.
DR HOGENOM; CLU_042266_4_1_2; -.
DR InParanoid; Q97X95; -.
DR OMA; NAFAFGR; -.
DR PhylomeDB; Q97X95; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR HAMAP; MF_00188; Pept_M48_protease_HtpX; 1.
DR InterPro; IPR022919; Pept_M48_protease_HtpX.
DR InterPro; IPR001915; Peptidase_M48.
DR Pfam; PF01435; Peptidase_M48; 1.
PE 3: Inferred from homology;
KW Cell membrane; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..311
FT /note="Protease HtpX homolog 1"
FT /id="PRO_0000138930"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT ACT_SITE 138
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
SQ SEQUENCE 311 AA; 34985 MW; 7FCDCC0BFC8759F2 CRC64;
MDVRQRLISS MVISLGLTII SEGIVLIGIA SLLHISLFFI FPALVIFWLF QWIISPYVVG
RGGYEVSPND PQYGWLYNLV RRIAEESKIK PPRVFVIDAP YPNAFAYGNR LGGMRVGITL
PLLNILDVDE LTAVIAHEVG HIKHRDVEIG MTIGLIPTVL GYISTLLMNF GYLALFLAAD
EIELLFAIAA LAIGFVIFVV TFILQIFVLW FNRLRESYAD YNSFLVLGEG SKALATALAK
IEIYMQNIRI DPFTGIIVTA PPVKVEEKDP HLLVEQWLRT KVSAFKDILS THPYPARRAQ
MIYRLIYGSN I