ID   HTPX_PYRAE              Reviewed;         347 AA.
AC   Q8ZT30;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Protease HtpX homolog {ECO:0000255|HAMAP-Rule:MF_00188};
DE            EC=3.4.24.- {ECO:0000255|HAMAP-Rule:MF_00188};
GN   Name=htpX {ECO:0000255|HAMAP-Rule:MF_00188}; OrderedLocusNames=PAE3461;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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; AE009441; AAL64933.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8ZT30; -.
DR   STRING; 178306.PAE3461; -.
DR   EnsemblBacteria; AAL64933; AAL64933; PAE3461.
DR   KEGG; pai:PAE3461; -.
DR   PATRIC; fig|178306.9.peg.2605; -.
DR   eggNOG; arCOG01331; Archaea.
DR   HOGENOM; CLU_042266_4_2_2; -.
DR   InParanoid; Q8ZT30; -.
DR   OMA; SRYREYV; -.
DR   Proteomes; UP000002439; 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.
DR   PROSITE; PS00142; ZINC_PROTEASE; 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..347
FT                   /note="Protease HtpX homolog"
FT                   /id="PRO_0000138924"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   TRANSMEM        44..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   TRANSMEM        76..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   TRANSMEM        141..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   TRANSMEM        185..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   TRANSMEM        221..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   ACT_SITE        175
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   BINDING         174
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   BINDING         178
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   BINDING         248
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
SQ   SEQUENCE   347 AA;  38038 MW;  E9F2CF37BCBD60E6 CRC64;
     MFPIFDPVAL GLYIVGYIFM LIIAATIAPK VAKSISGRFT LYGAMALTAV LVVLTTAFII
     YLFVTVALPH MGAYGLSFLL GLIFFVVLMN IITYFASPYL INLSYGARPD PRLQQIVDEV
     AARLGAPFKL KAVVVDGPPN AFAYGNFLTG RYVAVTSSML ALTDRRELEA VIGHEIGHHL
     HRDNAIMLLF GILPSIVYYL GVTAVHMAMA SSGNRGGNPA ILAAVGIAAV IVSFLIQLLV
     LAFSRLREYY ADTAGAKAAG KEAMQFALAK IHKFYFANPE AHEVVRDSKF RALFIYALVN
     AVANPFVSVT RSDLEEIKRS SYSVFQEIFS THPPIPKRLK FLDELQF