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HTPX_HALSA
ID   HTPX_HALSA              Reviewed;         289 AA.
AC   Q9HSQ2;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 119.
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}; Synonyms=hsp4;
GN   OrderedLocusNames=VNG_0129G;
OS   Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS   (Halobacterium halobium).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=64091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX   PubMed=11016950; DOI=10.1073/pnas.190337797;
RA   Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA   Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA   Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA   Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA   Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA   Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA   Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA   DasSarma S.;
RT   "Genome sequence of Halobacterium species NRC-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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; AE004437; AAG18751.1; -; Genomic_DNA.
DR   PIR; C84173; C84173.
DR   RefSeq; WP_010902046.1; NC_002607.1.
DR   AlphaFoldDB; Q9HSQ2; -.
DR   STRING; 64091.VNG_0129G; -.
DR   PaxDb; Q9HSQ2; -.
DR   EnsemblBacteria; AAG18751; AAG18751; VNG_0129G.
DR   GeneID; 39854175; -.
DR   GeneID; 5952384; -.
DR   KEGG; hal:VNG_0129G; -.
DR   PATRIC; fig|64091.14.peg.88; -.
DR   HOGENOM; CLU_042266_0_2_2; -.
DR   InParanoid; Q9HSQ2; -.
DR   OMA; SRYREYV; -.
DR   OrthoDB; 62484at2157; -.
DR   Proteomes; UP000000554; 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..289
FT                   /note="Protease HtpX homolog"
FT                   /id="PRO_0000138914"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   TRANSMEM        28..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   TRANSMEM        144..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   REGION          222..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        130
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   BINDING         129
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   BINDING         133
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   BINDING         197
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
SQ   SEQUENCE   289 AA;  31756 MW;  55A6C5B88D1A6E6E CRC64;
     MAIVGTILFA FYSVAIAAAW FFFGQNQTIL AIAIVGSVVL VGVQYKVGKW MALRSVGAED
     MDEQEFPRIH RRVESLSRDM GIKKPTLKVA NMGVPNAFAV GRKGNGTVVV SRELIDILEH
     EELDGVLAHE LSHIANRDVV TMQLGQGIAS IVGIVAQYIV LFSGDNDLAD FFLAIVVGNL
     VQFLVTLFVL AISRYREYVA DADARRAIGT GEPLARALEK ISQGNEQAAQ QQRQRTSRGR
     GRRQRGQRND DGLDQQVSAL CISSPDTSVL QKLVSTHPPT EKRIQRLRS
 
 
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