ID   HTPX_RHOPT              Reviewed;         324 AA.
AC   B3QED3;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=Rpal_0855;
OS   Rhodopseudomonas palustris (strain TIE-1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=395960;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TIE-1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Emerson D.,
RA   Newman D.K., Roden E., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris TIE-1.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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 inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00188}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00188}.
CC   -!- SIMILARITY: Belongs to the peptidase M48B family. {ECO:0000255|HAMAP-
CC       Rule:MF_00188}.
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DR   EMBL; CP001096; ACE99412.1; -; Genomic_DNA.
DR   RefSeq; WP_011156354.1; NC_011004.1.
DR   AlphaFoldDB; B3QED3; -.
DR   EnsemblBacteria; ACE99412; ACE99412; Rpal_0855.
DR   GeneID; 66891803; -.
DR   KEGG; rpt:Rpal_0855; -.
DR   HOGENOM; CLU_042266_3_0_5; -.
DR   OMA; AVCCTEG; -.
DR   OrthoDB; 1918093at2; -.
DR   BioCyc; RPAL395960:RPAL_RS04310-MON; -.
DR   Proteomes; UP000001725; 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 inner membrane; Cell membrane; Hydrolase; Membrane; Metal-binding;
KW   Metalloprotease; Protease; Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN           1..324
FT                   /note="Protease HtpX homolog"
FT                   /id="PRO_1000098838"
FT   TRANSMEM        7..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   TRANSMEM        29..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   TRANSMEM        145..165
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          288..324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..309
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        131
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   BINDING         130
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   BINDING         134
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   BINDING         201
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
SQ   SEQUENCE   324 AA;  34187 MW;  D63F8F78FF4582E2 CRC64;
     MSYFKTALLL AGLTALFMGV GYLIGGANGA LIALVVAAAM NIFTYWNSDR MVLSMYGAQE
     VDERSAPDLY RMVAELAGRA SLPMPRVFIM DNPQPNAFAT GRNPENAAVA VTTGLMNQLS
     REELAGVVAH ELAHIKNHDT LLMTITATIA GAISMVAQFG MFFGGNRENN NGPGLIGSLA
     LMILAPLGAM LVQMAISRTR EYAADEMGAR ICGQPMWLAS ALGRIEAAAH QVPNYDAERS
     PATAHMFIIN PLSGQGMDNL FATHPSTDNR VAALQRLAAE IGGSSYRPAS TFSRGAGTAA
     SSGTPRGTGR SPWGGQPRGR GPWG