HTPX_DICTD
ID HTPX_DICTD Reviewed; 304 AA.
AC B8E160;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 62.
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=Dtur_0907;
OS Dictyoglomus turgidum (strain DSM 6724 / Z-1310).
OC Bacteria; Dictyoglomi; Dictyoglomales; Dictyoglomaceae; Dictyoglomus.
OX NCBI_TaxID=515635;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6724 / Z-1310;
RX PubMed=28066333; DOI=10.3389/fmicb.2016.01979;
RA Brumm P.J., Gowda K., Robb F.T., Mead D.A.;
RT "The complete genome sequence of hyperthermophile Dictyoglomus turgidum DSM
RT 6724 reveals a specialized carbohydrate fermentor.";
RL Front. Microbiol. 7:1979-1979(2016).
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; CP001251; ACK42188.1; -; Genomic_DNA.
DR RefSeq; WP_012583272.1; NC_011661.1.
DR RefSeq; YP_002352802.1; NC_011661.1.
DR AlphaFoldDB; B8E160; -.
DR SMR; B8E160; -.
DR STRING; 515635.Dtur_0907; -.
DR EnsemblBacteria; ACK42188; ACK42188; Dtur_0907.
DR KEGG; dtu:Dtur_0907; -.
DR eggNOG; COG0501; Bacteria.
DR HOGENOM; CLU_042266_3_0_0; -.
DR InParanoid; B8E160; -.
DR OMA; AVCCTEG; -.
DR OrthoDB; 1918093at2; -.
DR Proteomes; UP000007719; 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; Reference proteome; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..304
FT /note="Protease HtpX homolog"
FT /id="PRO_1000203972"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT ACT_SITE 147
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
SQ SEQUENCE 304 AA; 34628 MW; 979487CE088DC71D CRC64;
MKPFTFYEAI ESNKRKTWFI VFIIYFLLFF VCYAVVSYFE LGEIGIIIAF LIVLFTNYYA
YQKSNEIILN YSGVREPTRE EYPYLLNVVE GLSIAAGIPT PKIYIMDDPS PNAFATGKDP
QNSVVVVTKG LLDILNRTEL EGVIAHEISH IKNYDVRLQT IAAVMVGLIV ILGDGLKRSF
YYSKRRRDKD ENILGIVSLI IAILAPFLAT LLRFALSRQR EYMADASAAM LTRYPEGLAS
ALEKIAKNFQ PIKRANVMTA PLYIVNPLSS NAVSKLFSTH PPIEERIRRL RMMGERWKML
DKEG
