HTPX_HELAH
ID HTPX_HELAH Reviewed; 309 AA.
AC Q17WX4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=Hac_1088;
OS Helicobacter acinonychis (strain Sheeba).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=382638;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sheeba;
RX PubMed=16789826; DOI=10.1371/journal.pgen.0020120;
RA Eppinger M., Baar C., Linz B., Raddatz G., Lanz C., Keller H., Morelli G.,
RA Gressmann H., Achtman M., Schuster S.C.;
RT "Who ate whom? Adaptive Helicobacter genomic changes that accompanied a
RT host jump from early humans to large felines.";
RL PLoS Genet. 2:1097-1110(2006).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM260522; CAJ99852.1; -; Genomic_DNA.
DR AlphaFoldDB; Q17WX4; -.
DR STRING; 382638.Hac_1088; -.
DR EnsemblBacteria; CAJ99852; CAJ99852; Hac_1088.
DR KEGG; hac:Hac_1088; -.
DR eggNOG; COG0501; Bacteria.
DR HOGENOM; CLU_042266_2_1_7; -.
DR OMA; REYMADS; -.
DR Proteomes; UP000000775; 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..309
FT /note="Protease HtpX homolog"
FT /id="PRO_1000071689"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT ACT_SITE 166
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
SQ SEQUENCE 309 AA; 35060 MW; A20AA20B7EC8062F CRC64;
MNFEKIIAQN KLKTNAVLTT YCVIFAFIGL LVDVIRINAN DLGIALFKLI TFQIFPTITV
IMFLVAFVVI VVCIQNFSSI MLSGDEYKLI DPSKVLSSKE NQIHGLLLEL LEEAKLNFEP
KLYIINAPYM NAFASGWNET NSLIALTSAL IERLDRDELK AVIAHELSHI RHNDIRLTMC
VGILSNIMLL VANFSVYFFM GNRKNSGANL AKMILLVLQI VLPFLTLILQ MYLSRTREYM
ADSGAAFLMH DSKPMIRALQ KISNDYKEND YKEIDTNSTR SAAYLFNAEM FSTHPSIKNR
IQSLSRRAL
