HTPX_THEPX
ID HTPX_THEPX Reviewed; 299 AA.
AC B0K4Z5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
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};
GN OrderedLocusNames=Teth514_2259;
OS Thermoanaerobacter sp. (strain X514).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacter;
OC unclassified Thermoanaerobacter.
OX NCBI_TaxID=399726;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=X514;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Saunders E., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Hemme C., Fields M.W., He Z., Zhou J., Richardson P.;
RT "Complete sequence of Thermoanaerobacter sp. X514.";
RL Submitted (JAN-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 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; CP000923; ABY93526.1; -; Genomic_DNA.
DR RefSeq; WP_012268785.1; NC_010320.1.
DR AlphaFoldDB; B0K4Z5; -.
DR SMR; B0K4Z5; -.
DR EnsemblBacteria; ABY93526; ABY93526; Teth514_2259.
DR KEGG; tex:Teth514_2259; -.
DR HOGENOM; CLU_042266_3_0_9; -.
DR OMA; AVCCTEG; -.
DR Proteomes; UP000002155; 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; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..299
FT /note="Protease HtpX homolog"
FT /id="PRO_1000098855"
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 198..218
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 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
SQ SEQUENCE 299 AA; 33733 MW; BDD28EC177CD721B CRC64;
MSRKTLYELQ AENVRKTYLF IVTFSLILFA IGYFFVWYFN WGLTGIVLLA IFIVLYNWIA
YEQSDKIALA SVGAIPANPE EYYVLHNIVE EVALAAGIPK PNVYIMEESQ PNAFATGKDP
KHASVCVTTG LLQMMNREEL QGVIAHEISH IRNRDILLMT VVAVVAGLII LLRDVMLRSM
WWGMGESRRR DKNDNGAIIL LIIGLIFSII APLIVLIIRS AISRQREYLA DATGAYIVRD
PYGLASALEK IGNYTRPMRV TSDATAHLFI SNPFGRAEKL FATHPPIEER IKRLKSLTM
