HTPX_THISH
ID HTPX_THISH Reviewed; 295 AA.
AC B8GTV4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Protease HtpX {ECO:0000255|HAMAP-Rule:MF_00188};
DE EC=3.4.24.- {ECO:0000255|HAMAP-Rule:MF_00188};
DE AltName: Full=Heat shock protein HtpX {ECO:0000255|HAMAP-Rule:MF_00188};
GN Name=htpX {ECO:0000255|HAMAP-Rule:MF_00188}; OrderedLocusNames=Tgr7_2118;
OS Thioalkalivibrio sulfidiphilus (strain HL-EbGR7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thioalkalivibrio.
OX NCBI_TaxID=396588;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-EbGR7;
RX PubMed=21475584; DOI=10.4056/sigs.1483693;
RA Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Clum A., Ivanova N.,
RA Pati A., d'Haeseleer P., Woyke T., Kyrpides N.C.;
RT "Complete genome sequence of 'Thioalkalivibrio sulfidophilus' HL-EbGr7.";
RL Stand. Genomic Sci. 4:23-35(2011).
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; CP001339; ACL73198.1; -; Genomic_DNA.
DR RefSeq; WP_012638676.1; NC_011901.1.
DR AlphaFoldDB; B8GTV4; -.
DR SMR; B8GTV4; -.
DR STRING; 396588.Tgr7_2118; -.
DR MEROPS; M48.002; -.
DR EnsemblBacteria; ACL73198; ACL73198; Tgr7_2118.
DR KEGG; tgr:Tgr7_2118; -.
DR eggNOG; COG0501; Bacteria.
DR HOGENOM; CLU_042266_1_0_6; -.
DR OMA; SRYREYV; -.
DR OrthoDB; 1918093at2; -.
DR Proteomes; UP000002383; 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; Stress response;
KW Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..295
FT /note="Protease HtpX"
FT /id="PRO_1000192753"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT ACT_SITE 148
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
SQ SEQUENCE 295 AA; 32453 MW; DB5752FF096AD6AD CRC64;
MKRIFLFLAT NLAIIVVLSI VLRLLGVERI LDESGTNLNL NALLIFAAVF GFGGSFISLA
ISKWMAKKTM RVHVIEQPRN STEQWLLETV RRQAREAGIG MPEVGIFNSP DPNAFATGMS
KNNALVAVST GLMDRMNADE VEAVLGHEVA HVANGDMVTL ALIQGVVNTF VIFLARVVGH
FVDRVVFKNE QGHGPAFWIT TIVAEIVFAI LASIIVMWFS RQREFRADAG GARLAGREKM
ISALEKLRAV HTPSQMPDQM AAFGIRGGMG QGLKKLFMSH PPLEERIMAL KAMQR