HTPX_YERPG
ID HTPX_YERPG Reviewed; 293 AA.
AC A9R0E2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
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};
GN OrderedLocusNames=YpAngola_A2662;
OS Yersinia pestis bv. Antiqua (strain Angola).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=349746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Angola;
RX PubMed=20061468; DOI=10.1128/jb.01518-09;
RA Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S.,
RA Achtman M., Lindler L.E., Ravel J.;
RT "Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals
RT new insights into the evolution and pangenome of the plague bacterium.";
RL J. Bacteriol. 192:1685-1699(2010).
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; CP000901; ABX86441.1; -; Genomic_DNA.
DR RefSeq; WP_002210847.1; NZ_CP009935.1.
DR AlphaFoldDB; A9R0E2; -.
DR SMR; A9R0E2; -.
DR MEROPS; M48.002; -.
DR GeneID; 66841193; -.
DR KEGG; ypg:YpAngola_A2662; -.
DR PATRIC; fig|349746.12.peg.3690; -.
DR OMA; AVCCTEG; -.
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..293
FT /note="Protease HtpX"
FT /id="PRO_1000098864"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT ACT_SITE 140
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
SQ SEQUENCE 293 AA; 32064 MW; 24B1038E0153D7DF CRC64;
MMRIALFLLT NLAVMLVFGL VLSLTGIQSS SVQGLMIMAG LFGFGGAFVS LLMSKWMALR
SVGGEVIERP RNETEYWLLE TVRRQSQQVG IAMPQVAIYQ APDINAFATG ARRDASLVAV
STGLLQNMSR DEAEAVIAHE ISHVANGDMV TMTLIQGVVN TFVIFISRLI AQIAAGFLSG
DRDGESNSPG NPMVYFAVSM VLELVFGILA SIITMWFSRH REFHADAGSA KLVGREKMIA
ALQRLKTSYE PQEAGSMMAF CINGKSKTFS ELFMSHPPLD KRIEALRSGQ YLK
