HTPX_ECO57
ID HTPX_ECO57 Reviewed; 293 AA.
AC P65813; Q8XCN0;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Protease HtpX;
DE EC=3.4.24.-;
DE AltName: Full=Heat shock protein HtpX;
GN Name=htpX; OrderedLocusNames=Z2876, ECs2539;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
RN [3]
RP INDUCTION BY ACIDITY.
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=19346340; DOI=10.1128/aem.02841-08;
RA Bergholz T.M., Vanaja S.K., Whittam T.S.;
RT "Gene expression induced in Escherichia coli O157:H7 upon exposure to model
RT apple juice.";
RL Appl. Environ. Microbiol. 75:3542-3553(2009).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- INDUCTION: More highly expressed in exponential than stationary phase,
CC it is induced 2-fold in response to model apple juice (pH 3.5).
CC {ECO:0000269|PubMed:19346340}.
CC -!- SIMILARITY: Belongs to the peptidase M48B family. {ECO:0000305}.
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DR EMBL; AE005174; AAG56819.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB35962.1; -; Genomic_DNA.
DR PIR; C90946; C90946.
DR PIR; G85794; G85794.
DR RefSeq; NP_310566.1; NC_002695.1.
DR RefSeq; WP_000984517.1; NZ_SWKA01000004.1.
DR AlphaFoldDB; P65813; -.
DR SMR; P65813; -.
DR STRING; 155864.EDL933_2802; -.
DR MEROPS; M48.002; -.
DR EnsemblBacteria; AAG56819; AAG56819; Z2876.
DR EnsemblBacteria; BAB35962; BAB35962; ECs_2539.
DR GeneID; 66674281; -.
DR GeneID; 912682; -.
DR KEGG; ece:Z2876; -.
DR KEGG; ecs:ECs_2539; -.
DR PATRIC; fig|386585.9.peg.2662; -.
DR eggNOG; COG0501; Bacteria.
DR HOGENOM; CLU_042266_1_0_6; -.
DR OMA; AVCCTEG; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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 2: Evidence at transcript level;
KW Cell inner membrane; Cell membrane; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..293
FT /note="Protease HtpX"
FT /id="PRO_0000138862"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..33
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..157
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..192
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..293
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 140
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 293 AA; 31957 MW; 132B39F6392DD5BF CRC64;
MMRIALFLLT NLAVMVVFGL VLSLTGIQSS SVQGLMIMAL LFGFGGSFVS LLMSKWMALR
SVGGEVIEQP RNERERWLVN TVATQARQAG IAMPQVAIYH APDINAFATG ARRDASLVAV
STGLLQNMSP DEAEAVIAHE ISHIANGDMV TMTLIQGVVN TFVIFISRIL AQLAAGFMGG
NRDEGEESNG NPLIYFAVAT VLELVFGILA SIITMWFSRH REFHADAGSA KLVGREKMIA
ALQRLKTSYE PQEATSMMAF CINGKSKSLS ELFMTHPPLD KRIEALRTGE YLK
