HTPX_ECOLI
ID HTPX_ECOLI Reviewed; 293 AA.
AC P23894;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Protease HtpX;
DE EC=3.4.24.-;
DE AltName: Full=Heat shock protein HtpX;
GN Name=htpX; OrderedLocusNames=b1829, JW1818;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION BY HEAT SHOCK, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=K12 / W3350 / ATCC 27020;
RX PubMed=1826904; DOI=10.1128/jb.173.9.2944-2953.1991;
RA Kornitzer D., Teff D., Altuvia S., Oppenheim A.B.;
RT "Isolation, characterization, and sequence of an Escherichia coli heat
RT shock gene, htpX.";
RL J. Bacteriol. 173:2944-2953(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP POSSIBLE FUNCTION AS A PROTEASE.
RX PubMed=8524875; DOI=10.1073/pnas.92.25.11921;
RA Koonin E.V., Tatusov R.L., Rudd K.E.;
RT "Sequence similarity analysis of Escherichia coli proteins: functional and
RT evolutionary implications.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:11921-11925(1995).
RN [6]
RP SUBCELLULAR LOCATION, TOPOLOGY, INDUCTION BY CPXR, AND MUTAGENESIS OF
RP ASN-105; PHE-107; HIS-139; GLU-140; GLU-222; ASP-226 AND HIS-276.
RX PubMed=12081643; DOI=10.1046/j.1365-2443.2002.00554.x;
RA Shimohata N., Chiba S., Saikawa N., Ito K., Akiyama Y.;
RT "The Cpx stress response system of Escherichia coli senses plasma membrane
RT proteins and controls HtpX, a membrane protease with a cytosolic active
RT site.";
RL Genes Cells 7:653-662(2002).
RN [7]
RP FUNCTION, CHARACTERIZATION AS A PROTEASE, COFACTOR, AND AUTOCATALYSIS.
RC STRAIN=K12 / CSH26 / AD16;
RX PubMed=16076848; DOI=10.1074/jbc.m506180200;
RA Sakoh M., Ito K., Akiyama Y.;
RT "Proteolytic activity of HtpX, a membrane-bound and stress-controlled
RT protease from Escherichia coli.";
RL J. Biol. Chem. 280:33305-33310(2005).
RN [8]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [9]
RP REVIEW.
RX PubMed=19454621; DOI=10.1093/jb/mvp071;
RA Akiyama Y.;
RT "Quality control of cytoplasmic membrane proteins in Escherichia coli.";
RL J. Biochem. 146:449-454(2009).
CC -!- FUNCTION: Membrane-localized protease able to endoproteolytically
CC degrade overproduced SecY but not YccA, another membrane protein. It
CC seems to cleave SecY at specific cytoplasmic sites. Does not require
CC ATP. Its natural substrate has not been identified. Probably plays a
CC role in the quality control of integral membrane proteins.
CC {ECO:0000269|PubMed:16076848}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000305|PubMed:16076848};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000305|PubMed:16076848};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:12081643}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:12081643}. Note=Bioinformatics programs predict 4
CC transmembrane helices, however PhoA and Bla fusions as well as other
CC experiments only confirm the first 2. {ECO:0000269|PubMed:12081643}.
CC -!- INDUCTION: By temperature upshift (by the sigma-32 heat shock
CC transcription factor). Also under control of CpxR.
CC {ECO:0000269|PubMed:12081643, ECO:0000269|PubMed:1826904}.
CC -!- PTM: Undergoes self-cleavage. This may not be physiological.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, however one of HtpX or FtsH
CC is essential for cell viability. {ECO:0000269|PubMed:1826904}.
CC -!- SIMILARITY: Belongs to the peptidase M48B family. {ECO:0000305}.
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DR EMBL; M58470; AAA62779.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74899.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15637.1; -; Genomic_DNA.
DR PIR; A43659; A43659.
DR RefSeq; NP_416343.1; NC_000913.3.
DR RefSeq; WP_000984520.1; NZ_SSZK01000001.1.
DR AlphaFoldDB; P23894; -.
DR SMR; P23894; -.
DR BioGRID; 4260355; 36.
DR STRING; 511145.b1829; -.
DR MEROPS; M48.002; -.
DR TCDB; 9.B.1.1.6; the integral membrane caax protease (caax protease) family.
DR jPOST; P23894; -.
DR PaxDb; P23894; -.
DR PRIDE; P23894; -.
DR EnsemblBacteria; AAC74899; AAC74899; b1829.
DR EnsemblBacteria; BAA15637; BAA15637; BAA15637.
DR GeneID; 946076; -.
DR KEGG; ecj:JW1818; -.
DR KEGG; eco:b1829; -.
DR PATRIC; fig|1411691.4.peg.421; -.
DR EchoBASE; EB0457; -.
DR eggNOG; COG0501; Bacteria.
DR HOGENOM; CLU_042266_1_0_6; -.
DR InParanoid; P23894; -.
DR OMA; AVCCTEG; -.
DR PhylomeDB; P23894; -.
DR BioCyc; EcoCyc:EG10462-MON; -.
DR PRO; PR:P23894; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:EcoCyc.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR GO; GO:0006508; P:proteolysis; IDA:EcoCyc.
DR GO; GO:0009266; P:response to temperature stimulus; IEP:EcoCyc.
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 1: Evidence at protein level;
KW Autocatalytic cleavage; Cell inner membrane; Cell membrane; Hydrolase;
KW Membrane; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Stress response; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..293
FT /note="Protease HtpX"
FT /id="PRO_0000138860"
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 TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..293
FT /note="Cytoplasmic"
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"
FT MUTAGEN 105
FT /note="N->D: Does not complement a double ftsH/htpX
FT disruption mutant."
FT /evidence="ECO:0000269|PubMed:12081643"
FT MUTAGEN 107
FT /note="F->A: Does not complement a double ftsH/htpX
FT disruption mutant."
FT /evidence="ECO:0000269|PubMed:12081643"
FT MUTAGEN 139
FT /note="H->F: Does not complement a double ftsH/htpX
FT disruption mutant. No self-degradation."
FT /evidence="ECO:0000269|PubMed:12081643"
FT MUTAGEN 140
FT /note="E->Q: Does not complement a double ftsH/htpX
FT disruption mutant."
FT /evidence="ECO:0000269|PubMed:12081643"
FT MUTAGEN 222
FT /note="E->Q: Does not complement a double ftsH/htpX
FT disruption mutant."
FT /evidence="ECO:0000269|PubMed:12081643"
FT MUTAGEN 226
FT /note="D->N: Does not complement a double ftsH/htpX
FT disruption mutant."
FT /evidence="ECO:0000269|PubMed:12081643"
FT MUTAGEN 276
FT /note="H->F: Does not complement a double ftsH/htpX
FT disruption mutant."
FT /evidence="ECO:0000269|PubMed:12081643"
SQ SEQUENCE 293 AA; 31923 MW; 13253716D92DD5BF 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 PQEATSMMAL CINGKSKSLS ELFMTHPPLD KRIEALRTGE YLK
