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Protein

Protease HtpX

Gene

htpX

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Membrane-localized protease able to endoproteolytically degrade overproduced SecY but not YccA, another membrane protein. It seems to cleave SecY at specific cytoplasmic sites. Does not require ATP. Its natural substrate has not been identified. Probably plays a role in the quality control of integral membrane proteins.1 Publication

Cofactori

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi139 – 1391Zinc; catalyticBy similarity
Active sitei140 – 1401By similarity
Metal bindingi143 – 1431Zinc; catalyticBy similarity
Metal bindingi222 – 2221Zinc; catalyticBy similarity

GO - Molecular functioni

  • metalloendopeptidase activity Source: EcoCyc
  • zinc ion binding Source: EcoCyc

GO - Biological processi

  • proteolysis Source: EcoCyc
  • response to temperature stimulus Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Stress response

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:EG10462-MONOMER.
ECOL316407:JW1818-MONOMER.

Protein family/group databases

MEROPSiM48.002.
TCDBi9.B.1.1.6. the integral membrane caax protease (caax protease) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Protease HtpX (EC:3.4.24.-)
Alternative name(s):
Heat shock protein HtpX
Gene namesi
Name:htpX
Ordered Locus Names:b1829, JW1818
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10462. htpX.

Subcellular locationi

  • Cell inner membrane 1 Publication; Multi-pass membrane protein 1 Publication

  • Note: Bioinformatics programs predict 4 transmembrane helices, however PhoA and Bla fusions as well as other experiments only confirm the first 2.1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 33CytoplasmicSequence analysis
Transmembranei4 – 2421HelicalSequence analysisAdd
BLAST
Topological domaini25 – 339Periplasmic
Transmembranei34 – 5421HelicalSequence analysisAdd
BLAST
Topological domaini55 – 293239CytoplasmicAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: EcoCyc
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

No visible phenotype, however one of HtpX or FtsH is essential for cell viability.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi105 – 1051N → D: Does not complement a double ftsH/htpX disruption mutant. 1 Publication
Mutagenesisi107 – 1071F → A: Does not complement a double ftsH/htpX disruption mutant. 1 Publication
Mutagenesisi139 – 1391H → F: Does not complement a double ftsH/htpX disruption mutant. No self-degradation. 1 Publication
Mutagenesisi140 – 1401E → Q: Does not complement a double ftsH/htpX disruption mutant. 1 Publication
Mutagenesisi222 – 2221E → Q: Does not complement a double ftsH/htpX disruption mutant. 1 Publication
Mutagenesisi226 – 2261D → N: Does not complement a double ftsH/htpX disruption mutant. 1 Publication
Mutagenesisi276 – 2761H → F: Does not complement a double ftsH/htpX disruption mutant. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 293293Protease HtpXPRO_0000138860Add
BLAST

Post-translational modificationi

Undergoes self-cleavage. This may not be physiological.

Keywords - PTMi

Autocatalytic cleavage

Proteomic databases

PaxDbiP23894.
PRIDEiP23894.

Expressioni

Inductioni

By temperature upshift (by the sigma-32 heat shock transcription factor). Also under control of CpxR.2 Publications

Interactioni

Protein-protein interaction databases

BioGridi4260355. 7 interactions.
STRINGi511145.b1829.

Structurei

3D structure databases

ProteinModelPortaliP23894.
SMRiP23894. Positions 57-157.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M48B family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105D0M. Bacteria.
COG0501. LUCA.
HOGENOMiHOG000227302.
InParanoidiP23894.
KOiK03799.
OMAiAWIASRF.
OrthoDBiEOG6F55J5.
PhylomeDBiP23894.

Family and domain databases

HAMAPiMF_00188. Pept_M48_protease_HtpX.
InterProiIPR022919. Pept_M48_protease_HtpX.
IPR001915. Peptidase_M48.
[Graphical view]
PfamiPF01435. Peptidase_M48. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P23894-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMRIALFLLT NLAVMVVFGL VLSLTGIQSS SVQGLMIMAL LFGFGGSFVS
60 70 80 90 100
LLMSKWMALR SVGGEVIEQP RNERERWLVN TVATQARQAG IAMPQVAIYH
110 120 130 140 150
APDINAFATG ARRDASLVAV STGLLQNMSP DEAEAVIAHE ISHIANGDMV
160 170 180 190 200
TMTLIQGVVN TFVIFISRIL AQLAAGFMGG NRDEGEESNG NPLIYFAVAT
210 220 230 240 250
VLELVFGILA SIITMWFSRH REFHADAGSA KLVGREKMIA ALQRLKTSYE
260 270 280 290
PQEATSMMAL CINGKSKSLS ELFMTHPPLD KRIEALRTGE YLK
Length:293
Mass (Da):31,923
Last modified:November 1, 1991 - v1
Checksum:i13253716D92DD5BF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58470 Genomic DNA. Translation: AAA62779.1.
U00096 Genomic DNA. Translation: AAC74899.1.
AP009048 Genomic DNA. Translation: BAA15637.1.
PIRiA43659.
RefSeqiNP_416343.1. NC_000913.3.
WP_000984520.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74899; AAC74899; b1829.
BAA15637; BAA15637; BAA15637.
GeneIDi946076.
KEGGiecj:JW1818.
eco:b1829.
PATRICi32118979. VBIEscCol129921_1907.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58470 Genomic DNA. Translation: AAA62779.1.
U00096 Genomic DNA. Translation: AAC74899.1.
AP009048 Genomic DNA. Translation: BAA15637.1.
PIRiA43659.
RefSeqiNP_416343.1. NC_000913.3.
WP_000984520.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP23894.
SMRiP23894. Positions 57-157.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260355. 7 interactions.
STRINGi511145.b1829.

Protein family/group databases

MEROPSiM48.002.
TCDBi9.B.1.1.6. the integral membrane caax protease (caax protease) family.

Proteomic databases

PaxDbiP23894.
PRIDEiP23894.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74899; AAC74899; b1829.
BAA15637; BAA15637; BAA15637.
GeneIDi946076.
KEGGiecj:JW1818.
eco:b1829.
PATRICi32118979. VBIEscCol129921_1907.

Organism-specific databases

EchoBASEiEB0457.
EcoGeneiEG10462. htpX.

Phylogenomic databases

eggNOGiENOG4105D0M. Bacteria.
COG0501. LUCA.
HOGENOMiHOG000227302.
InParanoidiP23894.
KOiK03799.
OMAiAWIASRF.
OrthoDBiEOG6F55J5.
PhylomeDBiP23894.

Enzyme and pathway databases

BioCyciEcoCyc:EG10462-MONOMER.
ECOL316407:JW1818-MONOMER.

Miscellaneous databases

PROiP23894.

Family and domain databases

HAMAPiMF_00188. Pept_M48_protease_HtpX.
InterProiIPR022919. Pept_M48_protease_HtpX.
IPR001915. Peptidase_M48.
[Graphical view]
PfamiPF01435. Peptidase_M48. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation, characterization, and sequence of an Escherichia coli heat shock gene, htpX."
    Kornitzer D., Teff D., Altuvia S., Oppenheim A.B.
    J. Bacteriol. 173:2944-2953(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION BY HEAT SHOCK, DISRUPTION PHENOTYPE.
    Strain: K12 / W3350 / ATCC 27020.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Sequence similarity analysis of Escherichia coli proteins: functional and evolutionary implications."
    Koonin E.V., Tatusov R.L., Rudd K.E.
    Proc. Natl. Acad. Sci. U.S.A. 92:11921-11925(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE FUNCTION AS A PROTEASE.
  6. "The Cpx stress response system of Escherichia coli senses plasma membrane proteins and controls HtpX, a membrane protease with a cytosolic active site."
    Shimohata N., Chiba S., Saikawa N., Ito K., Akiyama Y.
    Genes Cells 7:653-662(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TOPOLOGY, INDUCTION BY CPXR, MUTAGENESIS OF ASN-105; PHE-107; HIS-139; GLU-140; GLU-222; ASP-226 AND HIS-276.
  7. "Proteolytic activity of HtpX, a membrane-bound and stress-controlled protease from Escherichia coli."
    Sakoh M., Ito K., Akiyama Y.
    J. Biol. Chem. 280:33305-33310(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CHARACTERIZATION AS A PROTEASE, COFACTOR, AUTOCATALYSIS.
    Strain: K12 / CSH26 / AD16.
  8. "Global topology analysis of the Escherichia coli inner membrane proteome."
    Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
    Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: K12 / MG1655 / ATCC 47076.
  9. "Quality control of cytoplasmic membrane proteins in Escherichia coli."
    Akiyama Y.
    J. Biochem. 146:449-454(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiHTPX_ECOLI
AccessioniPrimary (citable) accession number: P23894
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: January 20, 2016
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.