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Protein

Protein deglycase 1

Gene

hchA

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

Functioni

Protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Is able to repair glycated serum albumin, aspartate aminotransferase, glyceraldehyde-3-phosphate dehydrogenase, and fructose biphosphate aldolase. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of Schiff bases and advanced glycation endproducts (AGE) (PubMed:26102038, PubMed:26774339). Has been reported to display chaperone, peptidase and glutathione-independent glyoxalase activities (PubMed:12235139, PubMed:12565879, PubMed:14731284, PubMed:15550391, PubMed:7848303, PubMed:21696459). However, these apparently disparate activities are all recruited to execute its protein deglycase primary function (PubMed:26102038, PubMed:26774339). Plays an important role in protecting cells from carbonyl stress, severe heat shock and starvation, as well as in acid resistance of stationary-phase cells (PubMed:12235139, PubMed:16796689, PubMed:17158627).10 Publications

Catalytic activityi

(R)-lactate = methylglyoxal + H2O.2 Publications

Enzyme regulationi

The glyoxalase activity is inhibited by copper and zinc cations, activated by ferrous cations, and inactivated by thiol-blocking reagents (PubMed:21696459, PubMed:7848303). The aminopeptidase activity is inhibited by iodoacetamide, dithiothreitol, EDTA and 1, 10-phenanthroline (PubMed:15550391). Binding of ATP at high temperatures induces a conformational change that reduces HchA surface hydrophobicity, interferes with its ability to capture substrate proteins and inhibits chaperone activity (PubMed:12235139).4 Publications

Kineticsi

kcat is 156.9 min(-1) for glyoxalase activity with methylglyoxal as substrate (PubMed:21696459). kcat is 0.43 min(-1) for aminopeptidase activity with Lys-AMC as substrate. kcat is 0.51 min(-1) for aminopeptidase activity with Arg-AMC as substrate. kcat is 1.1 min(-1) for aminopeptidase activity with Ala-AMC as substrate (PubMed:15550391).2 Publications

  1. KM=55 µM for Lys-AMC (at 37 degrees Celsius and pH 8.5)1 Publication
  2. KM=95 µM for Arg-AMC (at 37 degrees Celsius and pH 8.5)1 Publication
  3. KM=120 µM for Ala-AMC (at 37 degrees Celsius and pH 8.5)1 Publication
  4. KM=1.43 mM for methylglyoxal1 Publication

    pH dependencei

    Optimum pH is between 6 and 8 for glyoxalase activity (PubMed:21696459, PubMed:7848303). Significant inhibition of glyoxalase activity below pH 5 (PubMed:21696459). Optimum pH is 8 for aminopeptidase activity (PubMed:15550391).3 Publications

    Temperature dependencei

    Optimum temperature for glyoxalase activity is around 37 degrees Celsius (PubMed:21696459). Optimum temperature for aminopeptidase activity is around 43 degrees Celsius (PubMed:15550391).2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi86 – 861Zinc1 Publication
    Metal bindingi91 – 911Zinc1 Publication
    Metal bindingi123 – 1231Zinc1 Publication
    Active sitei185 – 1851NucleophileCurated

    GO - Molecular functioni

    • glyoxalase III activity Source: EcoCyc
    • hydrolase activity Source: UniProtKB-KW
    • zinc ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    • lactate biosynthetic process Source: GOC
    • methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione Source: EcoCyc
    • protein refolding Source: UniProtKB-HAMAP
    • response to acidic pH Source: EcoCyc
    • response to methylglyoxal Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Chaperone, Hydrolase, Lyase

    Keywords - Biological processi

    Stress response

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciEcoCyc:G7055-MONOMER.
    ECOL316407:JW1950-MONOMER.
    MetaCyc:G7055-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein deglycase 11 Publication (EC:3.1.2.-2 Publications, EC:3.5.1.-2 Publications)
    Alternative name(s):
    Glyoxalase III2 Publications (EC:4.2.1.1302 Publications)
    Holding molecular chaperone1 Publication
    Hsp311 Publication
    Gene namesi
    Name:hchA
    Synonyms:yedU, yzzC
    Ordered Locus Names:b1967, JW1950
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11755. hchA.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Cells lacking this gene show a loss of glyoxalase and reduction in aminopeptidase activity (PubMed:15550391, PubMed:21696459). They accumulate methylglyoxal and are more susceptible to methylglyoxal than the parent strain (PubMed:21696459). Cells exhibit growth defects above 48 degrees Celsius and accumulate higher levels of peptides than wild-type (PubMed:14731284, PubMed:15550391). They display increased glycation levels (PubMed:26102038). Moreover, the double and triple mutants lacking yhbO and yajL, and yhbO, yajL and hchA, respectively, display impressive amounts of glycated proteins, suggesting that the YhbO, YajL and Hsp31 deglycases display relatively redundant functions (PubMed:26774339). They hchA mutant cells show decreased viability in methylglyoxal- or glucose-containing media (PubMed:26774339).5 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi77 – 771E → A: Loss of glyoxalase activity. 1 Publication
    Mutagenesisi185 – 1851C → A: Loss of glyoxalase and aminopeptidase activities. 3 Publications
    Mutagenesisi186 – 1861H → A: Shows approximately 17% remaining glyoxalase activity compared with that of the wild-type. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemoved1 Publication
    Chaini2 – 283282Protein deglycase 1PRO_0000209412Add
    BLAST

    Proteomic databases

    PaxDbiP31658.
    PRIDEiP31658.

    2D gel databases

    SWISS-2DPAGEP31658.

    Expressioni

    Inductioni

    By heat shock.

    Interactioni

    Subunit structurei

    Homodimer.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    asnCP0ACI62EBI-909144,EBI-1133670

    Protein-protein interaction databases

    BioGridi4260394. 20 interactions.
    DIPiDIP-11851N.
    IntActiP31658. 32 interactions.
    STRINGi511145.b1967.

    Structurei

    Secondary structure

    1
    283
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 114Combined sources
    Beta strandi18 – 203Combined sources
    Helixi23 – 297Combined sources
    Beta strandi50 – 545Combined sources
    Beta strandi60 – 623Combined sources
    Beta strandi68 – 703Combined sources
    Helixi75 – 8713Combined sources
    Beta strandi92 – 998Combined sources
    Helixi106 – 1083Combined sources
    Helixi116 – 12813Combined sources
    Helixi133 – 1386Combined sources
    Beta strandi145 – 1517Combined sources
    Helixi155 – 1584Combined sources
    Helixi161 – 1633Combined sources
    Helixi165 – 17612Combined sources
    Beta strandi180 – 1845Combined sources
    Helixi187 – 1948Combined sources
    Beta strandi195 – 1973Combined sources
    Turni200 – 2034Combined sources
    Helixi211 – 2155Combined sources
    Turni216 – 2216Combined sources
    Beta strandi222 – 2254Combined sources
    Beta strandi227 – 2293Combined sources
    Helixi231 – 2377Combined sources
    Beta strandi251 – 2544Combined sources
    Beta strandi257 – 2626Combined sources
    Helixi263 – 2653Combined sources
    Helixi266 – 28116Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IZYX-ray2.80A/B1-283[»]
    1IZZX-ray2.31A1-283[»]
    1N57X-ray1.60A1-283[»]
    1ONSX-ray2.20A2-283[»]
    1PV2X-ray2.71A/B/C/D/E/F/G/H1-283[»]
    ProteinModelPortaliP31658.
    SMRiP31658. Positions 5-283.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP31658.

    Family & Domainsi

    Domaini

    Consists of a large A domain and a smaller P domain connected by a linker. The thermally induced motion of the flexible linker-loop region leads to the uncovering of a high-affinity substrate-binding site that is essential to capture nonnative proteins at high temperatures.1 Publication

    Sequence similaritiesi

    Belongs to the peptidase C56 family. HchA subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4105TMR. Bacteria.
    COG0693. LUCA.
    HOGENOMiHOG000221774.
    InParanoidiP31658.
    KOiK05523.
    OMAiPMYHLDK.
    OrthoDBiEOG65J50B.

    Family and domain databases

    Gene3Di3.40.50.880. 1 hit.
    HAMAPiMF_01046. Prot_deglyc_HchA.
    InterProiIPR029062. Class_I_gatase-like.
    IPR017283. HchA.
    [Graphical view]
    PIRSFiPIRSF037798. Chaperone_HchA. 1 hit.
    SUPFAMiSSF52317. SSF52317. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P31658-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTVQTSKNPQ VDIAEDNAFF PSEYSLSQYT SPVSDLDGVD YPKPYRGKHK
    60 70 80 90 100
    ILVIAADERY LPTDNGKLFS TGNHPIETLL PLYHLHAAGF EFEVATISGL
    110 120 130 140 150
    MTKFEYWAMP HKDEKVMPFF EQHKSLFRNP KKLADVVASL NADSEYAAIF
    160 170 180 190 200
    VPGGHGALIG LPESQDVAAA LQWAIKNDRF VISLCHGPAA FLALRHGDNP
    210 220 230 240 250
    LNGYSICAFP DAADKQTPEI GYMPGHLTWY FGEELKKMGM NIINDDITGR
    260 270 280
    VHKDRKLLTG DSPFAANALG KLAAQEMLAA YAG
    Length:283
    Mass (Da):31,190
    Last modified:January 23, 2007 - v3
    Checksum:i5CA8A53843A83B72
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA. Translation: AAC75033.1.
    AP009048 Genomic DNA. Translation: BAA15794.1.
    PIRiC64961.
    RefSeqiNP_416476.1. NC_000913.3.
    WP_000218212.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75033; AAC75033; b1967.
    BAA15794; BAA15794; BAA15794.
    GeneIDi946481.
    KEGGiecj:JW1950.
    eco:b1967.
    PATRICi32119265. VBIEscCol129921_2047.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA. Translation: AAC75033.1.
    AP009048 Genomic DNA. Translation: BAA15794.1.
    PIRiC64961.
    RefSeqiNP_416476.1. NC_000913.3.
    WP_000218212.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IZYX-ray2.80A/B1-283[»]
    1IZZX-ray2.31A1-283[»]
    1N57X-ray1.60A1-283[»]
    1ONSX-ray2.20A2-283[»]
    1PV2X-ray2.71A/B/C/D/E/F/G/H1-283[»]
    ProteinModelPortaliP31658.
    SMRiP31658. Positions 5-283.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4260394. 20 interactions.
    DIPiDIP-11851N.
    IntActiP31658. 32 interactions.
    STRINGi511145.b1967.

    2D gel databases

    SWISS-2DPAGEP31658.

    Proteomic databases

    PaxDbiP31658.
    PRIDEiP31658.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75033; AAC75033; b1967.
    BAA15794; BAA15794; BAA15794.
    GeneIDi946481.
    KEGGiecj:JW1950.
    eco:b1967.
    PATRICi32119265. VBIEscCol129921_2047.

    Organism-specific databases

    EchoBASEiEB1705.
    EcoGeneiEG11755. hchA.

    Phylogenomic databases

    eggNOGiENOG4105TMR. Bacteria.
    COG0693. LUCA.
    HOGENOMiHOG000221774.
    InParanoidiP31658.
    KOiK05523.
    OMAiPMYHLDK.
    OrthoDBiEOG65J50B.

    Enzyme and pathway databases

    BioCyciEcoCyc:G7055-MONOMER.
    ECOL316407:JW1950-MONOMER.
    MetaCyc:G7055-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiP31658.
    PROiP31658.

    Family and domain databases

    Gene3Di3.40.50.880. 1 hit.
    HAMAPiMF_01046. Prot_deglyc_HchA.
    InterProiIPR029062. Class_I_gatase-like.
    IPR017283. HchA.
    [Graphical view]
    PIRSFiPIRSF037798. Chaperone_HchA. 1 hit.
    SUPFAMiSSF52317. SSF52317. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "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.
    4. "Function of the Escherichia coli nucleoid protein, H-NS: molecular analysis of a subset of proteins whose expression is enhanced in a hns deletion mutant."
      Yoshida T., Ueguchi C., Yamada H., Mizuno T.
      Mol. Gen. Genet. 237:113-122(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-21.
      Strain: K12.
    5. "Glyoxalase III from Escherichia coli: a single novel enzyme for the conversion of methylglyoxal into D-lactate without reduced glutathione."
      Misra K., Banerjee A.B., Ray S., Ray M.
      Biochem. J. 305:999-1003(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A GLYOXALASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
    6. "Hsp31, the Escherichia coli yedU gene product, is a molecular chaperone whose activity is inhibited by ATP at high temperatures."
      Sastry M.S.R., Korotkov K., Brodsky Y., Baneyx F.
      J. Biol. Chem. 277:46026-46034(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A CHAPERONE, SUBUNIT, ENZYME REGULATION.
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
    7. "Characterization of the Escherichia coli YedU protein as a molecular chaperone."
      Malki A., Kern R., Abdallah J., Richarme G.
      Biochem. Biophys. Res. Commun. 301:430-436(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A CHAPERONE, SUBUNIT.
    8. "Escherichia coli Hsp31 functions as a holding chaperone that cooperates with the DnaK-DnaJ-GrpE system in the management of protein misfolding under severe stress conditions."
      Mujacic M., Bader M.W., Baneyx F.
      Mol. Microbiol. 51:849-859(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A CHAPERONE, DISRUPTION PHENOTYPE.
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
    9. "The linker-loop region of Escherichia coli chaperone Hsp31 functions as a gate that modulates high-affinity substrate binding at elevated temperatures."
      Sastry M.S.R., Quigley P.M., Hol W.G.J., Baneyx F.
      Proc. Natl. Acad. Sci. U.S.A. 101:8587-8592(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN.
    10. Cited for: FUNCTION AS AN AMINOPEPTIDASE, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF CYS-185.
    11. "Regulation of Escherichia coli hchA, a stress-inducible gene encoding molecular chaperone Hsp31."
      Mujacic M., Baneyx F.
      Mol. Microbiol. 60:1576-1589(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN STRESS RESISTANCE.
    12. "Chaperone Hsp31 contributes to acid resistance in stationary-phase Escherichia coli."
      Mujacic M., Baneyx F.
      Appl. Environ. Microbiol. 73:1014-1018(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ACID STRESS RESISTANCE.
    13. "Hsp31 of Escherichia coli K-12 is glyoxalase III."
      Subedi K.P., Choi D., Kim I., Min B., Park C.
      Mol. Microbiol. 81:926-936(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A GLYOXALASE, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-77; CYS-185 AND HIS-186, DISRUPTION PHENOTYPE, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: K12 / MG1655 / ATCC 47076.
    14. "Crystallization and preliminary X-ray crystallographic analysis of a yedU gene product from Escherichia coli."
      Kim O.-G., Kim I.-K., Kim G.-H., Ko J., Park C., Suh P.-G., Kang S.-O., Lee H.-S., Cha S.-S.
      Acta Crystallogr. D 58:1217-1219(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: CRYSTALLIZATION.
    15. "The DJ-1 superfamily member Hsp31 repairs proteins from glycation by methylglyoxal and glyoxal."
      Mihoub M., Abdallah J., Gontero B., Dairou J., Richarme G.
      Biochem. Biophys. Res. Commun. 463:1305-1310(2015) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A PROTEIN DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
    16. "The DJ-1 superfamily members YhbO and YajL from Escherichia coli repair proteins from glycation by methylglyoxal and glyoxal."
      Abdallah J., Mihoub M., Gautier V., Richarme G.
      Biochem. Biophys. Res. Commun. 470:282-286(2016) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A PROTEIN DEGLYCASE, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE.
      Strain: K12 / MG1655 / ATCC 47076.
    17. "Crystal structures of human DJ-1 and Escherichia coli Hsp31, which share an evolutionarily conserved domain."
      Lee S.-J., Kim S.J., Kim I.-K., Ko J., Jeong C.-S., Kim G.-H., Park C., Kang S.-O., Suh P.-G., Lee H.-S., Cha S.-S.
      J. Biol. Chem. 278:44552-44559(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS), PROTEOLYTIC ACTIVITY, MUTAGENESIS OF CYS-185.
    18. "The 1.6-A crystal structure of the class of chaperones represented by Escherichia coli Hsp31 reveals a putative catalytic triad."
      Quigley P.M., Korotkov K., Baneyx F., Hol W.G.J.
      Proc. Natl. Acad. Sci. U.S.A. 100:3137-3142(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 6-291.
    19. "The crystal structure of Escherichia coli heat shock protein YedU reveals three potential catalytic active sites."
      Zhao Y., Liu D., Kaluarachchi W.D., Bellamy H.D., White M.A., Fox R.O.
      Protein Sci. 12:2303-2311(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-283 IN COMPLEX WITH ZINC, METAL-BINDING.
      Strain: K12 / MG1655 / ATCC 47076.
    20. "A new native EcHsp31 structure suggests a key role of structural flexibility for chaperone function."
      Quigley P.M., Korotkov K., Baneyx F., Hol W.G.J.
      Protein Sci. 13:269-277(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS).

    Entry informationi

    Entry nameiHCHA_ECOLI
    AccessioniPrimary (citable) accession number: P31658
    Secondary accession number(s): P76338
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: January 23, 2007
    Last modified: May 11, 2016
    This is version 136 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    According to some authors, HchA exhibits an exceedingly weak proteolytic activity against bovine serum albumin (BSA) and some peptidase activity against small single amino acids conjugated to a fluorogenic reporter (PubMed:12939276). Another report showed that HchA does not display any significant proteolytic activity but displays a physiologically relevant aminopeptidase activity (PubMed:15550391).2 Publications

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Peptidase families
      Classification of peptidase families and list of entries
    4. 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.