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Protein

Beta-lactamase

Gene

blaCTX-M-9a

Organism
Escherichia coli
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

A beta-lactam + H2O = a substituted beta-amino acid.UniRule annotationSAAS annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

HydrolaseUniRule annotationSAAS annotation

Keywords - Biological processi

Antibiotic resistanceUniRule annotationSAAS annotation

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-lactamaseUniRule annotationSAAS annotation (EC:3.5.2.6UniRule annotationSAAS annotation)
Gene namesi
Name:blaCTX-M-9aImported
Synonyms:blaCTX-M-9Imported, blaCTX-M-9bImported
Encoded oniPlasmid pMSP071Imported
Plasmid pOZ173Imported
OrganismiEscherichia coliImported
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence analysisAdd
BLAST
Chaini29 – 291263Beta-lactamaseSequence analysisPRO_5006751925Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei29 – 291Pyrrolidone carboxylic acidCombined sources

Keywords - PTMi

Pyrrolidone carboxylic acidCombined sources

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YLJX-ray0.98A29-291[»]
1YM1X-ray1.12A/B29-291[»]
1YMSX-ray1.60A/B29-291[»]
1YMXX-ray1.70A/B29-291[»]
2P74X-ray0.88A/B29-288[»]
3G2YX-ray1.31A/B29-291[»]
3G2ZX-ray1.50A/B29-291[»]
3G30X-ray1.80A29-291[»]
3G31X-ray1.70A/B29-291[»]
3G32X-ray1.31A/B29-291[»]
3G34X-ray1.31A/B29-291[»]
3G35X-ray1.41A/B29-291[»]
3HLWX-ray1.50A/B29-291[»]
3HREX-ray1.45A/B29-291[»]
3HUOX-ray1.50A/B29-291[»]
3HVFX-ray1.50A/B29-291[»]
3Q07X-ray1.50A/B29-291[»]
3Q1FX-ray1.50A/B29-291[»]
4DDSX-ray1.36A/B30-291[»]
4DDYX-ray1.36A/B30-291[»]
4DE0X-ray1.12A/B30-291[»]
4DE1X-ray1.26A/B30-291[»]
4DE2X-ray1.40A/B30-291[»]
4DE3X-ray1.44A/B30-291[»]
4LENX-ray1.50A/B29-291[»]
SMRiQ9L5C8. Positions 29-291.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the class-A beta-lactamase family.UniRule annotationSAAS annotation

Keywords - Domaini

SignalSequence analysis

Phylogenomic databases

KOiK18767.

Family and domain databases

Gene3Di3.40.710.10. 1 hit.
InterProiIPR012338. Beta-lactam/transpept-like.
IPR000871. Beta-lactam_class-A.
IPR023650. Beta-lactam_class-A_AS.
[Graphical view]
PRINTSiPR00118. BLACTAMASEA.
SUPFAMiSSF56601. SSF56601. 1 hit.
PROSITEiPS00146. BETA_LACTAMASE_A. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9L5C8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVTKRVQRMM FAAAACIPLL LGSAPLYAQT SAVQQKLAAL EKSSGGRLGV
60 70 80 90 100
ALIDTADNTQ VLYRGDERFP MCSTSKVMAA AAVLKQSETQ KQLLNQPVEI
110 120 130 140 150
KPADLVNYNP IAEKHVNGTM TLAELSAAAL QYSDNTAMNK LIAQLGGPGG
160 170 180 190 200
VTAFARAIGD ETFRLDRTEP TLNTAIPGDP RDTTTPRAMA QTLRQLTLGH
210 220 230 240 250
ALGETQRAQL VTWLKGNTTG AASIRAGLPT SWTAGDKTGS GDYGTTNDIA
260 270 280 290
VIWPQGRAPL VLVTYFTQPQ QNAESRRDVL ASAARIIAEG L
Length:291
Mass (Da):30,951
Last modified:October 1, 2000 - v1
Checksum:iC8CB0A7739B9469E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF174129 Genomic DNA. Translation: AAF05311.2.
AF252621 Genomic DNA. Translation: AAF72529.1.
EU418915 Genomic DNA. Translation: ACM04461.1.
HM569735 Genomic DNA. Translation: ADJ19345.1.
AJ416345 Genomic DNA. Translation: CAC95176.1.
AM040708 Genomic DNA. Translation: CAJ13580.1.

Genome annotation databases

KEGGiag:AAF05311.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF174129 Genomic DNA. Translation: AAF05311.2.
AF252621 Genomic DNA. Translation: AAF72529.1.
EU418915 Genomic DNA. Translation: ACM04461.1.
HM569735 Genomic DNA. Translation: ADJ19345.1.
AJ416345 Genomic DNA. Translation: CAC95176.1.
AM040708 Genomic DNA. Translation: CAJ13580.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YLJX-ray0.98A29-291[»]
1YM1X-ray1.12A/B29-291[»]
1YMSX-ray1.60A/B29-291[»]
1YMXX-ray1.70A/B29-291[»]
2P74X-ray0.88A/B29-288[»]
3G2YX-ray1.31A/B29-291[»]
3G2ZX-ray1.50A/B29-291[»]
3G30X-ray1.80A29-291[»]
3G31X-ray1.70A/B29-291[»]
3G32X-ray1.31A/B29-291[»]
3G34X-ray1.31A/B29-291[»]
3G35X-ray1.41A/B29-291[»]
3HLWX-ray1.50A/B29-291[»]
3HREX-ray1.45A/B29-291[»]
3HUOX-ray1.50A/B29-291[»]
3HVFX-ray1.50A/B29-291[»]
3Q07X-ray1.50A/B29-291[»]
3Q1FX-ray1.50A/B29-291[»]
4DDSX-ray1.36A/B30-291[»]
4DDYX-ray1.36A/B30-291[»]
4DE0X-ray1.12A/B30-291[»]
4DE1X-ray1.26A/B30-291[»]
4DE2X-ray1.40A/B30-291[»]
4DE3X-ray1.44A/B30-291[»]
4LENX-ray1.50A/B29-291[»]
SMRiQ9L5C8. Positions 29-291.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAF05311.

Phylogenomic databases

KOiK18767.

Family and domain databases

Gene3Di3.40.710.10. 1 hit.
InterProiIPR012338. Beta-lactam/transpept-like.
IPR000871. Beta-lactam_class-A.
IPR023650. Beta-lactam_class-A_AS.
[Graphical view]
PRINTSiPR00118. BLACTAMASEA.
SUPFAMiSSF56601. SSF56601. 1 hit.
PROSITEiPS00146. BETA_LACTAMASE_A. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and sequence of the gene encoding a novel cefotaxime-hydrolyzing beta-lactamase (CTX-M-9) from Escherichia coli in Spain."
    Sabate M., Tarrago R., Navarro F., Miro E., Verges C., Barbe J., Prats G.
    Antimicrob. Agents Chemother. 44:1970-1973(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: 785-DImported.
    Plasmid: pMSP071
  2. Hwang S.Y., Kim S.E., Biro S., Choi Y.C.
    Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: RAJImported.
  3. "Three cefotaximases, CTX-M-9, CTX-M-13, and CTX-M-14, among Enterobacteriaceae in the People's Republic of China."
    Chanawong A., M'Zali F.H., Heritage J., Xiong J.H., Hawkey P.M.
    Antimicrob. Agents Chemother. 46:630-637(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: ACH08Imported.
    Plasmid: pOZ173
  4. "Novel complex sul1-type integron in Escherichia coli carrying bla(CTX-M-9)."
    Sabate M., Navarro F., Miro E., Campoy S., Mirelis B., Barbe J., Prats G.
    Antimicrob. Agents Chemother. 46:2656-2661(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: 785-DImported.
    Plasmid: pMSP071
  5. "Diversity of CTX-M beta-lactamases and their promoter regions from Enterobacteriaceae isolated in three Parisian hospitals."
    Saladin M., Bao Cao V.T., Lambert T., Donay J.L., Herrmann J.L., Ould Hocine Z., Verdet C., Delisle F., Philippon A., Arlet G.
    FEMS Microbiol. Lett. 209:161-168(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: RAJImported.
  6. "Structure, function, and inhibition along the reaction coordinate of CTX-M beta-lactamases."
    Chen Y., Shoichet B., Bonnet R.
    J. Am. Chem. Soc. 127:5423-5434(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.12 ANGSTROMS) OF 29-291.
  7. "Atomic resolution structures of CTX-M beta-lactamases: extended spectrum activities from increased mobility and decreased stability."
    Chen Y., Delmas J., Sirot J., Shoichet B., Bonnet R.
    J. Mol. Biol. 348:349-362(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (0.98 ANGSTROMS) OF 29-291.
  8. Castro L.F.C., Santos M.M., Reis-Henriques M.A.
    Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: TN05Imported.
  9. "DNA sequence analysis of the genetic environment of various blaCTX-M genes."
    Eckert C., Gautier V., Arlet G.
    J. Antimicrob. Chemother. 57:14-23(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: TN05Imported.
  10. "The acylation mechanism of CTX-M beta-lactamase at 0.88 a resolution."
    Chen Y., Bonnet R., Shoichet B.K.
    J. Am. Chem. Soc. 129:5378-5380(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (0.88 ANGSTROMS) OF 29-288, PYRROLIDONE CARBOXYLIC ACID AT GLN-29.
  11. "Dominance of blaCTX-M within an Australian extended-spectrum beta-lactamase gene pool."
    Zong Z., Partridge S.R., Thomas L., Iredell J.R.
    Antimicrob. Agents Chemother. 52:4198-4202(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: JIE059Imported.
  12. "Molecular docking and ligand specificity in fragment-based inhibitor discovery."
    Chen Y., Shoichet B.K.
    Nat. Chem. Biol. 5:358-364(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.31 ANGSTROMS) OF 29-291.
  13. "Dynamic view of the early and late steps of the catalytic mechanism mediated by the emerging enzymes CTX-M."
    Delmas J., Leyssene D., Dubois D., Birck C., Samama J.-P., Robin F., Bonnet R.
    Submitted (JUN-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 29-291.
  14. "Structural insights into substrate recognition and product expulsion in CTX-M enzymes."
    Delmas J., Leyssene D., Dubois D., Birck C., Vazeille E., Robin F., Bonnet R.
    J. Mol. Biol. 400:108-120(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 29-291.
  15. Liu M.-X., Liu Q.-F., Li Y.-Y., Di H., He Y.
    Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: K-340Imported.
  16. "CTX-M-9 S70G mutant in complex with hydrolyzed piperacillin."
    Leyssne D., Delmas J., Coignoux A., Robin F., Bonnet R.
    Submitted (DEC-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 29-291.
  17. "CTX-M-9 S70G mutant in complex with piperacillin."
    Leyssne D., Delmas J., Coignoux A., Robin F., Bonnet R.
    Submitted (DEC-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 29-291.
  18. "Structure-based design of potent and ligand-efficient inhibitors of CTX-M class A beta-lactamase."
    Nichols D.A., Jaishankar P., Larson W., Smith E., Liu G., Beyrouthy R., Bonnet R., Renslo A.R., Chen Y.
    J. Med. Chem. 55:2163-2172(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.12 ANGSTROMS) OF 30-291.
  19. "Targeting class A and C serine beta-lactamases with a broad-spectrum boronic acid derivative."
    Tondi D., Venturelli A., Bonnet R., Pozzi C., Shoichet B.K., Costi M.P.
    J. Med. Chem. 57:5449-5458(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 29-291.

Entry informationi

Entry nameiQ9L5C8_ECOLX
AccessioniPrimary (citable) accession number: Q9L5C8
Secondary accession number(s): Q9RP34
Entry historyi
Integrated into UniProtKB/TrEMBL: October 1, 2000
Last sequence update: October 1, 2000
Last modified: May 11, 2016
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, PlasmidImported

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.