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P00811

- AMPC_ECOLI

UniProt

P00811 - AMPC_ECOLI

Protein

Beta-lactamase

Gene

ampC

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.

    Catalytic activityi

    A beta-lactam + H2O = a substituted beta-amino acid.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei80 – 801Acyl-ester intermediate1 PublicationPROSITE-ProRule annotation
    Active sitei166 – 1661Proton acceptor

    GO - Molecular functioni

    1. beta-lactamase activity Source: EcoliWiki

    GO - Biological processi

    1. antibiotic catabolic process Source: InterPro
    2. response to antibiotic Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Antibiotic resistance

    Enzyme and pathway databases

    BioCyciEcoCyc:EG10040-MONOMER.
    ECOL316407:JW4111-MONOMER.
    MetaCyc:EG10040-MONOMER.
    SABIO-RKP00811.

    Protein family/group databases

    MEROPSiS12.006.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Beta-lactamase (EC:3.5.2.6)
    Alternative name(s):
    Cephalosporinase
    Gene namesi
    Name:ampC
    Synonyms:ampA
    Ordered Locus Names:b4150, JW4111
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10040. ampC.

    Subcellular locationi

    GO - Cellular componenti

    1. outer membrane-bounded periplasmic space Source: InterPro

    Keywords - Cellular componenti

    Periplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi80 – 801S → D, E or G: Loss of activity. 1 Publication
    Mutagenesisi83 – 831K → Q or T: Lowers activity more than 1000-fold and increases protein stability. 1 Publication
    Mutagenesisi166 – 1661Y → E: Lowers activity more than 1000-fold. 1 Publication
    Mutagenesisi168 – 1681N → D or H: Lowers activity more than 1000-fold. 1 Publication
    Mutagenesisi331 – 3311K → A: Lowers activity more than 1000-fold. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 19191 PublicationAdd
    BLAST
    Chaini20 – 377358Beta-lactamasePRO_0000016958Add
    BLAST

    2D gel databases

    SWISS-2DPAGEP00811.

    PTM databases

    PhosSiteiP0809371.

    Expressioni

    Gene expression databases

    GenevestigatoriP00811.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    IntActiP00811. 1 interaction.
    STRINGi511145.b4150.

    Structurei

    Secondary structure

    1
    377
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi22 – 3918
    Beta strandi42 – 509
    Beta strandi53 – 6311
    Turni64 – 674
    Beta strandi75 – 773
    Helixi79 – 813
    Helixi82 – 9514
    Helixi105 – 1084
    Helixi115 – 1173
    Helixi122 – 1265
    Helixi144 – 15310
    Beta strandi162 – 1643
    Helixi168 – 17811
    Turni179 – 1835
    Helixi186 – 1938
    Turni194 – 1996
    Beta strandi204 – 2063
    Helixi209 – 2146
    Beta strandi218 – 2203
    Beta strandi223 – 2253
    Turni229 – 2313
    Helixi233 – 2364
    Beta strandi240 – 2423
    Helixi243 – 25412
    Helixi256 – 2583
    Helixi262 – 27110
    Beta strandi273 – 2786
    Beta strandi281 – 2833
    Beta strandi288 – 2936
    Helixi296 – 3016
    Beta strandi303 – 3053
    Beta strandi306 – 3083
    Beta strandi310 – 3134
    Beta strandi315 – 3217
    Beta strandi325 – 33511
    Beta strandi338 – 3458
    Helixi346 – 3483
    Beta strandi350 – 3589
    Helixi362 – 37615

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1C3BX-ray2.25A/B20-377[»]
    1FCMX-ray2.46A/B20-377[»]
    1FCNX-ray2.35A/B20-377[»]
    1FCOX-ray2.20A/B20-377[»]
    1FSWX-ray1.90A/B20-376[»]
    1FSYX-ray1.75A/B20-376[»]
    1GA9X-ray2.10A/B20-377[»]
    1I5QX-ray1.83A/B20-377[»]
    1IELX-ray2.00A/B20-377[»]
    1IEMX-ray2.30A/B20-377[»]
    1KDSX-ray2.15A/B20-377[»]
    1KDWX-ray2.28A/B20-377[»]
    1KE0X-ray2.30A/B20-377[»]
    1KE3X-ray2.15A/B20-377[»]
    1KE4X-ray1.72A/B20-377[»]
    1KVLX-ray1.53A/B20-377[»]
    1KVMX-ray2.06A/B20-377[»]
    1L0DX-ray1.53A/B20-377[»]
    1L0EX-ray1.90A/B20-377[»]
    1L0FX-ray1.66A/B20-377[»]
    1L0GX-ray1.50A/B20-377[»]
    1L2SX-ray1.94A/B20-377[»]
    1LL5X-ray1.80A/B20-377[»]
    1LL9X-ray1.87A/B20-377[»]
    1LLBX-ray1.72A/B20-377[»]
    1MXOX-ray1.83A/B20-377[»]
    1MY8X-ray1.72A/B20-377[»]
    1O07X-ray1.71A/B20-377[»]
    1PI4X-ray1.39A/B20-377[»]
    1PI5X-ray1.49A/B20-377[»]
    1XGIX-ray1.96A/B20-377[»]
    1XGJX-ray1.97A/B20-377[»]
    2BLSX-ray2.00A/B20-377[»]
    2FFYX-ray1.07A/B20-377[»]
    2HDQX-ray2.10A/B20-377[»]
    2HDRX-ray2.20A/B20-377[»]
    2HDSX-ray1.16A/B20-377[»]
    2HDUX-ray1.49A/B20-377[»]
    2I72X-ray2.20A/B20-377[»]
    2P9VX-ray1.80A/B20-377[»]
    2PU2X-ray1.86A/B20-377[»]
    2PU4X-ray2.00A/B20-377[»]
    2R9WX-ray1.80A/B20-377[»]
    2R9XX-ray1.90A/B20-377[»]
    2RCXX-ray2.00A/B20-377[»]
    3BLSX-ray2.30A/B20-377[»]
    3BM6X-ray2.10A/B20-377[»]
    3FKVX-ray1.85A/B20-377[»]
    3FKWX-ray1.50A/B20-377[»]
    3GQZX-ray1.80A/B20-377[»]
    3GR2X-ray1.80A/B20-377[»]
    3GRJX-ray2.49A/B20-377[»]
    3GSGX-ray2.10A/B20-377[»]
    3GTCX-ray1.90A/B20-377[»]
    3GV9X-ray1.80A/B20-377[»]
    3GVBX-ray1.80A/B20-377[»]
    3IWIX-ray1.64A/B20-377[»]
    3IWOX-ray1.90A/B20-377[»]
    3IWQX-ray1.84A/B20-377[»]
    3IXBX-ray1.63A/B20-377[»]
    3IXDX-ray2.64A/B20-377[»]
    3IXGX-ray2.14A/B20-377[»]
    3IXHX-ray2.30A/B20-377[»]
    3O86X-ray1.60A/B20-377[»]
    3O87X-ray1.78A/B20-377[»]
    3O88X-ray1.64A/B20-377[»]
    4E3IX-ray1.60A/B20-377[»]
    4E3JX-ray1.80A/B20-377[»]
    4E3KX-ray1.43A/B20-377[»]
    4E3LX-ray1.43A/B20-377[»]
    4E3MX-ray1.44A/B20-377[»]
    4E3NX-ray1.49A/B20-377[»]
    4E3OX-ray1.60A/B20-377[»]
    4JXSX-ray1.90A/B20-377[»]
    4JXVX-ray1.76A/B20-377[»]
    4JXWX-ray2.30A/B20-377[»]
    4KZ3X-ray1.67A/B20-377[»]
    4KZ4X-ray1.42A/B20-377[»]
    4KZ5X-ray1.35A/B20-377[»]
    4KZ6X-ray1.68A/B20-377[»]
    4KZ7X-ray1.43A/B20-377[»]
    4KZ8X-ray2.28A/B20-377[»]
    4KZ9X-ray1.72A/B20-377[»]
    4KZAX-ray1.60A/B20-377[»]
    4KZBX-ray1.37A/B20-377[»]
    4OKPX-ray1.37A/B20-377[»]
    4OLDX-ray1.48A/B20-377[»]
    4OLGX-ray1.71A/B20-377[»]
    ProteinModelPortaliP00811.
    SMRiP00811. Positions 20-377.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00811.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni331 – 3333Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the class-C beta-lactamase family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG1680.
    HOGENOMiHOG000267102.
    KOiK01467.
    OMAiKVGDMTQ.
    OrthoDBiEOG60SCH1.
    PhylomeDBiP00811.

    Family and domain databases

    Gene3Di3.40.710.10. 1 hit.
    InterProiIPR001466. Beta-lactam-related.
    IPR012338. Beta-lactam/transpept-like.
    IPR001586. Beta-lactam_class-C_AS.
    [Graphical view]
    PfamiPF00144. Beta-lactamase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56601. SSF56601. 1 hit.
    PROSITEiPS00336. BETA_LACTAMASE_C. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P00811-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFKTTLCALL ITASCSTFAA PQQINDIVHR TITPLIEQQK IPGMAVAVIY    50
    QGKPYYFTWG YADIAKKQPV TQQTLFELGS VSKTFTGVLG GDAIARGEIK 100
    LSDPTTKYWP ELTAKQWNGI TLLHLATYTA GGLPLQVPDE VKSSSDLLRF 150
    YQNWQPAWAP GTQRLYANSS IGLFGALAVK PSGLSFEQAM QTRVFQPLKL 200
    NHTWINVPPA EEKNYAWGYR EGKAVHVSPG ALDAEAYGVK STIEDMARWV 250
    QSNLKPLDIN EKTLQQGIQL AQSRYWQTGD MYQGLGWEML DWPVNPDSII 300
    NGSDNKIALA ARPVKAITPP TPAVRASWVH KTGATGGFGS YVAFIPEKEL 350
    GIVMLANKNY PNPARVDAAW QILNALQ 377
    Length:377
    Mass (Da):41,556
    Last modified:July 21, 1986 - v1
    Checksum:i3C6FB4FE4EF96C9F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01611 Genomic DNA. Translation: AAA23441.1.
    U14003 Genomic DNA. Translation: AAA97049.1.
    U00096 Genomic DNA. Translation: AAC77110.1.
    AP009048 Genomic DNA. Translation: BAE78154.1.
    V00277 Genomic DNA. Translation: CAA23537.1.
    PIRiA01007. QKEC.
    RefSeqiNP_418574.1. NC_000913.3.
    YP_492295.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC77110; AAC77110; b4150.
    BAE78154; BAE78154; BAE78154.
    GeneIDi12932283.
    948669.
    KEGGiecj:Y75_p4039.
    eco:b4150.
    PATRICi32123873. VBIEscCol129921_4284.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01611 Genomic DNA. Translation: AAA23441.1 .
    U14003 Genomic DNA. Translation: AAA97049.1 .
    U00096 Genomic DNA. Translation: AAC77110.1 .
    AP009048 Genomic DNA. Translation: BAE78154.1 .
    V00277 Genomic DNA. Translation: CAA23537.1 .
    PIRi A01007. QKEC.
    RefSeqi NP_418574.1. NC_000913.3.
    YP_492295.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1C3B X-ray 2.25 A/B 20-377 [» ]
    1FCM X-ray 2.46 A/B 20-377 [» ]
    1FCN X-ray 2.35 A/B 20-377 [» ]
    1FCO X-ray 2.20 A/B 20-377 [» ]
    1FSW X-ray 1.90 A/B 20-376 [» ]
    1FSY X-ray 1.75 A/B 20-376 [» ]
    1GA9 X-ray 2.10 A/B 20-377 [» ]
    1I5Q X-ray 1.83 A/B 20-377 [» ]
    1IEL X-ray 2.00 A/B 20-377 [» ]
    1IEM X-ray 2.30 A/B 20-377 [» ]
    1KDS X-ray 2.15 A/B 20-377 [» ]
    1KDW X-ray 2.28 A/B 20-377 [» ]
    1KE0 X-ray 2.30 A/B 20-377 [» ]
    1KE3 X-ray 2.15 A/B 20-377 [» ]
    1KE4 X-ray 1.72 A/B 20-377 [» ]
    1KVL X-ray 1.53 A/B 20-377 [» ]
    1KVM X-ray 2.06 A/B 20-377 [» ]
    1L0D X-ray 1.53 A/B 20-377 [» ]
    1L0E X-ray 1.90 A/B 20-377 [» ]
    1L0F X-ray 1.66 A/B 20-377 [» ]
    1L0G X-ray 1.50 A/B 20-377 [» ]
    1L2S X-ray 1.94 A/B 20-377 [» ]
    1LL5 X-ray 1.80 A/B 20-377 [» ]
    1LL9 X-ray 1.87 A/B 20-377 [» ]
    1LLB X-ray 1.72 A/B 20-377 [» ]
    1MXO X-ray 1.83 A/B 20-377 [» ]
    1MY8 X-ray 1.72 A/B 20-377 [» ]
    1O07 X-ray 1.71 A/B 20-377 [» ]
    1PI4 X-ray 1.39 A/B 20-377 [» ]
    1PI5 X-ray 1.49 A/B 20-377 [» ]
    1XGI X-ray 1.96 A/B 20-377 [» ]
    1XGJ X-ray 1.97 A/B 20-377 [» ]
    2BLS X-ray 2.00 A/B 20-377 [» ]
    2FFY X-ray 1.07 A/B 20-377 [» ]
    2HDQ X-ray 2.10 A/B 20-377 [» ]
    2HDR X-ray 2.20 A/B 20-377 [» ]
    2HDS X-ray 1.16 A/B 20-377 [» ]
    2HDU X-ray 1.49 A/B 20-377 [» ]
    2I72 X-ray 2.20 A/B 20-377 [» ]
    2P9V X-ray 1.80 A/B 20-377 [» ]
    2PU2 X-ray 1.86 A/B 20-377 [» ]
    2PU4 X-ray 2.00 A/B 20-377 [» ]
    2R9W X-ray 1.80 A/B 20-377 [» ]
    2R9X X-ray 1.90 A/B 20-377 [» ]
    2RCX X-ray 2.00 A/B 20-377 [» ]
    3BLS X-ray 2.30 A/B 20-377 [» ]
    3BM6 X-ray 2.10 A/B 20-377 [» ]
    3FKV X-ray 1.85 A/B 20-377 [» ]
    3FKW X-ray 1.50 A/B 20-377 [» ]
    3GQZ X-ray 1.80 A/B 20-377 [» ]
    3GR2 X-ray 1.80 A/B 20-377 [» ]
    3GRJ X-ray 2.49 A/B 20-377 [» ]
    3GSG X-ray 2.10 A/B 20-377 [» ]
    3GTC X-ray 1.90 A/B 20-377 [» ]
    3GV9 X-ray 1.80 A/B 20-377 [» ]
    3GVB X-ray 1.80 A/B 20-377 [» ]
    3IWI X-ray 1.64 A/B 20-377 [» ]
    3IWO X-ray 1.90 A/B 20-377 [» ]
    3IWQ X-ray 1.84 A/B 20-377 [» ]
    3IXB X-ray 1.63 A/B 20-377 [» ]
    3IXD X-ray 2.64 A/B 20-377 [» ]
    3IXG X-ray 2.14 A/B 20-377 [» ]
    3IXH X-ray 2.30 A/B 20-377 [» ]
    3O86 X-ray 1.60 A/B 20-377 [» ]
    3O87 X-ray 1.78 A/B 20-377 [» ]
    3O88 X-ray 1.64 A/B 20-377 [» ]
    4E3I X-ray 1.60 A/B 20-377 [» ]
    4E3J X-ray 1.80 A/B 20-377 [» ]
    4E3K X-ray 1.43 A/B 20-377 [» ]
    4E3L X-ray 1.43 A/B 20-377 [» ]
    4E3M X-ray 1.44 A/B 20-377 [» ]
    4E3N X-ray 1.49 A/B 20-377 [» ]
    4E3O X-ray 1.60 A/B 20-377 [» ]
    4JXS X-ray 1.90 A/B 20-377 [» ]
    4JXV X-ray 1.76 A/B 20-377 [» ]
    4JXW X-ray 2.30 A/B 20-377 [» ]
    4KZ3 X-ray 1.67 A/B 20-377 [» ]
    4KZ4 X-ray 1.42 A/B 20-377 [» ]
    4KZ5 X-ray 1.35 A/B 20-377 [» ]
    4KZ6 X-ray 1.68 A/B 20-377 [» ]
    4KZ7 X-ray 1.43 A/B 20-377 [» ]
    4KZ8 X-ray 2.28 A/B 20-377 [» ]
    4KZ9 X-ray 1.72 A/B 20-377 [» ]
    4KZA X-ray 1.60 A/B 20-377 [» ]
    4KZB X-ray 1.37 A/B 20-377 [» ]
    4OKP X-ray 1.37 A/B 20-377 [» ]
    4OLD X-ray 1.48 A/B 20-377 [» ]
    4OLG X-ray 1.71 A/B 20-377 [» ]
    ProteinModelPortali P00811.
    SMRi P00811. Positions 20-377.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P00811. 1 interaction.
    STRINGi 511145.b4150.

    Chemistry

    BindingDBi P00811.
    ChEMBLi CHEMBL2026.
    DrugBanki DB00456. Cefalotin.
    DB01147. Cloxacillin.

    Protein family/group databases

    MEROPSi S12.006.

    PTM databases

    PhosSitei P0809371.

    2D gel databases

    SWISS-2DPAGE P00811.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC77110 ; AAC77110 ; b4150 .
    BAE78154 ; BAE78154 ; BAE78154 .
    GeneIDi 12932283.
    948669.
    KEGGi ecj:Y75_p4039.
    eco:b4150.
    PATRICi 32123873. VBIEscCol129921_4284.

    Organism-specific databases

    EchoBASEi EB0038.
    EcoGenei EG10040. ampC.

    Phylogenomic databases

    eggNOGi COG1680.
    HOGENOMi HOG000267102.
    KOi K01467.
    OMAi KVGDMTQ.
    OrthoDBi EOG60SCH1.
    PhylomeDBi P00811.

    Enzyme and pathway databases

    BioCyci EcoCyc:EG10040-MONOMER.
    ECOL316407:JW4111-MONOMER.
    MetaCyc:EG10040-MONOMER.
    SABIO-RK P00811.

    Miscellaneous databases

    EvolutionaryTracei P00811.
    PROi P00811.

    Gene expression databases

    Genevestigatori P00811.

    Family and domain databases

    Gene3Di 3.40.710.10. 1 hit.
    InterProi IPR001466. Beta-lactam-related.
    IPR012338. Beta-lactam/transpept-like.
    IPR001586. Beta-lactam_class-C_AS.
    [Graphical view ]
    Pfami PF00144. Beta-lactamase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56601. SSF56601. 1 hit.
    PROSITEi PS00336. BETA_LACTAMASE_C. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "ampC cephalosporinase of Escherichia coli K-12 has a different evolutionary origin from that of beta-lactamases of the penicillinase type."
      Jaurin B., Grundstroem T.
      Proc. Natl. Acad. Sci. U.S.A. 78:4897-4901(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 20-31.
      Strain: K12.
    2. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
      Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
      Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    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. "Overlap between ampC and frd operons on the Escherichia coli chromosome."
      Grundstroem T., Jaurin B.
      Proc. Natl. Acad. Sci. U.S.A. 79:1111-1115(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
    6. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    7. "Three-dimensional structure of AmpC beta-lactamase from Escherichia coli bound to a transition-state analogue: possible implications for the oxyanion hypothesis and for inhibitor design."
      Usher K.C., Blaszczak L.C., Weston G.S., Shoichet B.K., Remington S.J.
      Biochemistry 37:16082-16092(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    8. "The complexed structure and antimicrobial activity of a non-beta-lactam inhibitor of AmpC beta-lactamase."
      Powers R.A., Blazquez J., Weston G.S., Morosini M.I., Baquero F., Shoichet B.K.
      Protein Sci. 8:2330-2337(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
    9. "Structures of ceftazidime and its transition-state analogue in complex with AmpC beta-lactamase: implications for resistance mutations and inhibitor design."
      Powers R.A., Caselli E., Focia P.J., Prati F., Shoichet B.K.
      Biochemistry 40:9207-9214(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGUE.
    10. "Structural bases of stability-function tradeoffs in enzymes."
      Beadle B.M., Shoichet B.K.
      J. Mol. Biol. 321:285-296(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.53 ANGSTROMS), MUTAGENESIS OF SER-80; LYS-83; TYR-166; ASN-168 AND LYS-331.
    11. Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS).

    Entry informationi

    Entry nameiAMPC_ECOLI
    AccessioniPrimary (citable) accession number: P00811
    Secondary accession number(s): Q2M6F2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 144 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

    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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3