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P05364

- AMPC_ENTCL

UniProt

P05364 - AMPC_ENTCL

Protein

Beta-lactamase

Gene

ampC

Organism
Enterobacter cloacae
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 1 (01 Nov 1988)
      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 sitei84 – 841Acyl-ester intermediate
    Active sitei170 – 1701Proton acceptor

    GO - Molecular functioni

    1. beta-lactamase activity Source: UniProtKB-EC

    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

    SABIO-RKP05364.

    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
    OrganismiEnterobacter cloacae
    Taxonomic identifieri550 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEnterobacterEnterobacter cloacae complex

    Subcellular locationi

    Periplasm By similarity

    GO - Cellular componenti

    1. outer membrane-bounded periplasmic space Source: InterPro

    Keywords - Cellular componenti

    Periplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Add
    BLAST
    Chaini21 – 381361Beta-lactamasePRO_0000016959Add
    BLAST

    Interactioni

    Structurei

    Secondary structure

    1
    381
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi25 – 4218
    Beta strandi46 – 549
    Beta strandi57 – 6711
    Turni68 – 714
    Beta strandi79 – 813
    Helixi83 – 853
    Helixi86 – 9914
    Helixi109 – 1124
    Helixi119 – 1213
    Helixi126 – 1305
    Helixi148 – 15710
    Beta strandi166 – 1683
    Helixi172 – 18211
    Helixi184 – 1863
    Helixi190 – 1978
    Turni198 – 2036
    Beta strandi207 – 2104
    Helixi213 – 2186
    Beta strandi222 – 2243
    Beta strandi227 – 2293
    Helixi237 – 2415
    Helixi247 – 25812
    Helixi260 – 2623
    Helixi266 – 27510
    Beta strandi277 – 2826
    Beta strandi285 – 2873
    Beta strandi292 – 2976
    Helixi300 – 3078
    Helixi309 – 3124
    Beta strandi319 – 3257
    Beta strandi329 – 33810
    Beta strandi343 – 3497
    Helixi350 – 3523
    Beta strandi354 – 3629
    Helixi366 – 37914

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BLSX-ray2.30A/B21-381[»]
    1GCEX-ray1.80A21-381[»]
    1RGZX-ray1.37A22-381[»]
    1XX2X-ray1.88A/B21-381[»]
    1Y54X-ray2.10A21-381[»]
    2Q9MX-ray2.05A22-380[»]
    2Q9NX-ray2.20A22-380[»]
    3S4XX-ray1.95A21-381[»]
    ProteinModelPortaliP05364.
    SMRiP05364. Positions 22-380.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05364.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni335 – 3373Substrate binding

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal

    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.

    P05364-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMRKSLCCAL LLGISCSALA TPVSEKQLAE VVANTITPLM KAQSVPGMAV    50
    AVIYQGKPHY YTFGKADIAA NKPVTPQTLF ELGSISKTFT GVLGGDAIAR 100
    GEISLDDAVT RYWPQLTGKQ WQGIRMLDLA TYTAGGLPLQ VPDEVTDNAS 150
    LLRFYQNWQP QWKPGTTRLY ANASIGLFGA LAVKPSGMPY EQAMTTRVLK 200
    PLKLDHTWIN VPKAEEAHYA WGYRDGKAVR VSPGMLDAQA YGVKTNVQDM 250
    ANWVMANMAP ENVADASLKQ GIALAQSRYW RIGSMYQGLG WEMLNWPVEA 300
    NTVVEGSDSK VALAPLPVAE VNPPAPPVKA SWVHKTGSTG GFGSYVAFIP 350
    EKQIGIVMLA NTSYPNPARV EAAYHILEAL Q 381
    Length:381
    Mass (Da):41,302
    Last modified:November 1, 1988 - v1
    Checksum:i90F56ABAF07AA304
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti3 – 31R → I in strain: MHN1.
    Natural varianti14 – 141I → L in strain: MHN1.
    Natural varianti21 – 211T → A in strain: MHN1.
    Natural varianti36 – 361I → V in strain: MHN1 and Q980R.
    Natural varianti58 – 581P → S in strain: MHN1.
    Natural varianti108 – 1081A → P in strain: MHN1 and Q980R.
    Natural varianti152 – 1521L → V in strain: Q980R.
    Natural varianti262 – 2621N → K in strain: MHN1.
    Natural varianti319 – 3191A → V in strain: Q980R.
    Natural varianti362 – 3621T → K in strain: MHN1.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07274 Genomic DNA. Translation: CAA30257.1.
    X08082 Genomic DNA. Translation: CAA30879.1.
    X08081 Genomic DNA. Translation: CAA30878.1.
    PIRiS00404. PNKBP.
    S00405. PNKBQ.
    S00406. PNKBM.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07274 Genomic DNA. Translation: CAA30257.1 .
    X08082 Genomic DNA. Translation: CAA30879.1 .
    X08081 Genomic DNA. Translation: CAA30878.1 .
    PIRi S00404. PNKBP.
    S00405. PNKBQ.
    S00406. PNKBM.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BLS X-ray 2.30 A/B 21-381 [» ]
    1GCE X-ray 1.80 A 21-381 [» ]
    1RGZ X-ray 1.37 A 22-381 [» ]
    1XX2 X-ray 1.88 A/B 21-381 [» ]
    1Y54 X-ray 2.10 A 21-381 [» ]
    2Q9M X-ray 2.05 A 22-380 [» ]
    2Q9N X-ray 2.20 A 22-380 [» ]
    3S4X X-ray 1.95 A 21-381 [» ]
    ProteinModelPortali P05364.
    SMRi P05364. Positions 22-380.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P05364.
    ChEMBLi CHEMBL2725.

    Protein family/group databases

    MEROPSi S12.006.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK P05364.

    Miscellaneous databases

    EvolutionaryTracei P05364.

    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. "Sequence and comparative analysis of three Enterobacter cloacae ampC beta-lactamase genes and their products."
      Galleni M., Lindberg F., Normark S., Cole S., Honore N., Joris B., Frere J.-M.
      Biochem. J. 250:753-760(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: MHN1, P99 and Q908R.
    2. "Evolution of an enzyme activity: crystallographic structure at 2-A resolution of cephalosporinase from the ampC gene of Enterobacter cloacae P99 and comparison with a class A penicillinase."
      Lobkovsky E., Moews P.C., Liu H., Zhao H., Frere J.-M., Knox J.R.
      Proc. Natl. Acad. Sci. U.S.A. 90:11257-11261(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
      Strain: P99.
    3. "Crystallographic structure of a phosphonate derivative of the Enterobacter cloacae P99 cephalosporinase: mechanistic interpretation of a beta-lactamase transition-state analog."
      Lobkovsky E., Billings E.M., Moews P.C., Rahil J., Pratt R.F., Knox J.R.
      Biochemistry 33:6762-6772(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
      Strain: P99.

    Entry informationi

    Entry nameiAMPC_ENTCL
    AccessioniPrimary (citable) accession number: P05364
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: November 1, 1988
    Last modified: October 1, 2014
    This is version 93 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The sequence shown is that of strain P99.

    Keywords - Technical termi

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3