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P05193

- AMPC_CITFR

UniProt

P05193 - AMPC_CITFR

Protein

Beta-lactamase

Gene

ampC

Organism
Citrobacter freundii
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 1 (13 Aug 1987)
      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

    Enzyme regulationi

    Sulbactam is an effective progressive inhibitor but a poor competitive inhibitor.

    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: CACAO

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Antibiotic resistance

    Enzyme and pathway databases

    SABIO-RKP05193.

    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:blaC
    OrganismiCitrobacter freundii
    Taxonomic identifieri546 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeCitrobacterCitrobacter freundii complex

    Subcellular locationi

    Periplasm By similarity

    GO - Cellular componenti

    1. outer membrane-bounded periplasmic space Source: InterPro

    Keywords - Cellular componenti

    Periplasm

    Pathology & Biotechi

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Add
    BLAST
    Chaini21 – 381361Beta-lactamasePRO_0000016957Add
    BLAST

    Interactioni

    Structurei

    Secondary structure

    1
    381
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi25 – 4319
    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
    Turni183 – 1875
    Helixi190 – 1978
    Turni198 – 2036
    Beta strandi207 – 2104
    Helixi213 – 2186
    Beta strandi222 – 2243
    Beta strandi227 – 2293
    Helixi237 – 2404
    Helixi247 – 25812
    Helixi260 – 2623
    Helixi266 – 27510
    Beta strandi277 – 2826
    Beta strandi285 – 2873
    Beta strandi292 – 2976
    Helixi300 – 3067
    Helixi309 – 3124
    Beta strandi319 – 3257
    Beta strandi329 – 33810
    Beta strandi343 – 3497
    Helixi350 – 3523
    Beta strandi354 – 3629
    Helixi366 – 37813

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1RGYX-ray1.52A22-381[»]
    ProteinModelPortaliP05193.
    SMRiP05193. Positions 22-381.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05193.

    Family & Domainsi

    Region

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

    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.

    P05193-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMKKSICCAL LLTASFSTFA AAKTEQQIAD IVNRTITPLM QEQAIPGMAV    50
    AIIYEGKPYY FTWGKADIAN NHPVTQQTLF ELGSVSKTFN GVLGGDRIAR 100
    GEIKLSDPVT KYWPELTGKQ WRGISLLHLA TYTAGGLPLQ IPGDVTDKAE 150
    LLRFYQNWQP QWTPGAKRLY ANSSIGLFGA LAVKSSGMSY EEAMTRRVLQ 200
    PLKLAHTWIT VPQSEQKNYA WGYLEGKPVH VSPGQLDAEA YGVKSSVIDM 250
    ARWVQANMDA SHVQEKTLQQ GIELAQSRYW RIGDMYQGLG WEMLNWPLKA 300
    DSIINGSDSK VALAALPAVE VNPPAPAVKA SWVHKTGSTG GFGSYVAFVP 350
    EKNLGIVMLA NKSYPNPARV EAAWRILEKL Q 381
    Length:381
    Mass (Da):41,975
    Last modified:August 13, 1987 - v1
    Checksum:i3F955F6933F0D76B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti98 – 981I → T(PubMed:3263684)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti97 – 971R → A in strain: GN346.
    Natural varianti143 – 1431G → D in strain: GN346.
    Natural varianti145 – 1451V → I in strain: GN346.
    Natural varianti150 – 1501E → A in strain: GN346.
    Natural varianti185 – 1851S → P in strain: GN346.
    Natural varianti224 – 2241L → R in strain: GN346.
    Natural varianti243 – 2431V → L in strain: GN346.
    Natural varianti325 – 3251A → V in strain: GN346.
    Natural varianti368 – 3681A → V in strain: GN346.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03866 Genomic DNA. Translation: CAA27494.1.
    X51632 Genomic DNA. Translation: CAA35959.1.
    PIRiS08296.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03866 Genomic DNA. Translation: CAA27494.1 .
    X51632 Genomic DNA. Translation: CAA35959.1 .
    PIRi S08296.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1RGY X-ray 1.52 A 22-381 [» ]
    ProteinModelPortali P05193.
    SMRi P05193. Positions 22-381.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P05193.
    ChEMBLi CHEMBL1255130.
    DrugBanki DB00355. Aztreonam.

    Protein family/group databases

    MEROPSi S12.006.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK P05193.

    Miscellaneous databases

    EvolutionaryTracei P05193.

    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 of the Citrobacter freundii OS60 chromosomal ampC beta-lactamase gene."
      Lindberg F., Normark S.
      Eur. J. Biochem. 156:441-445(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: OS60.
    2. "Role of lysine-67 in the active site of class C beta-lactamase from Citrobacter freundii GN346."
      Tsukamoto K., Tachibana K., Yamazaki N., Ishii Y., Ujiie K., Nishida N., Sawai T.
      Eur. J. Biochem. 188:15-22(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: GN346.
    3. "Amino acid sequence, active-site residue, and effect of suicide inhibitors on cephalosporinase of Citrobacter freundii GN346."
      Sawai T., Yamaguchi A., Tsukamoto K.
      Rev. Infect. Dis. 10:721-725(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 21-381, INHIBITION BY SULBACTAM.
      Strain: GN346.
    4. "Identification of the active site of Citrobacter freundii beta-lactamase using dansyl-penicillin."
      Yamaguchi A., Adachi H., Sawai T.
      FEBS Lett. 218:126-130(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 66-87.
    5. "Refined crystal structure of beta-lactamase from Citrobacter freundii indicates a mechanism for beta-lactam hydrolysis."
      Oefner C., D'Arcy A.A., Daly J.J., Gubernator K., Charnas R.L., Heinze I., Hubschwerlen C., Winkler F.K.
      Nature 343:284-288(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

    Entry informationi

    Entry nameiAMPC_CITFR
    AccessioniPrimary (citable) accession number: P05193
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: August 13, 1987
    Last modified: October 1, 2014
    This is version 90 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, Direct protein sequencing

    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