Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P05193

- AMPC_CITFR

UniProt

P05193 - AMPC_CITFR

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Beta-lactamase

Gene

ampC

Organism
Citrobacter freundii
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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 – 4319Combined sources
Beta strandi46 – 549Combined sources
Beta strandi57 – 6711Combined sources
Turni68 – 714Combined sources
Beta strandi79 – 813Combined sources
Helixi83 – 853Combined sources
Helixi86 – 9914Combined sources
Helixi109 – 1124Combined sources
Helixi119 – 1213Combined sources
Helixi126 – 1305Combined sources
Helixi148 – 15710Combined sources
Beta strandi166 – 1683Combined sources
Helixi172 – 18211Combined sources
Turni183 – 1875Combined sources
Helixi190 – 1978Combined sources
Turni198 – 2036Combined sources
Beta strandi207 – 2104Combined sources
Helixi213 – 2186Combined sources
Beta strandi222 – 2243Combined sources
Beta strandi227 – 2293Combined sources
Helixi237 – 2404Combined sources
Helixi247 – 25812Combined sources
Helixi260 – 2623Combined sources
Helixi266 – 27510Combined sources
Beta strandi277 – 2826Combined sources
Beta strandi285 – 2873Combined sources
Beta strandi292 – 2976Combined sources
Helixi300 – 3067Combined sources
Helixi309 – 3124Combined sources
Beta strandi319 – 3257Combined sources
Beta strandi329 – 33810Combined sources
Beta strandi343 – 3497Combined sources
Helixi350 – 3523Combined sources
Beta strandi354 – 3629Combined sources
Helixi366 – 37813Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MMKKSICCAL LLTASFSTFA AAKTEQQIAD IVNRTITPLM QEQAIPGMAV
60 70 80 90 100
AIIYEGKPYY FTWGKADIAN NHPVTQQTLF ELGSVSKTFN GVLGGDRIAR
110 120 130 140 150
GEIKLSDPVT KYWPELTGKQ WRGISLLHLA TYTAGGLPLQ IPGDVTDKAE
160 170 180 190 200
LLRFYQNWQP QWTPGAKRLY ANSSIGLFGA LAVKSSGMSY EEAMTRRVLQ
210 220 230 240 250
PLKLAHTWIT VPQSEQKNYA WGYLEGKPVH VSPGQLDAEA YGVKSSVIDM
260 270 280 290 300
ARWVQANMDA SHVQEKTLQQ GIELAQSRYW RIGDMYQGLG WEMLNWPLKA
310 320 330 340 350
DSIINGSDSK VALAALPAVE VNPPAPAVKA SWVHKTGSTG GFGSYVAFVP
360 370 380
EKNLGIVMLA NKSYPNPARV EAAWRILEKL Q
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:
EMBLi
GenBanki
DDBJi
Links Updated
X03866 Genomic DNA. Translation: CAA27494.1.
X51632 Genomic DNA. Translation: CAA35959.1.
PIRiS08296.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03866 Genomic DNA. Translation: CAA27494.1 .
X51632 Genomic DNA. Translation: CAA35959.1 .
PIRi S08296.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 91 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