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Protein

Beta-lactamase

Gene

ampC

Organism
Citrobacter freundii
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei84Acyl-ester intermediate1
Active sitei170Proton acceptor1

GO - Molecular functioni

GO - Biological processi

  • antibiotic catabolic process Source: InterPro
  • 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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeCitrobacterCitrobacter freundii complex

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1255130.
DrugBankiDB00355. Aztreonam.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Add BLAST20
ChainiPRO_000001695721 – 381Beta-lactamaseAdd BLAST361

Interactioni

Chemistry databases

BindingDBiP05193.

Structurei

Secondary structure

1381
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi25 – 43Combined sources19
Beta strandi46 – 54Combined sources9
Beta strandi57 – 67Combined sources11
Turni68 – 71Combined sources4
Beta strandi79 – 81Combined sources3
Helixi83 – 85Combined sources3
Helixi86 – 99Combined sources14
Helixi109 – 112Combined sources4
Helixi119 – 121Combined sources3
Helixi126 – 130Combined sources5
Helixi148 – 157Combined sources10
Beta strandi166 – 168Combined sources3
Helixi172 – 182Combined sources11
Turni183 – 187Combined sources5
Helixi190 – 197Combined sources8
Turni198 – 203Combined sources6
Beta strandi207 – 210Combined sources4
Helixi213 – 218Combined sources6
Beta strandi222 – 224Combined sources3
Beta strandi227 – 229Combined sources3
Helixi237 – 240Combined sources4
Helixi247 – 258Combined sources12
Helixi260 – 262Combined sources3
Helixi266 – 275Combined sources10
Beta strandi277 – 282Combined sources6
Beta strandi285 – 287Combined sources3
Beta strandi292 – 297Combined sources6
Helixi300 – 306Combined sources7
Helixi309 – 312Combined sources4
Beta strandi319 – 325Combined sources7
Beta strandi329 – 338Combined sources10
Beta strandi343 – 349Combined sources7
Helixi350 – 352Combined sources3
Beta strandi354 – 362Combined sources9
Helixi366 – 378Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RGYX-ray1.52A22-381[»]
ProteinModelPortaliP05193.
SMRiP05193.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05193.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni335 – 337Substrate bindingBy similarity3

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)DescriptionActionsGraphical viewLength
Sequence conflicti98I → T (PubMed:3263684).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti97R → A in strain: GN346. 1
Natural varianti143G → D in strain: GN346. 1
Natural varianti145V → I in strain: GN346. 1
Natural varianti150E → A in strain: GN346. 1
Natural varianti185S → P in strain: GN346. 1
Natural varianti224L → R in strain: GN346. 1
Natural varianti243V → L in strain: GN346. 1
Natural varianti325A → V in strain: GN346. 1
Natural varianti368A → V in strain: GN346. 1

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.
PIRiS08296.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RGYX-ray1.52A22-381[»]
ProteinModelPortaliP05193.
SMRiP05193.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiP05193.
ChEMBLiCHEMBL1255130.
DrugBankiDB00355. Aztreonam.

Protein family/group databases

MEROPSiS12.006.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP05193.

Miscellaneous databases

EvolutionaryTraceiP05193.

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]
ProtoNetiSearch...

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 2, 2016
This is version 95 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

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.