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P14559

- BLAC_STRAL

UniProt

P14559 - BLAC_STRAL

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Protein

Beta-lactamase

Gene
N/A
Organism
Streptomyces albus G
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei89 – 891Acyl-ester intermediate1 PublicationPROSITE-ProRule annotation

GO - Molecular functioni

  1. beta-lactamase activity Source: UniProtKB-EC

GO - Biological processi

  1. beta-lactam antibiotic catabolic process Source: InterPro
  2. response to antibiotic Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Antibiotic resistance

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-lactamase (EC:3.5.2.6)
Alternative name(s):
Penicillinase
OrganismiStreptomyces albus G
Taxonomic identifieri1962 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3939Tat-type signalAdd
BLAST
Chaini40 – 314275Beta-lactamasePRO_0000017012Add
BLAST

Post-translational modificationi

Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.

Structurei

Secondary structure

1
314
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi48 – 6013Combined sources
Beta strandi62 – 709Combined sources
Turni71 – 733Combined sources
Beta strandi76 – 805Combined sources
Helixi88 – 914Combined sources
Helixi92 – 10211Combined sources
Beta strandi105 – 1073Combined sources
Turni108 – 1114Combined sources
Helixi118 – 1247Combined sources
Turni129 – 1324Combined sources
Helixi134 – 1396Combined sources
Helixi144 – 15310Combined sources
Helixi157 – 16711Combined sources
Helixi171 – 1799Combined sources
Helixi193 – 1953Combined sources
Helixi208 – 21912Combined sources
Beta strandi221 – 2244Combined sources
Helixi226 – 23712Combined sources
Turni243 – 2453Combined sources
Helixi246 – 2494Combined sources
Beta strandi254 – 2629Combined sources
Beta strandi268 – 2758Combined sources
Beta strandi282 – 2898Combined sources
Helixi299 – 31214Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BSGX-ray1.85A47-314[»]
ProteinModelPortaliP14559.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14559.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni259 – 2613Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the class-A 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.
IPR000871. Beta-lactam_class-A/D.
IPR023650. Beta-lactam_class-A_AS.
IPR006311. TAT_signal.
[Graphical view]
PfamiPF00144. Beta-lactamase. 1 hit.
[Graphical view]
PRINTSiPR00118. BLACTAMASEA.
SUPFAMiSSF56601. SSF56601. 1 hit.
PROSITEiPS00146. BETA_LACTAMASE_A. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P14559-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MHPSTSRPSR RTLLTATAGA ALAAATLVPG TAHASSGGRG HGSGSVSDAE
60 70 80 90 100
RRLAGLERAS GARLGVYAYD TGSGRTVAYR ADELFPMCSV FKTLSSAAVL
110 120 130 140 150
RDLDRNGEFL SRRILYTQDD VEQADGAGPE TGKPQNLANA QLTVEELCEV
160 170 180 190 200
SITASDNCAA NLMLRELGGP AAVTRFVRSL GDRVTRLDRW EPELNSAEPG
210 220 230 240 250
RVTDTTSPRA ITRTYGRLVL GDALNPRDRR LLTSWLLANT TSGDRFRAGL
260 270 280 290 300
PDDWTLGDKT GAGRYGTNND AGVTWPPGRA PIVLTVLTAK TEQDAARDDG
310
LVADAARVLA ETLG
Length:314
Mass (Da):33,265
Last modified:January 1, 1990 - v1
Checksum:i5A17D7D19C84E511
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M28303 Genomic DNA. Translation: AAA26775.1.
PIRiS00057. PNSM1U.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M28303 Genomic DNA. Translation: AAA26775.1 .
PIRi S00057. PNSM1U.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BSG X-ray 1.85 A 47-314 [» ]
ProteinModelPortali P14559.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P14559.

Family and domain databases

Gene3Di 3.40.710.10. 1 hit.
InterProi IPR001466. Beta-lactam-related.
IPR012338. Beta-lactam/transpept-like.
IPR000871. Beta-lactam_class-A/D.
IPR023650. Beta-lactam_class-A_AS.
IPR006311. TAT_signal.
[Graphical view ]
Pfami PF00144. Beta-lactamase. 1 hit.
[Graphical view ]
PRINTSi PR00118. BLACTAMASEA.
SUPFAMi SSF56601. SSF56601. 1 hit.
PROSITEi PS00146. BETA_LACTAMASE_A. 1 hit.
PS51318. TAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Nucleotide sequence of the gene encoding the Streptomyces albus G beta-lactamase precursor."
    Dehottay P., Dusart J., de Meester F., Joris B., van Beeumen J., Erpicum T., Frere J.-M., Ghuysen J.-M.
    Eur. J. Biochem. 166:345-350(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
  2. "The active sites of the beta-lactamases of Streptomyces cacaoi and Streptomyces albus G."
    de Meester F., Joris B., Lenzini M.V., Dehottay P., Erpicium T., Dusart J., Klein D., Ghuysen J.-M., Frere J.-M., van Beeumen J.
    Biochem. J. 244:427-432(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 81-92, ACTIVE SITE SER-89.
  3. Fonze E., Charlier P., Dideberg O.
    Submitted (JUL-1998) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 47-314.

Entry informationi

Entry nameiBLAC_STRAL
AccessioniPrimary (citable) accession number: P14559
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: November 26, 2014
This is version 81 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