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Protein

Beta-lactamase SHV-1

Gene

bla

Organism
Klebsiella pneumoniae
Status
Reviewed-Annotation score: 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 sitei66 – 661Acyl-ester intermediate
Active sitei164 – 1641Proton acceptor

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

Enzyme and pathway databases

BRENDAi3.5.2.6. 2814.
SABIO-RKP0AD64.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-lactamase SHV-1 (EC:3.5.2.6)
Alternative name(s):
PIT-2
Gene namesi
Name:bla
Synonyms:shv1
Encoded oniPlasmid R9741 Publication
OrganismiKlebsiella pneumoniae
Taxonomic identifieri573 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Add
BLAST
Chaini22 – 286265Beta-lactamase SHV-1PRO_0000043362Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi73 ↔ 119

Keywords - PTMi

Disulfide bond

Interactioni

Structurei

Secondary structure

1
286
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi25 – 3612Combined sources
Beta strandi38 – 469Combined sources
Turni47 – 493Combined sources
Beta strandi52 – 576Combined sources
Helixi65 – 673Combined sources
Helixi68 – 8114Combined sources
Helixi95 – 973Combined sources
Helixi105 – 1084Combined sources
Turni109 – 1113Combined sources
Helixi115 – 12511Combined sources
Helixi128 – 13710Combined sources
Helixi140 – 15011Combined sources
Helixi164 – 1663Combined sources
Helixi179 – 19113Combined sources
Beta strandi192 – 1954Combined sources
Helixi197 – 20812Combined sources
Beta strandi211 – 2133Combined sources
Helixi214 – 2207Combined sources
Beta strandi226 – 2338Combined sources
Helixi235 – 2373Combined sources
Beta strandi239 – 2479Combined sources
Beta strandi253 – 2619Combined sources
Helixi266 – 28217Combined sources
Turni283 – 2853Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ONGX-ray1.10A22-286[»]
1Q2PX-ray2.00A22-286[»]
1RCJX-ray1.63A22-286[»]
1SHVX-ray1.98A22-286[»]
1TDGX-ray1.80A22-286[»]
1TDLX-ray1.80A22-286[»]
1VM1X-ray2.02A22-286[»]
2A3UX-ray1.34A22-286[»]
2A49X-ray1.43A22-286[»]
2G2UX-ray1.60A22-284[»]
2G2WX-ray1.80A22-284[»]
2H0TX-ray1.60A22-286[»]
2H0YX-ray1.70A22-284[»]
2H10X-ray1.75A22-284[»]
2H5SX-ray1.28A22-286[»]
2ZD8X-ray1.05A22-286[»]
3C4OX-ray1.70A22-286[»]
3C4PX-ray1.75A22-286[»]
3D4FX-ray1.55A1-286[»]
3MKEX-ray1.75A22-286[»]
3MKFX-ray1.33A22-286[»]
3MXRX-ray1.30A22-286[»]
3MXSX-ray1.24A22-286[»]
3N4IX-ray1.56A22-286[»]
3OPHX-ray1.34A1-286[»]
3OPLX-ray1.80A1-286[»]
3OPPX-ray1.80A1-286[»]
3OPRX-ray1.65A1-286[»]
3V50X-ray1.45A22-286[»]
3V5MX-ray1.30A22-286[»]
4FCFX-ray1.09A22-286[»]
4FD8X-ray1.52A22-286[»]
4FH2X-ray1.44A22-286[»]
4FH4X-ray1.09A22-286[»]
4GD6X-ray1.53A1-286[»]
4GD8X-ray1.60A1-286[»]
4GDBX-ray1.84A1-286[»]
4JPMX-ray1.14A1-286[»]
4MBFX-ray1.54A22-286[»]
4MBHX-ray1.22A22-286[»]
4MBKX-ray1.46A22-286[»]
ProteinModelPortaliP0AD64.
SMRiP0AD64. Positions 22-286.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AD64.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni230 – 2323Substrate binding

Sequence similaritiesi

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

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.710.10. 1 hit.
InterProiIPR012338. Beta-lactam/transpept-like.
IPR000871. Beta-lactam_class-A/D.
IPR023650. Beta-lactam_class-A_AS.
[Graphical view]
PRINTSiPR00118. BLACTAMASEA.
SUPFAMiSSF56601. SSF56601. 1 hit.
PROSITEiPS00146. BETA_LACTAMASE_A. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0AD64-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRYIRLCIIS LLATLPLAVH ASPQPLEQIK LSESQLSGRV GMIEMDLASG
60 70 80 90 100
RTLTAWRADE RFPMMSTFKV VLCGAVLARV DAGDEQLERK IHYRQQDLVD
110 120 130 140 150
YSPVSEKHLA DGMTVGELCA AAITMSDNSA ANLLLATVGG PAGLTAFLRQ
160 170 180 190 200
IGDNVTRLDR WETELNEALP GDARDTTTPA SMAATLRKLL TSQRLSARSQ
210 220 230 240 250
RQLLQWMVDD RVAGPLIRSV LPAGWFIADK TGAGERGARG IVALLGPNNK
260 270 280
AERIVVIYLR DTPASMAERN QQIAGIGAAL IEHWQR
Length:286
Mass (Da):31,224
Last modified:December 6, 2005 - v1
Checksum:iC78F42667E698E6C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti112 – 1121G → A in AAA26087 (PubMed:2221867).Curated
Sequence conflicti188 – 1892KL → NVG in AAA26087 (PubMed:2221867).Curated
Sequence conflicti278 – 2781A → K in AAA26087 (PubMed:2221867).Curated
Sequence conflicti281 – 2811I → Y in AAA26087 (PubMed:2221867).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59181 Genomic DNA. Translation: AAA26087.1.
X98098 Genomic DNA. Translation: CAA66726.1.
X98099 Genomic DNA. Translation: CAA66727.1.
X98100 Genomic DNA. Translation: CAA66728.1.
AF124984 Genomic DNA. Translation: AAD18054.1.
PIRiA44996.
RefSeqiYP_009079584.1. NG_036025.1.
YP_009086336.1. NG_039544.1.
YP_009086337.1. NG_039545.1.
YP_009086341.1. NG_039549.1.
YP_009086348.1. NG_039556.1.
YP_009086350.1. NG_039558.1.
YP_009086351.1. NG_039559.1.
YP_009091661.1. NG_036755.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59181 Genomic DNA. Translation: AAA26087.1.
X98098 Genomic DNA. Translation: CAA66726.1.
X98099 Genomic DNA. Translation: CAA66727.1.
X98100 Genomic DNA. Translation: CAA66728.1.
AF124984 Genomic DNA. Translation: AAD18054.1.
PIRiA44996.
RefSeqiYP_009079584.1. NG_036025.1.
YP_009086336.1. NG_039544.1.
YP_009086337.1. NG_039545.1.
YP_009086341.1. NG_039549.1.
YP_009086348.1. NG_039556.1.
YP_009086350.1. NG_039558.1.
YP_009086351.1. NG_039559.1.
YP_009091661.1. NG_036755.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ONGX-ray1.10A22-286[»]
1Q2PX-ray2.00A22-286[»]
1RCJX-ray1.63A22-286[»]
1SHVX-ray1.98A22-286[»]
1TDGX-ray1.80A22-286[»]
1TDLX-ray1.80A22-286[»]
1VM1X-ray2.02A22-286[»]
2A3UX-ray1.34A22-286[»]
2A49X-ray1.43A22-286[»]
2G2UX-ray1.60A22-284[»]
2G2WX-ray1.80A22-284[»]
2H0TX-ray1.60A22-286[»]
2H0YX-ray1.70A22-284[»]
2H10X-ray1.75A22-284[»]
2H5SX-ray1.28A22-286[»]
2ZD8X-ray1.05A22-286[»]
3C4OX-ray1.70A22-286[»]
3C4PX-ray1.75A22-286[»]
3D4FX-ray1.55A1-286[»]
3MKEX-ray1.75A22-286[»]
3MKFX-ray1.33A22-286[»]
3MXRX-ray1.30A22-286[»]
3MXSX-ray1.24A22-286[»]
3N4IX-ray1.56A22-286[»]
3OPHX-ray1.34A1-286[»]
3OPLX-ray1.80A1-286[»]
3OPPX-ray1.80A1-286[»]
3OPRX-ray1.65A1-286[»]
3V50X-ray1.45A22-286[»]
3V5MX-ray1.30A22-286[»]
4FCFX-ray1.09A22-286[»]
4FD8X-ray1.52A22-286[»]
4FH2X-ray1.44A22-286[»]
4FH4X-ray1.09A22-286[»]
4GD6X-ray1.53A1-286[»]
4GD8X-ray1.60A1-286[»]
4GDBX-ray1.84A1-286[»]
4JPMX-ray1.14A1-286[»]
4MBFX-ray1.54A22-286[»]
4MBHX-ray1.22A22-286[»]
4MBKX-ray1.46A22-286[»]
ProteinModelPortaliP0AD64.
SMRiP0AD64. Positions 22-286.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP0AD64.
ChEMBLiCHEMBL5094.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.5.2.6. 2814.
SABIO-RKP0AD64.

Miscellaneous databases

EvolutionaryTraceiP0AD64.

Family and domain databases

Gene3Di3.40.710.10. 1 hit.
InterProiIPR012338. Beta-lactam/transpept-like.
IPR000871. Beta-lactam_class-A/D.
IPR023650. Beta-lactam_class-A_AS.
[Graphical view]
PRINTSiPR00118. BLACTAMASEA.
SUPFAMiSSF56601. SSF56601. 1 hit.
PROSITEiPS00146. BETA_LACTAMASE_A. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning of SHV-2, OHIO-1, and OXA-6 beta-lactamases and cloning and sequencing of SHV-1 beta-lactamase."
    Mercier J., Levesque R.C.
    Antimicrob. Agents Chemother. 34:1577-1583(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Plasmid: R974
  2. "Survey and molecular genetics of SHV beta-lactamases in Enterobacteriaceae in Switzerland: two novel enzymes, SHV-11 and SHV-12."
    Nuesch-Inderbinen M., Kayser F.H., Hachler H.
    Antimicrob. Agents Chemother. 41:943-949(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: KPAA-1, KPZU-13 and KPZU-8.
  3. "High-level expression of chromosomally encoded SHV-1 beta-lactamase and an outer membrane protein change confer resistance to ceftazidime and piperacillin-tazobactam in a clinical isolate of Klebsiella pneumoniae."
    Rice L.B., Carias L.L., Hujer A.M., Bonafede M., Hutton R., Hoyen C., Bonomo R.A.
    Antimicrob. Agents Chemother. 44:362-367(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 15571.
  4. Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS).
    Strain: 15571.

Entry informationi

Entry nameiBLA1_KLEPN
AccessioniPrimary (citable) accession number: P0AD64
Secondary accession number(s): O07941, P14557, P23982
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: April 1, 2015
This is version 54 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, Plasmid

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

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 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.