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Protein
Submitted name:

Metallo-beta-lactamase

Gene

SMB-1

Organism
Serratia marcescens
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi90 – 901Zinc 1; via tele nitrogenCombined sources
Metal bindingi92 – 921Zinc 1; via pros nitrogenCombined sources
Metal bindingi94 – 941Zinc 2Combined sources
Metal bindingi95 – 951Zinc 2; via tele nitrogenCombined sources
Metal bindingi168 – 1681Zinc 1; via tele nitrogenCombined sources
Metal bindingi233 – 2331Zinc 2; via tele nitrogenCombined sources

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Ligandi

Metal-bindingCombined sources, ZincCombined sources

Names & Taxonomyi

Protein namesi
Submitted name:
Metallo-beta-lactamaseImported
Gene namesi
Name:SMB-1Imported
OrganismiSerratia marcescensImported
Taxonomic identifieri615 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSerratia

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi180 ↔ 185Combined sources
Disulfide bondi226 ↔ 260Combined sources

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VPEX-ray1.60A19-280[»]
3VQZX-ray2.20A19-280[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
InterProiIPR001279. Beta-lactamas-like.
[Graphical view]
PfamiPF00753. Lactamase_B. 1 hit.
[Graphical view]
SMARTiSM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMiSSF56281. SSF56281. 1 hit.

Sequencei

Sequence statusi: Complete.

G5ELM3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIIASLILA AFASVAQAQD RDWSSPQQPF TIYGNTHYVG TGGISAVLLS
60 70 80 90 100
SPQGHILVDG TTEKGAQVVA ANIRAMGFKL SDVKYILSTH SHEDHAGGIS
110 120 130 140 150
AMQKLTGATV LAGAANVDTL RTGVSPKSDP QFGSLSNFPG SAKVRAVADG
160 170 180 190 200
ELVKLGPLAV KAHATPGHTE GGITWTWQSC EQGKCKDVVF ADSLTAVSAD
210 220 230 240 250
SYRFSDHPEV VASLRGSFEA VEKLSCDIAI AAHPEVNDMW TRQQRAAKEG
260 270 280
NSAYVDNGAC RAIAAAGRKR LETRLASEKR
Length:280
Mass (Da):29,518
Last modified:January 25, 2012 - v1
Checksum:i9F3E9CE4F4EFCBBD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB636283 Genomic DNA. Translation: BAL14456.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB636283 Genomic DNA. Translation: BAL14456.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VPEX-ray1.60A19-280[»]
3VQZX-ray2.20A19-280[»]
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
InterProiIPR001279. Beta-lactamas-like.
[Graphical view]
PfamiPF00753. Lactamase_B. 1 hit.
[Graphical view]
SMARTiSM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMiSSF56281. SSF56281. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "SMB-1, a Novel Subclass B3 Metallo-beta-Lactamase, Associated with ISCR1 and a Class 1 Integron, from a Carbapenem-Resistant Serratia marcescens Clinical Isolate."
    Wachino J., Yoshida H., Yamane K., Suzuki S., Matsui M., Yamagishi T., Tsutsui A., Konda T., Shibayama K., Arakawa Y.
    Antimicrob. Agents Chemother. 55:5143-5149(2011)
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: 148Imported.
  2. "Structural insights into the subclass B3 metallo-?-lactamase SMB-1 and the mode of inhibition by the common metallo-?-lactamase inhibitor mercaptoacetate."
    Wachino J., Yamaguchi Y., Mori S., Kurosaki H., Arakawa Y., Shibayama K.
    Antimicrob. Agents Chemother. 57:101-109(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 19-280 IN COMPLEX WITH ZINC, ACTIVE SITE.

Entry informationi

Entry nameiG5ELM3_SERMA
AccessioniPrimary (citable) accession number: G5ELM3
Entry historyi
Integrated into UniProtKB/TrEMBL: January 25, 2012
Last sequence update: January 25, 2012
Last modified: March 4, 2015
This is version 16 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.