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Protein

Metallo-beta-lactamase L1 type 3

Gene
N/A
Organism
Stenotrophomonas maltophilia (Pseudomonas maltophilia) (Xanthomonas maltophilia)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Confers resistance to the different beta-lactams antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring.2 Publications

Catalytic activityi

A beta-lactam + H2O = a substituted beta-amino acid.1 Publication

Cofactori

Zn2+2 PublicationsNote: Binds 2 Zn2+ ions per subunit.2 Publications

Enzyme regulationi

Inhibited by Hg2+ or Cu2+, and by chelating agents such as EDTA and O-phenanthroline. Reduced enzymatic activity in presence of cobalt, nickel, cadmium, and manganese.1 Publication

pH dependencei

Unstable below pH 8, unless zinc is present.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi105Zinc 1; via tele nitrogen2 Publications1
Metal bindingi107Zinc 1; via pros nitrogen2 Publications1
Metal bindingi109Zinc 22 Publications1
Metal bindingi110Zinc 2; via tele nitrogen2 Publications1
Metal bindingi181Zinc 1; via tele nitrogen2 Publications1
Binding sitei205SubstrateBy similarity1
Metal bindingi246Zinc 2; via tele nitrogen1 Publication1

GO - Molecular functioni

  • beta-lactamase activity Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • antibiotic catabolic process Source: UniProtKB
  • response to antibiotic Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Antibiotic resistance

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.5.2.6. 5134.
SABIO-RKP52700.

Names & Taxonomyi

Protein namesi
Recommended name:
Metallo-beta-lactamase L1 type 3Curated (EC:3.5.2.61 Publication)
Alternative name(s):
B3 metallo-beta-lactamaseCurated
Beta-lactamase type III1 Publication
Metallo-beta-lactamase L1 type III1 Publication
Penicillinase1 Publication
OrganismiStenotrophomonas maltophilia (Pseudomonas maltophilia) (Xanthomonas maltophilia)
Taxonomic identifieri40324 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeStenotrophomonasStenotrophomonas maltophilia group

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3326.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
PropeptideiPRO_000001694722 – 331 PublicationAdd BLAST12
ChainiPRO_000001694834 – 290Metallo-beta-lactamase L1 type 3Add BLAST257

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi239 ↔ 2671 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homotetramer.3 Publications

Chemistry databases

BindingDBiP52700.

Structurei

Secondary structure

1290
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi36 – 39Combined sources4
Beta strandi45 – 48Combined sources4
Beta strandi51 – 53Combined sources3
Beta strandi55 – 59Combined sources5
Beta strandi62 – 66Combined sources5
Beta strandi69 – 73Combined sources5
Helixi78 – 80Combined sources3
Helixi81 – 90Combined sources10
Helixi95 – 97Combined sources3
Beta strandi98 – 102Combined sources5
Turni108 – 110Combined sources3
Helixi114 – 120Combined sources7
Beta strandi124 – 127Combined sources4
Helixi129 – 136Combined sources8
Turni137 – 139Combined sources3
Turni143 – 145Combined sources3
Turni147 – 149Combined sources3
Beta strandi157 – 159Combined sources3
Beta strandi165 – 168Combined sources4
Beta strandi171 – 177Combined sources7
Beta strandi180 – 182Combined sources3
Beta strandi186 – 194Combined sources9
Beta strandi197 – 203Combined sources7
Helixi223 – 235Combined sources13
Beta strandi240 – 243Combined sources4
Helixi247 – 250Combined sources4
Helixi254 – 259Combined sources6
Turni260 – 263Combined sources4
Helixi267 – 287Combined sources21

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SMLX-ray1.70A22-290[»]
2AIOX-ray1.70A22-290[»]
2FM6X-ray1.75A/B22-290[»]
2FU6X-ray2.05A/B22-290[»]
2FU7X-ray1.85A/B22-290[»]
2FU8X-ray1.80A/B22-290[»]
2FU9X-ray1.80A/B22-290[»]
2GFJX-ray1.80A/B22-290[»]
2GFKX-ray1.90A/B22-290[»]
2H6AX-ray1.80A/B22-290[»]
2HB9X-ray1.75A22-290[»]
2QDTX-ray2.00A22-290[»]
2QINX-ray1.76A/B/C/D22-290[»]
2QJSX-ray2.25A/B/C/D22-290[»]
5EVBX-ray1.84A22-290[»]
5EVDX-ray1.80A22-290[»]
5EVKX-ray1.63A22-290[»]
ProteinModelPortaliP52700.
SMRiP52700.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52700.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
InterProiIPR001018. Beta-lactamase_class-B_CS.
IPR001279. Metallo-B-lactamas.
[Graphical view]
PfamiPF00753. Lactamase_B. 1 hit.
[Graphical view]
SMARTiSM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMiSSF56281. SSF56281. 1 hit.
PROSITEiPS00743. BETA_LACTAMASE_B_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P52700-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSTLLAFAL AVALPAAHTS AAEVPLPQLR AYTVDASWLQ PMAPLQIADH
60 70 80 90 100
TWQIGTEDLT ALLVQTPDGA VLLDGGMPQM ASHLLDNMKA RGVTPRDLRL
110 120 130 140 150
ILLSHAHADH AGPVAELKRR TGAKVAANAE SAVLLARGGS DDLHFGDGIT
160 170 180 190 200
YPPANADRIV MDGEVITVGG IVFTAHFMAG HTPGSTAWTW TDTRNGKPVR
210 220 230 240 250
IAYADSLSAP GYQLQGNPRY PHLIEDYRRS FATVRALPCD VLLTPHPGAS
260 270 280 290
NWDYAAGARA GAKALTCKAY ADAAEQKFDG QLAKETAGAR
Length:290
Mass (Da):30,801
Last modified:October 1, 1996 - v1
Checksum:i0B34CAB54518BC1E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti36 – 37AS → QR AA sequence (PubMed:3931629).Curated2
Sequence conflicti40Q → A AA sequence (PubMed:3931629).Curated1
Sequence conflicti56 – 58TED → RQH AA sequence (PubMed:3931629).Curated3
Sequence conflicti63L → H AA sequence (PubMed:3931629).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75074 Genomic DNA. Translation: CAA52968.1.
PIRiS45349.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75074 Genomic DNA. Translation: CAA52968.1.
PIRiS45349.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1SMLX-ray1.70A22-290[»]
2AIOX-ray1.70A22-290[»]
2FM6X-ray1.75A/B22-290[»]
2FU6X-ray2.05A/B22-290[»]
2FU7X-ray1.85A/B22-290[»]
2FU8X-ray1.80A/B22-290[»]
2FU9X-ray1.80A/B22-290[»]
2GFJX-ray1.80A/B22-290[»]
2GFKX-ray1.90A/B22-290[»]
2H6AX-ray1.80A/B22-290[»]
2HB9X-ray1.75A22-290[»]
2QDTX-ray2.00A22-290[»]
2QINX-ray1.76A/B/C/D22-290[»]
2QJSX-ray2.25A/B/C/D22-290[»]
5EVBX-ray1.84A22-290[»]
5EVDX-ray1.80A22-290[»]
5EVKX-ray1.63A22-290[»]
ProteinModelPortaliP52700.
SMRiP52700.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiP52700.
ChEMBLiCHEMBL3326.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.5.2.6. 5134.
SABIO-RKP52700.

Miscellaneous databases

EvolutionaryTraceiP52700.

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
InterProiIPR001018. Beta-lactamase_class-B_CS.
IPR001279. Metallo-B-lactamas.
[Graphical view]
PfamiPF00753. Lactamase_B. 1 hit.
[Graphical view]
SMARTiSM00849. Lactamase_B. 1 hit.
[Graphical view]
SUPFAMiSSF56281. SSF56281. 1 hit.
PROSITEiPS00743. BETA_LACTAMASE_B_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBLA1_STEMA
AccessioniPrimary (citable) accession number: P52700
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 2, 2016
This is version 99 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.