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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi105 – 1051Zinc 1; via tele nitrogen2 Publications
Metal bindingi107 – 1071Zinc 1; via pros nitrogen2 Publications
Metal bindingi109 – 1091Zinc 22 Publications
Metal bindingi110 – 1101Zinc 2; via tele nitrogen2 Publications
Metal bindingi181 – 1811Zinc 1; via tele nitrogen2 Publications
Binding sitei205 – 2051SubstrateBy similarity
Metal bindingi246 – 2461Zinc 2; via tele nitrogen1 Publication

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

ChEMBLiCHEMBL3326.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Propeptidei22 – 33121 PublicationPRO_0000016947Add
BLAST
Chaini34 – 290257Metallo-beta-lactamase L1 type 3PRO_0000016948Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi239 ↔ 2671 Publication

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homotetramer.3 Publications

Chemistry

BindingDBiP52700.

Structurei

Secondary structure

1
290
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi36 – 394Combined sources
Beta strandi45 – 484Combined sources
Beta strandi51 – 533Combined sources
Beta strandi55 – 595Combined sources
Beta strandi62 – 665Combined sources
Beta strandi69 – 735Combined sources
Helixi78 – 803Combined sources
Helixi81 – 9010Combined sources
Helixi95 – 973Combined sources
Beta strandi98 – 1025Combined sources
Helixi108 – 1114Combined sources
Helixi114 – 1207Combined sources
Beta strandi124 – 1274Combined sources
Helixi129 – 1368Combined sources
Turni137 – 1393Combined sources
Turni143 – 1453Combined sources
Turni147 – 1493Combined sources
Beta strandi157 – 1593Combined sources
Beta strandi165 – 1684Combined sources
Beta strandi171 – 1777Combined sources
Beta strandi180 – 1823Combined sources
Beta strandi186 – 1949Combined sources
Beta strandi197 – 2037Combined sources
Helixi223 – 23513Combined sources
Beta strandi240 – 2434Combined sources
Helixi247 – 2504Combined sources
Helixi254 – 2596Combined sources
Turni260 – 2634Combined sources
Helixi267 – 28721Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 23-288.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti36 – 372AS → QR AA sequence (PubMed:3931629).Curated
Sequence conflicti40 – 401Q → A AA sequence (PubMed:3931629).Curated
Sequence conflicti56 – 583TED → RQH AA sequence (PubMed:3931629).Curated
Sequence conflicti63 – 631L → H AA sequence (PubMed:3931629).Curated

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
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. Positions 23-288.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

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: September 7, 2016
This is version 97 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.