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P52700

- BLA1_STEMA

UniProt

P52700 - BLA1_STEMA

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Protein

Metallo-beta-lactamase L1

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

Functioni

Has a high activity against imipenem.

Catalytic activityi

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

Cofactori

Zn2+Note: Binds 2 Zn(2+) ions per subunit.

Enzyme regulationi

Inhibited by Hg2+ or Cu2+. Reduced enzymatic activity in presence of Cobalt, Nickel, Cadmium, and Manganese.

pH dependencei

Unstable below pH 8, unless zinc is present.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi105 – 1051Zinc 1
Metal bindingi107 – 1071Zinc 1
Metal bindingi109 – 1091Zinc 2
Metal bindingi181 – 1811Zinc 1
Metal bindingi205 – 2051Zinc 2
Metal bindingi217 – 2171Zinc 2

GO - Molecular functioni

  1. beta-lactamase activity Source: UniProtKB-EC
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. antibiotic catabolic process Source: InterPro
  2. 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

SABIO-RKP52700.

Names & Taxonomyi

Protein namesi
Recommended name:
Metallo-beta-lactamase L1 (EC:3.5.2.6)
Alternative name(s):
Beta-lactamase type II
Penicillinase
OrganismiStenotrophomonas maltophilia (Pseudomonas maltophilia) (Xanthomonas maltophilia)
Taxonomic identifieri40324 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeStenotrophomonasStenotrophomonas maltophilia group

Subcellular locationi

Periplasm Curated

GO - Cellular componenti

  1. periplasmic space Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Propeptidei22 – 33121 PublicationPRO_0000016947Add
BLAST
Chaini34 – 290257Metallo-beta-lactamase L1PRO_0000016948Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi239 ↔ 267

Keywords - PTMi

Disulfide bond

Interactioni

Subunit structurei

Homotetramer.

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[»]
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.
InterProiIPR001279. Beta-lactamas-like.
IPR001018. Beta-lactamase_class-B_CS.
[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 .
PIRi S45349.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1SML X-ray 1.70 A 22-290 [» ]
2AIO X-ray 1.70 A 22-290 [» ]
2FM6 X-ray 1.75 A/B 22-290 [» ]
2FU6 X-ray 2.05 A/B 22-290 [» ]
2FU7 X-ray 1.85 A/B 22-290 [» ]
2FU8 X-ray 1.80 A/B 22-290 [» ]
2FU9 X-ray 1.80 A/B 22-290 [» ]
2GFJ X-ray 1.80 A/B 22-290 [» ]
2GFK X-ray 1.90 A/B 22-290 [» ]
2H6A X-ray 1.80 A/B 22-290 [» ]
2HB9 X-ray 1.75 A 22-290 [» ]
2QDT X-ray 2.00 A 22-290 [» ]
2QIN X-ray 1.76 A/B/C/D 22-290 [» ]
2QJS X-ray 2.25 A/B/C/D 22-290 [» ]
ProteinModelPortali P52700.
SMRi P52700. Positions 23-288.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P52700.
ChEMBLi CHEMBL3326.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

SABIO-RK P52700.

Miscellaneous databases

EvolutionaryTracei P52700.

Family and domain databases

Gene3Di 3.60.15.10. 1 hit.
InterProi IPR001279. Beta-lactamas-like.
IPR001018. Beta-lactamase_class-B_CS.
[Graphical view ]
Pfami PF00753. Lactamase_B. 1 hit.
[Graphical view ]
SMARTi SM00849. Lactamase_B. 1 hit.
[Graphical view ]
SUPFAMi SSF56281. SSF56281. 1 hit.
PROSITEi PS00743. BETA_LACTAMASE_B_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Sequence analysis of the L1 metallo-beta-lactamase from Xanthomonas maltophilia."
    Walsh T.R., Hall L., Assinder S.J., Nichols W.W., Cartwright S.J., Macgowan A.P., Bennett P.M.
    Biochim. Biophys. Acta 1218:199-201(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: IID 1275.
  2. "The production and molecular properties of the zinc beta-lactamase of Pseudomonas maltophilia IID 1275."
    Bicknell R., Emanuel E.L., Gagnon J., Waley S.G.
    Biochem. J. 229:791-797(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 34-65.
    Strain: IID 1275.
  3. "The crystal structure of the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia at 1.7 A resolution."
    Ullah J.H., Walsh T.R., Taylor I.A., Emery D.C., Verma C.S., Gamblin S.J., Spencer J.
    J. Mol. Biol. 284:125-136(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).

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 26, 2014
This is version 90 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