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Protein

Metallo-beta-lactamase type 2

Gene

blm

Organism
Bacillus cereus
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Confers resistance to the different beta-lactams antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring. Active on cephalosporin and penicillin.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+5 PublicationsNote: Binds 2 Zn2+ ions per subunit. The enzyme can also function with only 1 Zn2+ ion (PubMed:9761898).5 Publications

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by captopril stereoisomers and iodoacetate (PubMed:3930467, PubMed:26482303). Also inhibited by chelating agents such as EDTA (PubMed:3930467).2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi116Zinc 1; via tele nitrogen5 Publications1
Metal bindingi118Zinc 1; via pros nitrogen5 Publications1
Metal bindingi120Zinc 23 Publications1
Metal bindingi179Zinc 1; via tele nitrogen5 Publications1
Metal bindingi198Zinc 23 Publications1
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei201Substrate1 Publication1
Binding sitei210Substrate; via amide nitrogen2 Publications1
Metal bindingi240Zinc 2; via tele nitrogen3 Publications1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

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

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase
Biological processAntibiotic resistance
LigandMetal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.5.2.6 648

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P04190

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Metallo-beta-lactamase type 2Curated (EC:3.5.2.6By similarity)
Alternative name(s):
B2 metallo-beta-lactamaseCurated
Beta-lactamase II1 Publication
Cephalosporinase1 Publication
Metallo-beta-lactamase type II1 Publication
Metallothioprotein beta-lactamase II1 Publication
Penicillinase1 Publication
Zinc-requiring beta-lactamase II1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:blm1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiBacillus cereus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri1396 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Periplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB02153 3-Sulfinoalanine
DB02863 Alpha Chlorophyll A
DB04272 Citric Acid

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 301 PublicationAdd BLAST30
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001694231 – 257Metallo-beta-lactamase type 2Add BLAST227

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.1 Publication

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1257
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P04190

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P04190

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P04190

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.60.15.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001018 Beta-lactamase_class-B_CS
IPR001279 Metallo-B-lactamas
IPR036866 RibonucZ/Hydroxyglut_hydro

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00753 Lactamase_B, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00849 Lactamase_B, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56281 SSF56281, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00743 BETA_LACTAMASE_B_1, 1 hit
PS00744 BETA_LACTAMASE_B_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P04190-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKKNTLLKVG LCVGLLGTIQ FVSTISSVQA SQKVEKTVIK NETGTISISQ
60 70 80 90 100
LNKNVWVHTE LGSFNGEAVP SNGLVLNTSK GLVLVDSSWD DKLTKELIEM
110 120 130 140 150
VEKKFQKRVT DVIITHAHAD RIGGIKTLKE RGIKAHSTAL TAELAKKNGY
160 170 180 190 200
EEPLGDLQTV TNLKFGNMKV ETFYPGKGHT EDNIVVWLPQ YNILVGGCLV
210 220 230 240 250
KSTSAKDLGN VADAYVNEWS TSIENVLKRY RNINAVVPGH GEVGDKGLLL

HTLDLLK
Length:257
Mass (Da):28,092
Last modified:March 20, 1987 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i268EBFB7DDA45431
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M11189 Genomic DNA Translation: AAA22276.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A91806 PNBSU2

NCBI Reference Sequences

More...
RefSeqi
WP_000742468.1, NZ_UFSU01000001.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11189 Genomic DNA Translation: AAA22276.1
PIRiA91806 PNBSU2
RefSeqiWP_000742468.1, NZ_UFSU01000001.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BC2X-ray1.90A/B31-257[»]
1BMCX-ray2.50A37-257[»]
1BVTX-ray1.85A31-257[»]
1DXKX-ray1.85A31-257[»]
1MQOX-ray1.35A31-257[»]
2BC2X-ray1.70A/B31-257[»]
2BFKX-ray2.00A/B31-257[»]
2BFLX-ray1.80A/B31-257[»]
2BFZX-ray2.30A/B31-257[»]
2BG2X-ray2.40A/B31-257[»]
2BG6X-ray2.30A/B31-257[»]
2BG7X-ray2.10A/B31-257[»]
2BG8X-ray2.50A/B31-257[»]
2BGAX-ray2.70A/B31-257[»]
2M5CNMR-A31-257[»]
2M5DNMR-A31-257[»]
2NXAX-ray2.29A37-257[»]
2NYPX-ray1.84A37-257[»]
2NZEX-ray1.80A/B36-257[»]
2NZFX-ray2.28A37-257[»]
2UYXX-ray1.95A30-257[»]
3BC2X-ray1.70A31-257[»]
3FCZX-ray2.80A/B36-247[»]
3I0VX-ray1.60A31-257[»]
3I11X-ray1.45A31-257[»]
3I13X-ray1.74A31-257[»]
3I14X-ray1.55A31-257[»]
3I15X-ray1.55A31-257[»]
3KNRX-ray1.71A/B/C/D31-257[»]
3KNSX-ray1.58A/B/C/D31-257[»]
4C09X-ray1.20A31-257[»]
4C1CX-ray1.18A31-257[»]
4C1HX-ray1.10A31-257[»]
4NQ4X-ray1.67A36-257[»]
4NQ5X-ray2.29A36-257[»]
4NQ6X-ray1.80A36-257[»]
4TYTX-ray1.80A31-257[»]
5FQAX-ray1.10A31-257[»]
5FQBX-ray1.90A31-257[»]
5JMXX-ray1.44A31-257[»]
5W8WX-ray2.25A36-257[»]
6EUMX-ray1.18A31-257[»]
6EWEX-ray1.46A31-257[»]
6F2NX-ray1.15A31-257[»]
ProteinModelPortaliP04190
SMRiP04190
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

DrugBankiDB02153 3-Sulfinoalanine
DB02863 Alpha Chlorophyll A
DB04272 Citric Acid

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.5.2.6 648
SABIO-RKiP04190

Miscellaneous databases

EvolutionaryTraceiP04190

Family and domain databases

Gene3Di3.60.15.10, 1 hit
InterProiView protein in InterPro
IPR001018 Beta-lactamase_class-B_CS
IPR001279 Metallo-B-lactamas
IPR036866 RibonucZ/Hydroxyglut_hydro
PfamiView protein in Pfam
PF00753 Lactamase_B, 1 hit
SMARTiView protein in SMART
SM00849 Lactamase_B, 1 hit
SUPFAMiSSF56281 SSF56281, 1 hit
PROSITEiView protein in PROSITE
PS00743 BETA_LACTAMASE_B_1, 1 hit
PS00744 BETA_LACTAMASE_B_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiBLA2_BACCE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P04190
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: March 20, 1987
Last modified: December 5, 2018
This is version 127 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>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
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