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Protein

Beta-lactamase

Gene

blaC

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
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

Extended spectrum beta-lactamase (ESBL) that inactivates beta-lactam antibiotics by hydrolyzing the amide group of the beta-lactam ring. Displays high levels of penicillinase and cephalosporinase activity as well as measurable activity with carbapenems, including imipenem and meropenem. Plays a primary role in the intrinsic resistance of M.tuberculosis to beta-lactam antibiotics.5 Publications

<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 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

Is inhibited by sulbactam, tazobactam, and clavulanate. Sulbactam inhibits the enzyme competitively and reversibly with respect to nitrocefin. Tazobactam inhibits the enzyme in a time-dependent manner, but the activity of the enzyme reappears due to the slow hydrolysis of the covalently acylated enzyme. In contrast, clavulanate reacts with the enzyme quickly to form hydrolytically stable, inactive forms of the enzyme, via irreversible acylation of the catalytic serine residue. Clavulanate has potential to be used in combination with approved beta-lactam antibiotics to treat multi-drug resistant (MDR) and extremely drug resistant (XDR) strains of M.tuberculosis. Is also irreversibly inhibited by NXL104, which forms an extremely stable carbamoyl adduct with the enzyme but shows an inhibition efficiency more than 100-fold lower than that of clavulanate. Is inhibited by carbapenems, that are very poor substrates for the enzyme.5 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 600 min(-1) with ampicillin as substrate. kcat is 340 min(-1) with amoxicillin as substrate. kcat is 560 min(-1) with penicillin G as substrate. kcat is 2100 min(-1) with penicillin V as substrate. kcat is 690 min(-1) with piperacillin as substrate. kcat is 1070 min(-1) with cephalosporin C as substrate. kcat is 490 min(-1) with cephalotin as substrate. kcat is 490 min(-1) with cefuroxime as substrate. kcat is 3500 min(-1) with cefamandole as substrate. kcat is 48 min(-1) with cefoxitin as substrate. kcat is 2.0 min(-1) with ceftazidime as substrate. kcat is 49 min(-1) with ceftriaxone as substrate. kcat is 380 min(-1) with cefotaxime as substrate. kcat is 6680 min(-1) with nitrocefin as substrate. kcat is 1770 min(-1) with CENTA as substrate. kcat is 10 min(-1) with imipenem as substrate. kcat is 0.08 min(-1) with meropenem as substrate. Assays above performed at pH 6.4. kcat is 18.5 sec(-1) with ampicillin as substrate. kcat is 12.1 sec(-1) with cephalotin as substrate. kcat is 1.1 sec(-1) with cefoxitin as substrate. kcat is 0.2 sec(-1) with ceftazidime as substrate. kcat is 0.9 sec(-1) with meropenem as substrate. Assays above performed at pH 7.5. kcat is 0.08 min(-1) with meropenem as substrate at pH 6.5. kcat is 0.016 min(-1) with doripenem as substrate. kcat is 0.017 min(-1) with ertapenem as substrate. kcat is 0.65 min(-1) with faropenem as substrate. Assays above performed at pH 6.5.4 Publications
  1. KM=8 µM for ampicillin (at pH 6.4)1 Publication
  2. KM=22 µM for amoxicillin (at pH 6.4)1 Publication
  3. KM=19 µM for penicillin G (at pH 6.4)1 Publication
  4. KM=69 µM for penicillin V (at pH 6.4)1 Publication
  5. KM=59 µM for piperacillin (at pH 6.4)1 Publication
  6. KM=114 µM for cephalosporin C (at pH 6.4)1 Publication
  7. KM=152 µM for cephalotin (at pH 6.4)1 Publication
  8. KM=5100 µM for cefuroxime (at pH 6.4)1 Publication
  9. KM=184 µM for cefamandole (at pH 6.4)1 Publication
  10. KM=127 µM for cefoxitin (at pH 6.4)1 Publication
  11. KM=280 µM for ceftazidime (at pH 6.4)1 Publication
  12. KM=520 µM for ceftriaxone (at pH 6.4)1 Publication
  13. KM=5570 µM for cefotaxime (at pH 6.4)1 Publication
  14. KM=57 µM for nitrocefin (at pH 6.4)1 Publication
  15. KM=195 µM for CENTA (at pH 6.4)1 Publication
  16. KM=9.4 µM for imipenem (at pH 6.4)1 Publication
  17. KM=3.4 µM for meropenem (at pH 6.4)1 Publication
  18. KM=63 µM for ampicillin (at pH 7.5)1 Publication
  19. KM=117 µM for cephalotin (at pH 7.5)1 Publication
  20. KM=195 µM for cefoxitin (at pH 7.5)1 Publication
  21. KM=593 µM for ceftazidime (at pH 7.5)1 Publication
  22. KM=279 µM for meropenem (at pH 7.5)1 Publication
  23. KM=3.4 µM for meropenem (at pH 6.5)1 Publication
  24. KM=0.18 µM for doripenem (at pH 6.5)1 Publication
  25. KM=0.18 µM for ertapenem (at pH 6.5)1 Publication
  26. KM=55 µM for faropenem (at pH 6.5)1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei84Acyl-ester intermediate3 Publications1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei87Increases nucleophilicity of active site Ser2 Publications1
    Sitei117Functions as a gatekeeper residue that regulates substrate accessibility to the enzyme active site1 Publication1
    <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 sitei142Substrate3 Publications1
    Active sitei182Proton acceptor2 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

    GO - Biological processi

    • beta-lactam antibiotic catabolic process Source: MTBBASE
    • response to antibiotic Source: MTBBASE

    <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

    <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:
    Beta-lactamase1 Publication (EC:3.5.2.64 Publications)
    Alternative name(s):
    Ambler class A beta-lactamase1 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:blaC1 Publication
    Synonyms:blaA
    Ordered Locus Names:Rv2068c
    ORF Names:MTCY49.07c
    <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>OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
    <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 identifieri83332 [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 lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000001584 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

    Organism-specific databases

    Mycobacterium tuberculosis strain H37Rv genome database

    More...
    TubercuListi
    Rv2068c

    <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

    Cell inner membrane, Cell membrane, Membrane, Periplasm, Secreted

    <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

    <p>This subsection of the ‘Pathology and Biotech’ section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

    Can be used as a biomarker, which together with BlaC-specific fluorogenic substrates, allows a rapid and accurate detection of very low numbers of M.tuberculosis for the clinical diagnosis of tuberculosis in sputum and other specimens.2 Publications

    <p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

    Cells lacking this gene become significantly more susceptible (16- to 32-fold) to penicillins as well as third-generation cephalosporins and carbapenems. They have no detectable beta-lactamase activity.1 Publication

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi8 – 9RR → KK: No longer exported via the Tat-system. Loss of cell resistance to beta-lactam antibiotics. 1 Publication2
    Mutagenesisi87K → A: 200000-fold decrease in catalytic efficiency with cefamandole as substrate. 1 Publication1
    Mutagenesisi117I → F: Significant increase in ampicillin resistance. 2-fold and 3-fold increase in catalytic efficiency with ampicillin and nitrocefin as substrate, respectively, mainly due to an increase in substrate affinity. 1 Publication1
    Mutagenesisi142S → G: Significant reduction of catalytic activity for both nitrocefin and ampicillin. Leads to in vitro clavulanate resistance and decreased susceptibility to carbapenem inhibitors, but is still susceptible to ampicillin-clavulanate in vivo. 1 Publication1
    Mutagenesisi182E → A: Loss of catalytic activity with cefamandole as substrate. 1 Publication1
    Mutagenesisi236R → A or S: Significant reduction of catalytic activity for both nitrocefin and ampicillin. Leads to in vitro clavulanate resistance and decreased susceptibility to carbapenem inhibitors, but is still susceptible to ampicillin-clavulanate in vivo. 1 Publication1
    Mutagenesisi253T → A: Significant reduction of catalytic activity for both nitrocefin and ampicillin. Only minor impairment of the inactivation by clavulanate. Larger increase in resistance to carbapenems. 1 Publication1
    Mutagenesisi253T → S: Only minor impairment of catalytic activity with both nitrocefin and ampicillin. Still inhibited by clavulanate and carbapenems. 1 Publication1

    <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 – 34Tat-type signalPROSITE-ProRule annotationAdd BLAST34
    <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_000001700535 – 307Beta-lactamaseAdd BLAST273

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    Exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven.1 Publication

    Proteomic databases

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P9WKD3

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Constitutively expressed.1 Publication

    <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

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    83332.Rv2068c

    <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

    1307
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    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
    2GDNX-ray1.72A41-307[»]
    3CG5X-ray1.70A43-307[»]
    3DWZX-ray1.80A43-307[»]
    3IQAX-ray2.20A43-307[»]
    3M6BX-ray1.30A43-307[»]
    3M6HX-ray1.99A43-307[»]
    3N6IX-ray2.00A43-307[»]
    3N7WX-ray1.70A43-307[»]
    3N8LX-ray1.40A43-307[»]
    3N8RX-ray1.41A43-307[»]
    3N8SX-ray2.00A43-307[»]
    3NBLX-ray2.00A43-307[»]
    3NC8X-ray1.50A43-307[»]
    3NCKX-ray2.80A43-307[»]
    3NDEX-ray1.70A43-307[»]
    3NDGX-ray1.90A43-307[»]
    3NY4X-ray1.22A43-307[»]
    3VFFX-ray2.78A/B/C/D43-307[»]
    3VFHX-ray2.57A/B/C/D43-307[»]
    3ZHHX-ray2.85A/B/C/D32-307[»]
    4DF6X-ray2.29A43-307[»]
    4EBLX-ray2.10A/B/C/D43-307[»]
    4EBNX-ray2.85A/B/C/D43-307[»]
    4EBPX-ray2.29A/B/C/D43-307[»]
    4JLFX-ray2.10A43-307[»]
    4Q8IX-ray1.90A41-307[»]
    4QB8X-ray1.76A42-307[»]
    4QHCX-ray1.90A42-307[»]
    4X6TX-ray1.40A45-307[»]
    5NJ2X-ray1.19A/B43-307[»]
    5OYOX-ray2.10A/B43-307[»]
    6B5XX-ray2.45A/B/C/D41-307[»]
    6B5YX-ray2.75A/B/C/D41-307[»]
    6B68X-ray2.15A/B/C/D41-307[»]
    6B69X-ray2.20A/B/C/D41-307[»]
    6B6AX-ray2.30A/B/C/D41-307[»]
    6B6BX-ray1.80A41-307[»]
    6B6CX-ray1.90A41-307[»]
    6B6DX-ray1.80A41-307[»]
    6B6EX-ray1.90A41-307[»]
    6B6FX-ray2.05A41-307[»]

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P9WKD3

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

    More...
    SMRi
    P9WKD3

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <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

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni251 – 253Substrate binding3 Publications3

    <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

    Belongs to the class-A beta-lactamase family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4108J4B Bacteria
    COG2367 LUCA

    KEGG Orthology (KO)

    More...
    KOi
    K17836

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    EWMKGNA

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P9WKD3

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR012338 Beta-lactam/transpept-like
    IPR000871 Beta-lactam_class-A
    IPR023650 Beta-lactam_class-A_AS

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00118 BLACTAMASEA

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF56601 SSF56601, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00146 BETA_LACTAMASE_A, 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.

    P9WKD3-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MRNRGFGRRE LLVAMAMLVS VTGCARHASG ARPASTTLPA GADLADRFAE
    60 70 80 90 100
    LERRYDARLG VYVPATGTTA AIEYRADERF AFCSTFKAPL VAAVLHQNPL
    110 120 130 140 150
    THLDKLITYT SDDIRSISPV AQQHVQTGMT IGQLCDAAIR YSDGTAANLL
    160 170 180 190 200
    LADLGGPGGG TAAFTGYLRS LGDTVSRLDA EEPELNRDPP GDERDTTTPH
    210 220 230 240 250
    AIALVLQQLV LGNALPPDKR ALLTDWMARN TTGAKRIRAG FPADWKVIDK
    260 270 280 290 300
    TGTGDYGRAN DIAVVWSPTG VPYVVAVMSD RAGGGYDAEP REALLAEAAT

    CVAGVLA
    Length:307
    Mass (Da):32,568
    Last modified:April 16, 2014 - 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:i448CB2A0E05F4315
    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
    AL123456 Genomic DNA Translation: CCP44842.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    G70764

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_216584.1, NC_000962.3
    WP_003410677.1, NZ_NVQJ01000047.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    CCP44842; CCP44842; Rv2068c

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    888742

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    mtu:Rv2068c

    <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
    AL123456 Genomic DNA Translation: CCP44842.1
    PIRiG70764
    RefSeqiNP_216584.1, NC_000962.3
    WP_003410677.1, NZ_NVQJ01000047.1

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2GDNX-ray1.72A41-307[»]
    3CG5X-ray1.70A43-307[»]
    3DWZX-ray1.80A43-307[»]
    3IQAX-ray2.20A43-307[»]
    3M6BX-ray1.30A43-307[»]
    3M6HX-ray1.99A43-307[»]
    3N6IX-ray2.00A43-307[»]
    3N7WX-ray1.70A43-307[»]
    3N8LX-ray1.40A43-307[»]
    3N8RX-ray1.41A43-307[»]
    3N8SX-ray2.00A43-307[»]
    3NBLX-ray2.00A43-307[»]
    3NC8X-ray1.50A43-307[»]
    3NCKX-ray2.80A43-307[»]
    3NDEX-ray1.70A43-307[»]
    3NDGX-ray1.90A43-307[»]
    3NY4X-ray1.22A43-307[»]
    3VFFX-ray2.78A/B/C/D43-307[»]
    3VFHX-ray2.57A/B/C/D43-307[»]
    3ZHHX-ray2.85A/B/C/D32-307[»]
    4DF6X-ray2.29A43-307[»]
    4EBLX-ray2.10A/B/C/D43-307[»]
    4EBNX-ray2.85A/B/C/D43-307[»]
    4EBPX-ray2.29A/B/C/D43-307[»]
    4JLFX-ray2.10A43-307[»]
    4Q8IX-ray1.90A41-307[»]
    4QB8X-ray1.76A42-307[»]
    4QHCX-ray1.90A42-307[»]
    4X6TX-ray1.40A45-307[»]
    5NJ2X-ray1.19A/B43-307[»]
    5OYOX-ray2.10A/B43-307[»]
    6B5XX-ray2.45A/B/C/D41-307[»]
    6B5YX-ray2.75A/B/C/D41-307[»]
    6B68X-ray2.15A/B/C/D41-307[»]
    6B69X-ray2.20A/B/C/D41-307[»]
    6B6AX-ray2.30A/B/C/D41-307[»]
    6B6BX-ray1.80A41-307[»]
    6B6CX-ray1.90A41-307[»]
    6B6DX-ray1.80A41-307[»]
    6B6EX-ray1.90A41-307[»]
    6B6FX-ray2.05A41-307[»]
    ProteinModelPortaliP9WKD3
    SMRiP9WKD3
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi83332.Rv2068c

    Proteomic databases

    PaxDbiP9WKD3

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCCP44842; CCP44842; Rv2068c
    GeneIDi888742
    KEGGimtu:Rv2068c

    Organism-specific databases

    TubercuListiRv2068c

    Phylogenomic databases

    eggNOGiENOG4108J4B Bacteria
    COG2367 LUCA
    KOiK17836
    OMAiEWMKGNA
    PhylomeDBiP9WKD3

    Family and domain databases

    InterProiView protein in InterPro
    IPR012338 Beta-lactam/transpept-like
    IPR000871 Beta-lactam_class-A
    IPR023650 Beta-lactam_class-A_AS
    PRINTSiPR00118 BLACTAMASEA
    SUPFAMiSSF56601 SSF56601, 1 hit
    PROSITEiView protein in PROSITE
    PS00146 BETA_LACTAMASE_A, 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 nameiBLAC_MYCTU
    <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: P9WKD3
    Secondary accession number(s): L0T8I9
    , P0A5I6, P0C5C1, Q10670
    <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: April 16, 2014
    Last sequence update: April 16, 2014
    Last modified: December 5, 2018
    This is version 28 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, Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
      Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
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