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A5U493

- BLAC_MYCTA

UniProt

A5U493 - BLAC_MYCTA

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Protein

Beta-lactamase

Gene

blaC

Organism
Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Extended spectrum beta-lactamase (ESBL) that inactivates beta-lactam antibiotics by hydrolyzing the amide group of the beta-lactam ring. Exhibits predominant penicillinase activity. Also displays high levels of 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.By similarity1 Publication

Catalytic activityi

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

Enzyme regulationi

Is inhibited by clavulanate, sulbactam and m-aminophenylboronate but not by EDTA.1 Publication

Kineticsi

kcat is 21 sec(-1) with benzylpenicillin as substrate. kcat is 20 sec(-1) with phenoxymethylpenicillin as substrate. kcat is 2 sec(-1) with amoxicillin as substrate. kcat is 55 sec(-1) with azlocillin as substrate. kcat is 31 sec(-1) with nitrocefin as substrate. kcat is 8 sec(-1) with cephaloridine as substrate. kcat is 8 sec(-1) with cefazolin as substrate. kcat is 8 sec(-1) with cephalothin as substrate. kcat is 3 sec(-1) with cephapirin as substrate. kcat is 22 sec(-1) with cefamandole as substrate. Assays performed at pH 6.0.1 Publication

  1. KM=50 µM for benzylpenicillin (at pH 6.0)1 Publication
  2. KM=38 µM for phenoxymethylpenicillin (at pH 6.0)1 Publication
  3. KM=94 µM for amoxicillin (at pH 6.0)1 Publication
  4. KM=185 µM for azlocillin (at pH 6.0)1 Publication
  5. KM=81 µM for nitrocefin (at pH 6.0)1 Publication
  6. KM=798 µM for cephaloridine (at pH 6.0)1 Publication
  7. KM=490 µM for cefazolin (at pH 6.0)1 Publication
  8. KM=308 µM for cephalothin (at pH 6.0)1 Publication
  9. KM=680 µM for cephapirin (at pH 6.0)1 Publication
  10. KM=645 µM for cefamandole (at pH 6.0)1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei84 – 841Acyl-ester intermediateBy similarity
Sitei87 – 871Increases nucleophilicity of active site SerBy similarity
Sitei117 – 1171Functions as a gatekeeper residue that regulates substrate accessibility to the enzyme active siteBy similarity
Binding sitei142 – 1421SubstrateBy similarity
Active sitei182 – 1821Proton acceptorBy similarity

GO - Molecular functioni

  1. beta-lactamase activity Source: UniProtKB-EC

GO - Biological processi

  1. beta-lactam antibiotic catabolic process Source: InterPro
  2. response to antibiotic Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Antibiotic resistance

Enzyme and pathway databases

BioCyciMTUB419947:GJ8N-2149-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-lactamase1 Publication (EC:3.5.2.61 Publication)
Alternative name(s):
Ambler class A beta-lactamase1 Publication
Gene namesi
Name:blaC
Synonyms:blaA1 Publication
Ordered Locus Names:MRA_2082
OrganismiMycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
Taxonomic identifieri419947 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
ProteomesiUP000001988: Chromosome

Subcellular locationi

Periplasm By similarity. Secreted 1 Publication

GO - Cellular componenti

  1. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Periplasm, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3434Tat-type signalPROSITE-ProRule annotationAdd
BLAST
Chaini35 – 307273Beta-lactamasePRO_0000300061Add
BLAST

Post-translational modificationi

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

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

STRINGi419947.MRA_2082.

Structurei

3D structure databases

ProteinModelPortaliA5U493.
SMRiA5U493. Positions 43-307.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiA5U493.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni251 – 2533Substrate bindingBy similarity

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2367.
HOGENOMiHOG000201073.
KOiK17836.
OMAiMKLIGGP.
OrthoDBiEOG6K9QFS.

Family and domain databases

Gene3Di3.40.710.10. 1 hit.
InterProiIPR012338. Beta-lactam/transpept-like.
IPR000871. Beta-lactam_class-A/D.
IPR023650. Beta-lactam_class-A_AS.
[Graphical view]
PRINTSiPR00118. BLACTAMASEA.
SUPFAMiSSF56601. SSF56601. 1 hit.
PROSITEiPS00146. BETA_LACTAMASE_A. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

A5U493-1 [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:July 10, 2007 - v1
Checksum:i448CB2A0E05F4315
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U67924 Genomic DNA. Translation: AAB07556.1.
CP000611 Genomic DNA. Translation: ABQ73843.1.
RefSeqiYP_001283405.1. NC_009525.1.

Genome annotation databases

EnsemblBacteriaiABQ73843; ABQ73843; MRA_2082.
GeneIDi5212563.
KEGGimra:MRA_2082.
PATRICi18144269. VBIMycTub106795_2337.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U67924 Genomic DNA. Translation: AAB07556.1 .
CP000611 Genomic DNA. Translation: ABQ73843.1 .
RefSeqi YP_001283405.1. NC_009525.1.

3D structure databases

ProteinModelPortali A5U493.
SMRi A5U493. Positions 43-307.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 419947.MRA_2082.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABQ73843 ; ABQ73843 ; MRA_2082 .
GeneIDi 5212563.
KEGGi mra:MRA_2082.
PATRICi 18144269. VBIMycTub106795_2337.

Phylogenomic databases

eggNOGi COG2367.
HOGENOMi HOG000201073.
KOi K17836.
OMAi MKLIGGP.
OrthoDBi EOG6K9QFS.

Enzyme and pathway databases

BioCyci MTUB419947:GJ8N-2149-MONOMER.

Miscellaneous databases

EvolutionaryTracei A5U493.

Family and domain databases

Gene3Di 3.40.710.10. 1 hit.
InterProi IPR012338. Beta-lactam/transpept-like.
IPR000871. Beta-lactam_class-A/D.
IPR023650. Beta-lactam_class-A_AS.
[Graphical view ]
PRINTSi PR00118. BLACTAMASEA.
SUPFAMi SSF56601. SSF56601. 1 hit.
PROSITEi PS00146. BETA_LACTAMASE_A. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequence analysis of a class A beta-lactamase from Mycobacterium tuberculosis H37Ra."
    Hackbarth C.J., Unsal I., Chambers H.F.
    Antimicrob. Agents Chemother. 41:1182-1185(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 25177 / H37Ra.
  2. "Complete genomic sequence of Mycobacterium tuberculosis strain H37Ra, a non-pathogenic variant closely related to the well-characterized pathogenic strain H37Rv."
    Wang S.Y., Zheng H.J., Lv L.D., Wang B.F., Zhang X.L., Pu S.Y., Zhu G.F., Wang H.H., Zhao G.P., Zhang Y.
    Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25177 / H37Ra.
  3. "Recombinant expression and characterization of the major beta-lactamase of Mycobacterium tuberculosis."
    Voladri R.K., Lakey D.L., Hennigan S.H., Menzies B.E., Edwards K.M., Kernodle D.S.
    Antimicrob. Agents Chemother. 42:1375-1381(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBCELLULAR LOCATION.
    Strain: ATCC 25177 / H37Ra.

Entry informationi

Entry nameiBLAC_MYCTA
AccessioniPrimary (citable) accession number: A5U493
Secondary accession number(s): P0A5I6, Q10670
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: July 10, 2007
Last modified: October 29, 2014
This is version 51 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

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3