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P39824 (BLAC_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-lactamase

EC=3.5.2.6
Alternative name(s):
Penicillinase
Gene names
Name:penP
Ordered Locus Names:BSU18800
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length306 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This protein is a beta-lactamase with a substrate specificity for penicillins.

Catalytic activity

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

Subcellular location

Secreted Ref.4.

Sequence similarities

Belongs to the class-A beta-lactamase family.

Ontologies

Keywords
   Biological processAntibiotic resistance
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbeta-lactam antibiotic catabolic process

Inferred from electronic annotation. Source: InterPro

response to antibiotic

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionbeta-lactamase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3636 Ref.4
Chain37 – 306270Beta-lactamase
PRO_0000016975

Regions

Region251 – 2533Substrate binding By similarity

Sites

Active site891Acyl-ester intermediate By similarity

Experimental info

Sequence conflict511K → N in CAA84711. Ref.1
Sequence conflict97 – 993AAV → GGF in CAA84711. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P39824 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 95BE5644B731500E

FASTA30633,446
        10         20         30         40         50         60 
MKLKTKASIK FGICVGLLCL SITGFTPFFN STHAEAKSIE DTNMASCITN KKFVQLEKKF 

        70         80         90        100        110        120 
DARLGVYAID IGSNKTIAYR PNERFAYAST YKVLAAAAVL KKNSIEKLNE VIHYSKDDLV 

       130        140        150        160        170        180 
TYSPITEKHL DTGMSLKEIS EAAIRYSDNT AGNILLQQLG GPKGFEKSLK QIGDHVTKAK 

       190        200        210        220        230        240 
RFETDLNSAI PGDIRDTSTA KALATDLKAF TLDNTLTTDK RMILTDWMRG NATGDELIRA 

       250        260        270        280        290        300 
GAPIGWEVGD KSGAGSYGTR NDIAIVWPPN RAPIVVAILS NRFTKDANYD NALIAEAAKV 


VLNDLK 

« Hide

References

« Hide 'large scale' references
[1]"Identification of penicillinase-encoding genes of Bacillus amyloliquefaciens and Bacillus subtilis."
van Dijl J.M., de Jong A., Nauta A., Venema G., Bron S.
Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / 6GM.
[2]"Sequence analysis of the Bacillus subtilis chromosome region between the terC and odhAB loci cloned in a yeast artificial chromosome."
Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[4]"Proteome analysis of Bacillus subtilis extracellular proteins: a two-dimensional protein electrophoretic study."
Hirose I., Sano K., Shioda I., Kumano M., Nakamura K., Yamane K.
Microbiology 146:65-75(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 37-47, SUBCELLULAR LOCATION.
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z35652 Genomic DNA. Translation: CAA84711.1.
AF027868 Genomic DNA. Translation: AAB84426.1.
AL009126 Genomic DNA. Translation: CAB13772.1.
PIRG69674.
RefSeqNP_389761.1. NC_000964.3.

3D structure databases

ProteinModelPortalP39824.
SMRP39824. Positions 53-305.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU18800.

Proteomic databases

PaxDbP39824.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB13772; CAB13772; BSU18800.
GeneID940129.
KEGGbsu:BSU18800.
PATRIC18975601. VBIBacSub10457_1991.

Organism-specific databases

GenoListBSU18800. [Micado]

Phylogenomic databases

eggNOGCOG2367.
HOGENOMHOG000201073.
KOK17836.
OMAMKLIGGP.
OrthoDBEOG6K9QFS.
PhylomeDBP39824.

Enzyme and pathway databases

BioCycBSUB:BSU18800-MONOMER.

Family and domain databases

Gene3D3.40.710.10. 1 hit.
InterProIPR001466. Beta-lactam-related.
IPR012338. Beta-lactam/transpept-like.
IPR000871. Beta-lactam_class-A/D.
IPR023650. Beta-lactam_class-A_AS.
[Graphical view]
PfamPF00144. Beta-lactamase. 1 hit.
[Graphical view]
PRINTSPR00118. BLACTAMASEA.
SUPFAMSSF56601. SSF56601. 1 hit.
PROSITEPS00146. BETA_LACTAMASE_A. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBLAC_BACSU
AccessionPrimary (citable) accession number: P39824
Secondary accession number(s): O34848
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: May 30, 2000
Last modified: July 9, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList