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P71586 (PBPA_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Penicillin-binding protein A
Short name=PBPA
Gene names
Name:pbpA
Ordered Locus Names:Rv0016c, MT0019
ORF Names:MTCY10H4.16c
OrganismMycobacterium tuberculosis
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length491 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cell wall formation. Plays an important role in cell division and cell shape maintenance by cross-linking adjacent peptidoglycan chains through transpeptidation.

Pathway

Cell wall biogenesis; peptidoglycan biosynthesis.

Subcellular location

Cell membrane; Single-pass type II membrane protein Probable. Note: Localized to the division site (septum) along with newly synthesized peptidoglycan, between segregated nucleoids. Ref.3

Post-translational modification

Phosphorylation of Thr-437 may play an important role in regulating cell division, perhaps by targeting PBPA to the septum. Dephosphorylated by pstP. Ref.3

Sequence similarities

Belongs to the transpeptidase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 491491Penicillin-binding protein A
PRO_0000343832

Regions

Topological domain1 – 77Cytoplasmic Potential
Transmembrane8 – 2821Helical; Signal-anchor for type II membrane protein; Potential
Topological domain29 – 491463Extracellular Potential
Region160 – 484325Transpeptidase

Sites

Active site2221Acyl-ester intermediate By similarity

Amino acid modifications

Modified residue3621Phosphothreonine; by pknB Ref.3
Modified residue4371Phosphothreonine; by pknB Ref.3

Experimental info

Mutagenesis3621T → A: Reduced phosphorylation level. Abolish phosphorylation; when associated with A-437. Ref.3
Mutagenesis4371T → A: Reduced phosphorylation level. Lack of septum formation, which is restored in the complemented strain. Abolish phosphorylation; when associated with A-362. Ref.3

Secondary structure

1 ..................................................................... 491
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P71586 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 888DBA26BE251581

FASTA49151,576
        10         20         30         40         50         60 
MNASLRRISV TVMALIVLLL LNATMTQVFT ADGLRADPRN QRVLLDEYSR QRGQITAGGQ 

        70         80         90        100        110        120 
LLAYSVATDG RFRFLRVYPN PEVYAPVTGF YSLRYSSTAL ERAEDPILNG SDRRLFGRRL 

       130        140        150        160        170        180 
ADFFTGRDPR GGNVDTTINP RIQQAGWDAM QQGCYGPCKG AVVALEPSTG KILALVSSPS 

       190        200        210        220        230        240 
YDPNLLASHN PEVQAQAWQR LGDNPASPLT NRAISETYPP GSTFKVITTA AALAAGATET 

       250        260        270        280        290        300 
EQLTAAPTIP LPGSTAQLEN YGGAPCGDEP TVSLREAFVK SCNTAFVQLG IRTGADALRS 

       310        320        330        340        350        360 
MARAFGLDSP PRPTPLQVAE STVGPIPDSA ALGMTSIGQK DVALTPLANA EIAATIANGG 

       370        380        390        400        410        420 
ITMRPYLVGS LKGPDLANIS TTVGYQQRRA VSPQVAAKLT ELMVGAEKVA QQKGAIPGVQ 

       430        440        450        460        470        480 
IASKTGTAEH GTDPRHTPPH AWYIAFAPAQ APKVAVAVLV ENGADRLSAT GGALAAPIGR 

       490 
AVIEAALQGE P

« Hide

References

« Hide 'large scale' references
[1]"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence."
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. expand/collapse author list , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.
Nature 393:537-544(1998) [PubMed: 9634230] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[2]"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains."
Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. expand/collapse author list , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.
J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDC 1551 / Oshkosh.
[3]"The serine/threonine kinase PknB of Mycobacterium tuberculosis phosphorylates PBPA, a penicillin-binding protein required for cell division."
Dasgupta A., Datta P., Kundu M., Basu J.
Microbiology 152:493-504(2006) [PubMed: 16436437] [Abstract]
Cited for: PENICILLIN BINDING, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-362 AND THR-437, MUTAGENESIS OF THR-362 AND THR-437.
Strain: ATCC 25618 / H37Rv.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000516 Genomic DNA. Translation: AAK44241.1.
BX842572 Genomic DNA. Translation: CAB02436.1.
PIRF70699.
RefSeqNP_214530.1. NC_000962.2.
NP_334427.1. NC_002755.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3LO7X-ray2.05A/B35-491[»]
ProteinModelPortalP71586.
ModBaseSearch...

PTM databases

PhosSiteP71586.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000003488; EBMYCP00000003488; EBMYCG00000003486.
EBMYCT00000072473; EBMYCP00000070532; EBMYCG00000072468.
GeneID887078.
922467.
GenomeReviewsGene locus MT0019 in contig AE000516_GR.
Gene locus Rv0016c in contig AL123456_GR.
KEGGmtc:MT0019.
mtu:Rv0016c.
PATRIC18121768. VBIMycTub22151_0020.
TIGRMT0019.

Organism-specific databases

TubercuListRv0016c.

Phylogenomic databases

GeneTreeEBGT00050000015310.
HOGENOMHBG403509.
OMAGATENDQ.
PhylomeDBP71586.
ProtClustDBCLSK790194.

Family and domain databases

InterProIPR012338. Beta-lactam/transpept-like.
IPR001460. PCN-bd_Tpept.
[Graphical view]
Gene3DG3DSA:3.40.710.10. G3DSA:3.40.710.10. 1 hit.
KOK05364.
PfamPF00905. Transpeptidase. 1 hit.
[Graphical view]
SUPFAMSSF56601. PBP_transp_fold. 1 hit.
ProtoNetSearch...

Entry information

Entry namePBPA_MYCTU
AccessionPrimary (citable) accession number: P71586
Secondary accession number(s): Q7DAK5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: February 1, 1997
Last modified: January 25, 2012
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents