P39793 · PBPA_BACSU
- ProteinPenicillin-binding protein 1A/1B
- GeneponA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids914 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits) (Probable). Required for vegetative growth (Probable). Has a partially redundant function with PBP-2A (pbpA) during spore outgrowth (PubMed:9851991).
Catalytic activity
- [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H+
[GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate RHEA-COMP:9602 + CHEBI:60033 = [GlcNAc-(1→4)-Mur2Ac(oyl-L-Ala-γ-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate RHEA-COMP:9603 + CHEBI:58405 + CHEBI:15378
Pathway
Cell wall biogenesis; peptidoglycan biosynthesis.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 115 | Proton donor; for transglycosylase activity | ||||
Sequence: E | ||||||
Active site | 390 | Acyl-ester intermediate; for transpeptidase activity | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | penicillin binding | |
Molecular Function | peptidoglycan glycosyltransferase activity | |
Molecular Function | serine-type D-Ala-D-Ala carboxypeptidase activity | |
Biological Process | cell wall organization | |
Biological Process | peptidoglycan biosynthetic process | |
Biological Process | proteolysis | |
Biological Process | regulation of cell shape | |
Biological Process | response to antibiotic |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePenicillin-binding protein 1A/1B
- Short namesPBP1
Including 2 domains:
- Recommended namePenicillin-insensitive transglycosylase
- EC number
- Alternative names
- Recommended namePenicillin-sensitive transpeptidase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Bacillaceae > Bacillus
Accessions
- Primary accessionP39793
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type II membrane protein
Forespore inner membrane ; Single-pass type II membrane protein
Note: Probably found all over the whole cell at low concentrations. Also localizes to the division site in vegetative cells.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-37 | Cytoplasmic | ||||
Sequence: MSDQFNSREARRKANSKSSPSPKKGKKRKKGGLFKKT | ||||||
Transmembrane | 38-58 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: LFTLLILFVLGVVGGAVTFAV | ||||||
Topological domain | 59-914 | Extracellular | ||||
Sequence: MVSDAPSLDESKLKTPYSSTIYDKNGKEIAEVGAEKRTYVSIDEIPDVVKEAFIATEDARFYEHHGIDPVRIGGALVANFKDGFGAEGGSTITQQVVKNSLLSHQKTLKRKVQEVWLSIQLERNYSKDEILEMYLNRIYFSPRAYGIGKAAEEFFGVTDLSKLTVEQAATLAGMPQSPTAYNPVKNPDKAEKRRNIVLSLMKKQGFISDSQYNKAKKVAVKDEGVVSQKEYEKASTNKYSAFVEEVMKEIDEKSDVDPSADGLKIYTTLDTKAQDKLDELMDGDTVGFTEGMQGGVTLLDTKNGEVRAIGAGRNQPVGGFNYATQTKAQPGSTIKPILDYGPVIENKKWSTYEQIDDSAYTYSNGKPIRDWDRKYLGPISMRYALAQSRNIPALKAFQAVGKDTAVDFANGLGLGLTKDNVTEAYSIGGFGGNDGVSPLTMAGAYSAFGNNGTYNEPHFVKSIEFNDGTKLDLTPKSKSAMSDYTAFMITDMLKTAVKTGTGQLAQVPGVEVAGKTGTTNFDDNEVKRYNIASGGARDSWFVGYTPQYTAAVWTGMGENEAGKKSLSAEEQKVAKRIFAQLIADVDDGSGSFEKPDSVVEATVEKGSNPAKLAGPNTPSDKKLTEYFVKGTAPSTVSKTYEKEEKEETAKLSGLNVKYDKDNQSLTLSWNYDGDATFAVKQSVDGGSYSEIQNSSAKEAVISGVQPGSVYKFEVTAVSDDGKSTASTSYEVPKAEDDEDKKDQQQTDDEKQDDEKTQDDTQTDDSQKDDGQTDQDQTDDSTNDQDKKQDNTNTNPSDNNNQDQSNDNDNDNSNNQDTSDGDSNSGKNDSTGSDTNKNKTDTSNKTQTNSSSIEKTN |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Cells require increased levels of Mg2+ or Ca2+ for growth and germination. Approximately 50% of cells without the gene contain abnormal FtsZ rings, suggesting it is involved in septum synthesis; increased levels of Mg2+ or Ca2+ only partially eliminate the septation defects (PubMed:9721295).
Double ponA-pbpA deletions spores have greatly decreased viability, peptidoglycan synthesis and elongate poorly; increased levels of Mg2+ increase spore viability (PubMed:9851991).
Double ponA-pbpA deletions spores have greatly decreased viability, peptidoglycan synthesis and elongate poorly; increased levels of Mg2+ increase spore viability (PubMed:9851991).
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000083179 | 1-914 | Penicillin-binding protein 1A/1B | |||
Sequence: MSDQFNSREARRKANSKSSPSPKKGKKRKKGGLFKKTLFTLLILFVLGVVGGAVTFAVMVSDAPSLDESKLKTPYSSTIYDKNGKEIAEVGAEKRTYVSIDEIPDVVKEAFIATEDARFYEHHGIDPVRIGGALVANFKDGFGAEGGSTITQQVVKNSLLSHQKTLKRKVQEVWLSIQLERNYSKDEILEMYLNRIYFSPRAYGIGKAAEEFFGVTDLSKLTVEQAATLAGMPQSPTAYNPVKNPDKAEKRRNIVLSLMKKQGFISDSQYNKAKKVAVKDEGVVSQKEYEKASTNKYSAFVEEVMKEIDEKSDVDPSADGLKIYTTLDTKAQDKLDELMDGDTVGFTEGMQGGVTLLDTKNGEVRAIGAGRNQPVGGFNYATQTKAQPGSTIKPILDYGPVIENKKWSTYEQIDDSAYTYSNGKPIRDWDRKYLGPISMRYALAQSRNIPALKAFQAVGKDTAVDFANGLGLGLTKDNVTEAYSIGGFGGNDGVSPLTMAGAYSAFGNNGTYNEPHFVKSIEFNDGTKLDLTPKSKSAMSDYTAFMITDMLKTAVKTGTGQLAQVPGVEVAGKTGTTNFDDNEVKRYNIASGGARDSWFVGYTPQYTAAVWTGMGENEAGKKSLSAEEQKVAKRIFAQLIADVDDGSGSFEKPDSVVEATVEKGSNPAKLAGPNTPSDKKLTEYFVKGTAPSTVSKTYEKEEKEETAKLSGLNVKYDKDNQSLTLSWNYDGDATFAVKQSVDGGSYSEIQNSSAKEAVISGVQPGSVYKFEVTAVSDDGKSTASTSYEVPKAEDDEDKKDQQQTDDEKQDDEKTQDDTQTDDSQKDDGQTDQDQTDDSTNDQDKKQDNTNTNPSDNNNQDQSNDNDNDNSNNQDTSDGDSNSGKNDSTGSDTNKNKTDTSNKTQTNSSSIEKTN |
Post-translational modification
The product expressed from the translation of the ponA gene appears as two bands on a gel (1A and 1B), but the specific amino acid sequence of each protein is unknown.
The N-terminus is blocked.
Proteomic databases
Expression
Developmental stage
Expression is constant during growth, decreases during sporulation and is induced approximately 15 minutes into spore germination. Present in the inner forespore membrane of the dormant spore (PubMed:3080407).
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-16 | Basic and acidic residues | ||||
Sequence: MSDQFNSREARRKANS | ||||||
Region | 1-29 | Disordered | ||||
Sequence: MSDQFNSREARRKANSKSSPSPKKGKKRK | ||||||
Region | 77-246 | Transglycosylase | ||||
Sequence: STIYDKNGKEIAEVGAEKRTYVSIDEIPDVVKEAFIATEDARFYEHHGIDPVRIGGALVANFKDGFGAEGGSTITQQVVKNSLLSHQKTLKRKVQEVWLSIQLERNYSKDEILEMYLNRIYFSPRAYGIGKAAEEFFGVTDLSKLTVEQAATLAGMPQSPTAYNPVKNPD | ||||||
Region | 329-662 | Transpeptidase | ||||
Sequence: TKAQDKLDELMDGDTVGFTEGMQGGVTLLDTKNGEVRAIGAGRNQPVGGFNYATQTKAQPGSTIKPILDYGPVIENKKWSTYEQIDDSAYTYSNGKPIRDWDRKYLGPISMRYALAQSRNIPALKAFQAVGKDTAVDFANGLGLGLTKDNVTEAYSIGGFGGNDGVSPLTMAGAYSAFGNNGTYNEPHFVKSIEFNDGTKLDLTPKSKSAMSDYTAFMITDMLKTAVKTGTGQLAQVPGVEVAGKTGTTNFDDNEVKRYNIASGGARDSWFVGYTPQYTAAVWTGMGENEAGKKSLSAEEQKVAKRIFAQLIADVDDGSGSFEKPDSVVEATVE | ||||||
Domain | 708-795 | Fibronectin type-III | ||||
Sequence: KLSGLNVKYDKDNQSLTLSWNYDGDATFAVKQSVDGGSYSEIQNSSAKEAVISGVQPGSVYKFEVTAVSDDGKSTASTSYEVPKAEDD | ||||||
Region | 773-914 | Disordered | ||||
Sequence: TAVSDDGKSTASTSYEVPKAEDDEDKKDQQQTDDEKQDDEKTQDDTQTDDSQKDDGQTDQDQTDDSTNDQDKKQDNTNTNPSDNNNQDQSNDNDNDNSNNQDTSDGDSNSGKNDSTGSDTNKNKTDTSNKTQTNSSSIEKTN | ||||||
Compositional bias | 789-844 | Basic and acidic residues | ||||
Sequence: VPKAEDDEDKKDQQQTDDEKQDDEKTQDDTQTDDSQKDDGQTDQDQTDDSTNDQDK | ||||||
Compositional bias | 845-914 | Polar residues | ||||
Sequence: KQDNTNTNPSDNNNQDQSNDNDNDNSNNQDTSDGDSNSGKNDSTGSDTNKNKTDTSNKTQTNSSSIEKTN |
Sequence similarities
In the N-terminal section; belongs to the glycosyltransferase 51 family.
In the C-terminal section; belongs to the transpeptidase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length914
- Mass (Da)99,562
- Last updated1995-02-01 v1
- Checksum6978E33DFE2423E6
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-16 | Basic and acidic residues | ||||
Sequence: MSDQFNSREARRKANS | ||||||
Compositional bias | 789-844 | Basic and acidic residues | ||||
Sequence: VPKAEDDEDKKDQQQTDDEKQDDEKTQDDTQTDDSQKDDGQTDQDQTDDSTNDQDK | ||||||
Compositional bias | 845-914 | Polar residues | ||||
Sequence: KQDNTNTNPSDNNNQDQSNDNDNDNSNNQDTSDGDSNSGKNDSTGSDTNKNKTDTSNKTQTNSSSIEKTN |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U11883 EMBL· GenBank· DDBJ | AAA64947.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L47838 EMBL· GenBank· DDBJ | AAB38459.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL009126 EMBL· GenBank· DDBJ | CAB14148.1 EMBL· GenBank· DDBJ | Genomic DNA |