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UniProtKB - P02919 (PBPB_ECOLI)

Protein

Penicillin-binding protein 1B

Gene

mrcB

Organism
Escherichia coli (strain K12)
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

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).

Miscellaneous

A third isozyme, Beta, lacking the first 25 N-terminal amino acids of the isoform Alpha and a fourth isozyme, Delta, have been found, but seem to result from the artifactual degradation of the isoform Alpha and isoform Gamma respectively.

<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

  • Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.1 Publication EC:3.4.16.4

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: peptidoglycan biosynthesis

This protein is involved in the pathway peptidoglycan biosynthesis, which is part of Cell wall biogenesis.
View all proteins of this organism that are known to be involved in the pathway peptidoglycan biosynthesis and in Cell wall biogenesis.

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 sitei233Proton donor; for transglycosylase activity1 Publication1
Active sitei510Acyl-ester intermediate; for transpeptidase activity1 Publication1

<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

View the complete GO annotation on QuickGO ...

GO - Biological processi

  • cell wall organization Source: UniProtKB-KW
  • peptidoglycan biosynthetic process Source: EcoCyc
  • regulation of cell shape Source: EcoCyc
  • response to antibiotic Source: EcoCyc
  • response to X-ray Source: EcoCyc
View the complete GO annotation on QuickGO ...

<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 functionCarboxypeptidase, Glycosyltransferase, Hydrolase, Multifunctional enzyme, Protease, Transferase
Biological processAntibiotic resistance, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:EG10605-MONOMER
MetaCyc:EG10605-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.4.1.129 2026

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi
UPA00219

Protein family/group databases

Carbohydrate-Active enZymes

More...CAZyi		GT51 Glycosyltransferase Family 51

<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:
Penicillin-binding protein 1B
Short name:
PBP-1b
Short name:
PBP1b
Alternative name(s):
Murein polymerase
Including the following 2 domains:
Penicillin-insensitive transglycosylase (EC:2.4.1.1292 Publications)
Alternative name(s):
Peptidoglycan TGase
Peptidoglycan glycosyltransferase
Penicillin-sensitive transpeptidase (EC:3.4.16.41 Publication)
Alternative name(s):
DD-transpeptidase
<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:mrcB
Synonyms:pbpF, ponB
Ordered Locus Names:b0149, JW0145
<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>OrganismiEscherichia coli (strain K12)
<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 identifieri83333 [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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<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
  • UP000000318 <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
  • UP000000625 Componenti: Chromosome

Organism-specific databases

Escherichia coli strain K12 genome database

More...EcoGenei		EG10605 mrcB

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 63CytoplasmicCuratedAdd BLAST63
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei64 – 87Helical; Signal-anchor for type II membrane proteinCuratedAdd BLAST24
Topological domaini88 – 844PeriplasmicCuratedAdd BLAST757

GO - Cellular componenti

View the complete GO annotation on QuickGO ...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

<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

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>Mutagenesisi233E → Q: Loss of wild-type glycan chain elongation activity. No complementation in strain defective in PBP-1b. 1 Publication1
Mutagenesisi234D → N: 7-fold decrease in catalytic activity. No complementation in strain defective in PBP-1b. 1 Publication1
Mutagenesisi290E → Q: 11-fold decrease in catalytic activity. Shows complementation activity in strain defective in PBP-1b. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL1814

Drug and drug target database

More...DrugBanki		DB01414 Cefacetrile
DB01327 Cefazolin
DB00274 Cefmetazole
DB01328 Cefonicid
DB01329 Cefoperazone
DB01331 Cefoxitin
DB00430 Cefpiramide
DB00438 Ceftazidime
DB01415 Ceftibuten
DB01332 Ceftizoxime
DB06211 Doripenem
DB00303 Ertapenem
DB01598 Imipenem
DB04570 Latamoxef

<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 describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000121451 – 844Penicillin-binding protein 1BAdd BLAST844

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P02919

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

More...PaxDbi		P02919

PRoteomics IDEntifications database

More...PRIDEi		P02919

<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

Forms a trimeric complex with MipA and MltA. Has also been shown to exist as monomer or homodimer; homodimer of Alpha and Gamma isozymes can be found. Interacts with UvrA, FtsL and FtsN.2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		4260880, 259 interactors

Database of interacting proteins

More...DIPi		DIP-10252N

Protein interaction database and analysis system

More...IntActi		P02919, 15 interactors

STRING: functional protein association networks

More...STRINGi		316385.ECDH10B_0129

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P02919

<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

1844
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
3FWLX-ray3.09A58-804[»]
3VMAX-ray2.16A58-804[»]
5FGZX-ray2.85A58-804[»]
5HL9X-ray2.70A58-804[»]
5HLAX-ray2.36A58-804[»]
5HLBX-ray2.42A58-804[»]
5HLDX-ray2.31A58-804[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P02919

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

More...SMRi		P02919

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P02919

<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>Regioni88 – 250Membrane associationAdd BLAST163
Regioni109 – 200UvrB domain 2 homologAdd BLAST92
Regioni195 – 367TransglycosylaseAdd BLAST173
Regioni444 – 736TranspeptidaseAdd BLAST293

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The UvrB domain 2 homolog region (UB2H domain) is important for interaction with MltA.1 Publication

<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

In the N-terminal section; belongs to the glycosyltransferase 51 family.Curated
In the C-terminal section; belongs to the transpeptidase family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG4105BZ4 Bacteria
COG0744 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000282711

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P02919

KEGG Orthology (KO)

More...KOi		K05365

Database for complete collections of gene phylogenies

More...PhylomeDBi		P02919

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.3810.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR012338 Beta-lactam/transpept-like
IPR001264 Glyco_trans_51
IPR023346 Lysozyme-like_dom_sf
IPR032730 PBP1b_TM
IPR011813 PBP_1b
IPR036950 PBP_transglycosylase
IPR001460 PCN-bd_Tpept
IPR028166 UB2H

Pfam protein domain database

More...Pfami		View protein in Pfam
PF14812 PBP1_TM, 1 hit
PF00912 Transgly, 1 hit
PF00905 Transpeptidase, 1 hit
PF14814 UB2H, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF002799 PBP_1b, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF53955 SSF53955, 1 hit
SSF56601 SSF56601, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR02071 PBP_1b, 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>Sequences (2)i

<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.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative initiation. AlignAdd to basket
Isoform Alpha (identifier: P02919-1) [UniParc]FASTAAdd to basket
Also known as: Long

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MAGNDREPIG RKGKPTRPVK QKVSRRRYED DDDYDDYDDY EDEEPMPRKG 
        60         70         80         90        100
KGKGKGRKPR GKRGWLWLLL KLAIVFAVLI AIYGVYLDQK IRSRIDGKVW 
       110        120        130        140        150
QLPAAVYGRM VNLEPDMTIS KNEMVKLLEA TQYRQVSKMT RPGEFTVQAN 
       160        170        180        190        200
SIEMIRRPFD FPDSKEGQVR ARLTFDGDHL ATIVNMENNR QFGFFRLDPR 
       210        220        230        240        250
LITMISSPNG EQRLFVPRSG FPDLLVDTLL ATEDRHFYEH DGISLYSIGR 
       260        270        280        290        300
AVLANLTAGR TVQGASTLTQ QLVKNLFLSS ERSYWRKANE AYMALIMDAR 
       310        320        330        340        350
YSKDRILELY MNEVYLGQSG DNEIRGFPLA SLYYFGRPVE ELSLDQQALL 
       360        370        380        390        400
VGMVKGASIY NPWRNPKLAL ERRNLVLRLL QQQQIIDQEL YDMLSARPLG 
       410        420        430        440        450
VQPRGGVISP QPAFMQLVRQ ELQAKLGDKV KDLSGVKIFT TFDSVAQDAA 
       460        470        480        490        500
EKAAVEGIPA LKKQRKLSDL ETAIVVVDRF SGEVRAMVGG SEPQFAGYNR 
       510        520        530        540        550
AMQARRSIGS LAKPATYLTA LSQPKIYRLN TWIADAPIAL RQPNGQVWSP 
       560        570        580        590        600
QNDDRRYSES GRVMLVDALT RSMNVPTVNL GMALGLPAVT ETWIKLGVPK 
       610        620        630        640        650
DQLHPVPAML LGALNLTPIE VAQAFQTIAS GGNRAPLSAL RSVIAEDGKV 
       660        670        680        690        700
LYQSFPQAER AVPAQAAYLT LWTMQQVVQR GTGRQLGAKY PNLHLAGKTG 
       710        720        730        740        750
TTNNNVDTWF AGIDGSTVTI TWVGRDNNQP TKLYGASGAM SIYQRYLANQ 
       760        770        780        790        800
TPTPLNLVPP EDIADMGVDY DGNFVCSGGM RILPVWTSDP QSLCQQSEMQ 
       810        820        830        840 
QQPSGNPFDQ SSQPQQQPQQ QPAQQEQKDS DGVAGWIKDM FGSN
Length:844
Mass (Da):94,293
Last modified:July 19, 2003 - v2
<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:iCED0A19FAC73961E
GO
Isoform Gamma (identifier: P02919-2) [UniParc]FASTAAdd to basket
Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     1-45: Missing.

Show »
Length:799
Mass (Da):88,890
Checksum:i2A4869BED79A2530
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence CAA26099 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti103P → A (PubMed:3882429).Curated1
Sequence conflicti103P → A (PubMed:8202364).Curated1
Sequence conflicti754P → PTP (PubMed:8202364).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0187371 – 45Missing in isoform Gamma. CuratedAdd BLAST45

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
X02163 Genomic DNA Translation: CAA26098.1
X02163 Genomic DNA Translation: CAA26099.1 Different initiation.
U00096 Genomic DNA Translation: AAC73260.1
AP009048 Genomic DNA Translation: BAB96725.2

Protein sequence database of the Protein Information Resource

More...PIRi		E64738 ZPECPB

NCBI Reference Sequences

More...RefSeqi		NP_414691.1, NC_000913.3
WP_000918162.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC73260; AAC73260; b0149
BAB96725; BAB96725; BAB96725

Database of genes from NCBI RefSeq genomes

More...GeneIDi		944843

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW0145
eco:b0149

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.2132

Keywords - Coding sequence diversityi

Alternative initiation

<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
X02163 Genomic DNA Translation: CAA26098.1
X02163 Genomic DNA Translation: CAA26099.1 Different initiation.
U00096 Genomic DNA Translation: AAC73260.1
AP009048 Genomic DNA Translation: BAB96725.2
PIRiE64738 ZPECPB
RefSeqiNP_414691.1, NC_000913.3
WP_000918162.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3FWLX-ray3.09A58-804[»]
3VMAX-ray2.16A58-804[»]
5FGZX-ray2.85A58-804[»]
5HL9X-ray2.70A58-804[»]
5HLAX-ray2.36A58-804[»]
5HLBX-ray2.42A58-804[»]
5HLDX-ray2.31A58-804[»]
ProteinModelPortaliP02919
SMRiP02919
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260880, 259 interactors
DIPiDIP-10252N
IntActiP02919, 15 interactors
STRINGi316385.ECDH10B_0129

Chemistry databases

BindingDBiP02919
ChEMBLiCHEMBL1814
DrugBankiDB01414 Cefacetrile
DB01327 Cefazolin
DB00274 Cefmetazole
DB01328 Cefonicid
DB01329 Cefoperazone
DB01331 Cefoxitin
DB00430 Cefpiramide
DB00438 Ceftazidime
DB01415 Ceftibuten
DB01332 Ceftizoxime
DB06211 Doripenem
DB00303 Ertapenem
DB01598 Imipenem
DB04570 Latamoxef

Protein family/group databases

CAZyiGT51 Glycosyltransferase Family 51

Proteomic databases

jPOSTiP02919
PaxDbiP02919
PRIDEiP02919

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73260; AAC73260; b0149
BAB96725; BAB96725; BAB96725
GeneIDi944843
KEGGiecj:JW0145
eco:b0149
PATRICifig|1411691.4.peg.2132

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...EchoBASEi		EB0600
EcoGeneiEG10605 mrcB

Phylogenomic databases

eggNOGiENOG4105BZ4 Bacteria
COG0744 LUCA
HOGENOMiHOG000282711
InParanoidiP02919
KOiK05365
PhylomeDBiP02919

Enzyme and pathway databases

UniPathwayi
UPA00219

BioCyciEcoCyc:EG10605-MONOMER
MetaCyc:EG10605-MONOMER
BRENDAi2.4.1.129 2026

Miscellaneous databases

EvolutionaryTraceiP02919

Protein Ontology

More...PROi		PR:P02919

Family and domain databases

Gene3Di1.10.3810.10, 1 hit
InterProiView protein in InterPro
IPR012338 Beta-lactam/transpept-like
IPR001264 Glyco_trans_51
IPR023346 Lysozyme-like_dom_sf
IPR032730 PBP1b_TM
IPR011813 PBP_1b
IPR036950 PBP_transglycosylase
IPR001460 PCN-bd_Tpept
IPR028166 UB2H
PfamiView protein in Pfam
PF14812 PBP1_TM, 1 hit
PF00912 Transgly, 1 hit
PF00905 Transpeptidase, 1 hit
PF14814 UB2H, 1 hit
PIRSFiPIRSF002799 PBP_1b, 1 hit
SUPFAMiSSF53955 SSF53955, 1 hit
SSF56601 SSF56601, 1 hit
TIGRFAMsiTIGR02071 PBP_1b, 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 nameiPBPB_ECOLI
<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: P02919
Secondary accession number(s): P75664
<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: July 21, 1986
Last sequence update: July 19, 2003
Last modified: January 16, 2019
This is version 197 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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