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Protein

Peptidoglycan D,D-transpeptidase FtsI

Gene

ftsI

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

Essential cell division protein that catalyzes cross-linking of the peptidoglycan cell wall at the division septum (PubMed:1103132, PubMed:6450748, PubMed:9614966, PubMed:3531167, PubMed:7030331). Required for localization of FtsN (PubMed:9282742).6 Publications

Caution

Was originally thought to be a bifunctional enzyme with transglycosylase and transpeptidase activities.1 Publication

<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

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by beta-lactam antibiotics such as penicillin, moenomycin, macarbomycin, furazlocillin and piperacillin. Antibiotics inhibit the activity by binding to the catalytic serine.3 Publications

<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.UniRule annotation1 Publication
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 sitei307Acyl-ester intermediateUniRule annotation1 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

GO - Biological processi

  • cell division Source: EcoliWiki
  • cell wall organization Source: GO_Central
  • division septum assembly Source: UniProtKB-KW
  • FtsZ-dependent cytokinesis Source: UniProtKB-UniRule
  • peptidoglycan biosynthetic process Source: UniProtKB-UniRule
  • regulation of cell shape Source: UniProtKB-KW
  • response to drug Source: EcoliWiki

<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, Hydrolase, Protease
Biological processCell cycle, Cell division, Cell shape, Cell wall biogenesis/degradation, Peptidoglycan synthesis, Septation

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:EG10341-MONOMER
MetaCyc:EG10341-MONOMER

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

More...
UniPathwayi
UPA00219

<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:
Peptidoglycan D,D-transpeptidase FtsIUniRule annotationCurated (EC:3.4.16.4UniRule annotation3 Publications)
Alternative name(s):
Essential cell division protein FtsICurated
Murein transpeptidase1 Publication
Penicillin-binding protein 32 PublicationsUniRule annotation
Short name:
PBP-31 PublicationUniRule annotation
Peptidoglycan synthase FtsICurated
<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:ftsI1 PublicationUniRule annotation
Synonyms:pbpB
Ordered Locus Names:b0084, JW0082
<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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<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
EG10341 ftsI

<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 – 18Cytoplasmic1 PublicationAdd BLAST18
<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>Transmembranei19 – 39HelicalUniRule annotationAdd BLAST21
Topological domaini40 – 577Periplasmic1 PublicationAdd BLAST538

GO - Cellular componenti

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>Mutagenesisi23R → C or H: Impairs septal localization. 1 Publication1
Mutagenesisi39L → P: Impairs septal localization. 1 Publication1
Mutagenesisi46Q → H: Impairs septal localization. 1 Publication1
Mutagenesisi57G → D: Impairs recruitment of FtsN to the septal ring. 1 Publication1
Mutagenesisi61S → F or P: Impairs recruitment of FtsN to the septal ring. 1 Publication1
Mutagenesisi62L → P: Impairs recruitment of FtsN to the septal ring. 1 Publication1
Mutagenesisi210R → C or H: Impairs recruitment of FtsN to the septal ring. 1 Publication1
Mutagenesisi307S → A or T: Unable to bind penicillin. 1 Publication1
Mutagenesisi307S → C: Still able to bind penicillin. 1 Publication1
Mutagenesisi361N → S in PBPBR1; obtained after selection for increased resistance to cephalexin, causes a change in the shape of the cell: The polar caps are pointed. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2354204

Drug and drug target database

More...
DrugBanki
DB01327 Cefazolin
DB01413 Cefepime
DB00267 Cefmenoxime
DB00274 Cefmetazole
DB01328 Cefonicid
DB01329 Cefoperazone
DB01331 Cefoxitin
DB00430 Cefpiramide
DB01416 Cefpodoxime
DB00438 Ceftazidime
DB01415 Ceftibuten
DB01332 Ceftizoxime
DB04918 Ceftobiprole
DB00303 Ertapenem

<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_00000170521 – 577Peptidoglycan D,D-transpeptidase FtsIAdd BLAST577
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000017053578 – 5881 PublicationAdd BLAST11

Proteomic databases

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

More...
PaxDbi
P0AD68

PRoteomics IDEntifications database

More...
PRIDEi
P0AD68

<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

Homodimer (PubMed:20847002). Forms a complex with FtsW (PubMed:20847002). Interacts with FtsQ (PubMed:17185541).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
4261637, 166 interactors

Database of interacting proteins

More...
DIPi
DIP-47950N

Protein interaction database and analysis system

More...
IntActi
P0AD68, 18 interactors

Molecular INTeraction database

More...
MINTi
P0AD68

STRING: functional protein association networks

More...
STRINGi
316385.ECDH10B_0066

<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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P0AD68

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

More...
SMRi
P0AD68

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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

<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

Contains an N-terminal membrane anchor-containing module, a central non-catalytic domain and a C-terminal penicillin-binding (PB) catalytic domain. The transmembrane region is essential for localization to the septal ring, interaction with FtsW and cell septation.4 Publications

<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

Belongs to the transpeptidase family. FtsI subfamily.UniRule annotationCurated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105CJN Bacteria
COG0768 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000049554

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0AD68

KEGG Orthology (KO)

More...
KOi
K03587

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0AD68

Family and domain databases

HAMAP database of protein families

More...
HAMAPi
MF_02080 FtsI_transpept, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR012338 Beta-lactam/transpept-like
IPR037532 FtsI_transpept
IPR005311 PBP_dimer
IPR036138 PBP_dimer_sf
IPR001460 PCN-bd_Tpept

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03717 PBP_dimer, 1 hit
PF00905 Transpeptidase, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56519 SSF56519, 1 hit
SSF56601 SSF56601, 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>Sequencei

<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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P0AD68-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKAAAKTQKP KRQEEHANFI SWRFALLCGC ILLALAFLLG RVAWLQVISP
60 70 80 90 100
DMLVKEGDMR SLRVQQVSTS RGMITDRSGR PLAVSVPVKA IWADPKEVHD
110 120 130 140 150
AGGISVGDRW KALANALNIP LDQLSARINA NPKGRFIYLA RQVNPDMADY
160 170 180 190 200
IKKLKLPGIH LREESRRYYP SGEVTAHLIG FTNVDSQGIE GVEKSFDKWL
210 220 230 240 250
TGQPGERIVR KDRYGRVIED ISSTDSQAAH NLALSIDERL QALVYRELNN
260 270 280 290 300
AVAFNKAESG SAVLVDVNTG EVLAMANSPS YNPNNLSGTP KEAMRNRTIT
310 320 330 340 350
DVFEPGSTVK PMVVMTALQR GVVRENSVLN TIPYRINGHE IKDVARYSEL
360 370 380 390 400
TLTGVLQKSS NVGVSKLALA MPSSALVDTY SRFGLGKATN LGLVGERSGL
410 420 430 440 450
YPQKQRWSDI ERATFSFGYG LMVTPLQLAR VYATIGSYGI YRPLSITKVD
460 470 480 490 500
PPVPGERVFP ESIVRTVVHM MESVALPGGG GVKAAIKGYR IAIKTGTAKK
510 520 530 540 550
VGPDGRYINK YIAYTAGVAP ASQPRFALVV VINDPQAGKY YGGAVSAPVF
560 570 580
GAIMGGVLRT MNIEPDALTT GDKNEFVINQ GEGTGGRS
Length:588
Mass (Da):63,877
Last modified:March 20, 1987 - v1
<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:iC89A403D5980B2CD
GO

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
K00137 Genomic DNA Translation: AAA24300.1
X55034 Genomic DNA Translation: CAA38861.1
U00096 Genomic DNA Translation: AAC73195.1
AP009048 Genomic DNA Translation: BAB96652.1
S49802 Genomic DNA Translation: AAB24312.1
S49875 Genomic DNA Translation: AAB24310.1
X55814 Genomic DNA Translation: CAA39333.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A93123 ZPECP3

NCBI Reference Sequences

More...
RefSeqi
NP_414626.1, NC_000913.3
WP_000642196.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC73195; AAC73195; b0084
BAB96652; BAB96652; BAB96652

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
944799

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW0082
eco:b0084

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.2196

<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
K00137 Genomic DNA Translation: AAA24300.1
X55034 Genomic DNA Translation: CAA38861.1
U00096 Genomic DNA Translation: AAC73195.1
AP009048 Genomic DNA Translation: BAB96652.1
S49802 Genomic DNA Translation: AAB24312.1
S49875 Genomic DNA Translation: AAB24310.1
X55814 Genomic DNA Translation: CAA39333.1
PIRiA93123 ZPECP3
RefSeqiNP_414626.1, NC_000913.3
WP_000642196.1, NZ_LN832404.1

3D structure databases

ProteinModelPortaliP0AD68
SMRiP0AD68
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261637, 166 interactors
DIPiDIP-47950N
IntActiP0AD68, 18 interactors
MINTiP0AD68
STRINGi316385.ECDH10B_0066

Chemistry databases

ChEMBLiCHEMBL2354204
DrugBankiDB01327 Cefazolin
DB01413 Cefepime
DB00267 Cefmenoxime
DB00274 Cefmetazole
DB01328 Cefonicid
DB01329 Cefoperazone
DB01331 Cefoxitin
DB00430 Cefpiramide
DB01416 Cefpodoxime
DB00438 Ceftazidime
DB01415 Ceftibuten
DB01332 Ceftizoxime
DB04918 Ceftobiprole
DB00303 Ertapenem

Proteomic databases

PaxDbiP0AD68
PRIDEiP0AD68

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73195; AAC73195; b0084
BAB96652; BAB96652; BAB96652
GeneIDi944799
KEGGiecj:JW0082
eco:b0084
PATRICifig|1411691.4.peg.2196

Organism-specific databases

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

More...
EchoBASEi
EB0337
EcoGeneiEG10341 ftsI

Phylogenomic databases

eggNOGiENOG4105CJN Bacteria
COG0768 LUCA
HOGENOMiHOG000049554
InParanoidiP0AD68
KOiK03587
PhylomeDBiP0AD68

Enzyme and pathway databases

UniPathwayi
UPA00219

BioCyciEcoCyc:EG10341-MONOMER
MetaCyc:EG10341-MONOMER

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P0AD68

Family and domain databases

HAMAPiMF_02080 FtsI_transpept, 1 hit
InterProiView protein in InterPro
IPR012338 Beta-lactam/transpept-like
IPR037532 FtsI_transpept
IPR005311 PBP_dimer
IPR036138 PBP_dimer_sf
IPR001460 PCN-bd_Tpept
PfamiView protein in Pfam
PF03717 PBP_dimer, 1 hit
PF00905 Transpeptidase, 1 hit
SUPFAMiSSF56519 SSF56519, 1 hit
SSF56601 SSF56601, 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 nameiFTSI_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: P0AD68
Secondary accession number(s): P04286
<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: March 20, 1987
Last sequence update: March 20, 1987
Last modified: December 5, 2018
This is version 118 of the entry and version 1 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

Complete proteome, Reference proteome

Documents

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