Peptidoglycan synthase FtsI precursor - Escherichia coli (strain K12)

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P0AD68 (FTSI_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 78. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Peptidoglycan synthase FtsI
EC=2.4.1.129

Alternative name(s):
Penicillin-binding protein 3
Short name=PBP-3
Peptidoglycan glycosyltransferase 3

Gene names

Name:	ftsI
Synonyms:	pbpB
Ordered Locus Names:	b0084, JW0082

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	588 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Cell wall formation. Essential for the formation of a septum of the murein sacculus. Synthesis of cross-linked peptidoglycan from the lipid intermediates.
Catalytic activity	(GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n)-diphosphoundecaprenol + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol = (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n+1)-diphosphoundecaprenol + undecaprenyl diphosphate.
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular location	Cell inner membrane; Single-pass membrane protein; Periplasmic side. Note: The bulk of the molecule, except for the N-terminal membrane anchor region, protrudes into the periplasmic space, where it acts on murein.
Domain	Has an N-terminal penicillin insensitive transglycosylase domain (formation of linear glycan strands) and a C-terminal penicillin-sensitive transpeptidase domain (cross-linking of the peptide subunits).
Sequence similarities	Belongs to the transpeptidase family.

Ontologies

Keywords
Biological process	Antibiotic resistance Cell cycle Cell division Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from mutant phenotype PubMed 1103132. Source: EcoliWiki peptidoglycan biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW response to antibiotic Inferred from electronic annotation. Source: UniProtKB-KW response to drug Inferred from mutant phenotype PubMed 1103132. Source: EcoliWiki
Cellular_component	cell division site part Inferred from direct assay PubMed 9603865. Source: EcoliWiki integral to plasma membrane Inferred from direct assay PubMed 319999. Source: EcoliWiki
Molecular_function	penicillin binding Inferred from direct assay PubMed 1103132. Source: EcoliWiki peptidoglycan glycosyltransferase activity Inferred from direct assay PubMed 7030331. Source: EcoliWiki
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
divIB	Q8DQM0	3	EBI-548564,EBI-6446264	From a different organism.
ftsL	P0AEN4	4	EBI-548564,EBI-1119082
ftsN	P29131	3	EBI-548564,EBI-1134233
ftsQ	P06136	5	EBI-548564,EBI-1130157
ftsW	P0ABG4	7	EBI-548564,EBI-1214767
ymgF	P58034	3	EBI-548564,EBI-1214577

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 577

577

Peptidoglycan synthase FtsI

PRO_0000017052

Propeptide

578 – 588

PRO_0000017053

Regions

Topological domain

1 – 18

Cytoplasmic Potential

Transmembrane

19 – 39

Helical; Potential

Topological domain

40 – 577

538

Periplasmic Potential

Sites

Active site

307

Acyl-ester intermediate

Experimental info

Mutagenesis

307

S → A or T: Unable to bind penicillin. Ref.8

Mutagenesis

307

S → C: Still able to bind penicillin. Ref.8

Mutagenesis

361

N → 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. Ref.10

Sequences

Sequence

Length

Mass (Da)

Tools

P0AD68 [UniParc].

Last modified March 20, 1987. Version 1.
Checksum: C89A403D5980B2CD
Show »

FASTA

588

63,877

        10         20         30         40         50         60 
MKAAAKTQKP KRQEEHANFI SWRFALLCGC ILLALAFLLG RVAWLQVISP DMLVKEGDMR 

        70         80         90        100        110        120 
SLRVQQVSTS RGMITDRSGR PLAVSVPVKA IWADPKEVHD AGGISVGDRW KALANALNIP 

       130        140        150        160        170        180 
LDQLSARINA NPKGRFIYLA RQVNPDMADY IKKLKLPGIH LREESRRYYP SGEVTAHLIG 

       190        200        210        220        230        240 
FTNVDSQGIE GVEKSFDKWL TGQPGERIVR KDRYGRVIED ISSTDSQAAH NLALSIDERL 

       250        260        270        280        290        300 
QALVYRELNN AVAFNKAESG SAVLVDVNTG EVLAMANSPS YNPNNLSGTP KEAMRNRTIT 

       310        320        330        340        350        360 
DVFEPGSTVK PMVVMTALQR GVVRENSVLN TIPYRINGHE IKDVARYSEL TLTGVLQKSS 

       370        380        390        400        410        420 
NVGVSKLALA MPSSALVDTY SRFGLGKATN LGLVGERSGL YPQKQRWSDI ERATFSFGYG 

       430        440        450        460        470        480 
LMVTPLQLAR VYATIGSYGI YRPLSITKVD PPVPGERVFP ESIVRTVVHM MESVALPGGG 

       490        500        510        520        530        540 
GVKAAIKGYR IAIKTGTAKK VGPDGRYINK YIAYTAGVAP ASQPRFALVV VINDPQAGKY 

       550        560        570        580 
YGGAVSAPVF GAIMGGVLRT MNIEPDALTT GDKNEFVINQ GEGTGGRS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"On the process of cellular division in Escherichia coli: nucleotide sequence of the gene for penicillin-binding protein 3." Nakamura M., Maruyama I.N., Soma M., Kato J., Suzuki H., Horota Y. Mol. Gen. Genet. 191:1-9(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region." Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A. Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Escherichia coli mraR gene involved in cell growth and division." Ueki M., Wachi M., Jung H.K., Ishino F., Matsuhashi M. J. Bacteriol. 174:7841-7843(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-71. Strain: JE1011.
[6]	"FtsL, an essential cytoplasmic membrane protein involved in cell division in Escherichia coli." Guzman L.-M., Barondess J.J., Beckwith J. J. Bacteriol. 174:7716-7728(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-41.
[7]	"Revised interpretation of the sequence containing the murE gene encoding the UDP-N-acetylmuramyl-tripeptide synthetase of Escherichia coli." Michaud C., Parquet C., Flouret B., Blanot D., van Heijenoort J. Biochem. J. 269:277-278(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 550-588.
[8]	"Binding of penicillin to thiol-penicillin-binding protein 3 of Escherichia coli: identification of its active site." Houba-Herin N., Hara H., Inouye M., Hirota Y. Mol. Gen. Genet. 201:499-504(1985) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF SER-307.
[9]	"Determination of the cleavage site involved in C-terminal processing of penicillin-binding protein 3 of Escherichia coli." Nagasawa H., Sakagami Y., Suzuki A., Suzuki H., Hara H., Hirota Y. J. Bacteriol. 171:5890-5893(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEOLYTIC PROCESSING.
[10]	"An amino acid substitution in penicillin-binding protein 3 creates pointed polar caps in Escherichia coli." Taschner P.E.M., Ypenburg N., Spratt B.G., Woldringh C.L. J. Bacteriol. 170:4828-4837(1988) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF ASN-361.
[11]	"Membrane topology of penicillin-binding protein 3 of Escherichia coli." Bowler L.D., Spratt B.G. Mol. Microbiol. 3:1277-1286(1989) [PubMed] [Europe PMC] [Abstract] Cited for: TOPOLOGY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
PIR	ZPECP3. A93123.
RefSeq	NP_414626.1. NC_000913.2. YP_488389.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P0AD68.
SMR	P0AD68. Positions 67-568.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-47950N.
IntAct	P0AD68. 16 interactions.
STRING	511145.b0084.
Proteomic databases
PaxDb	P0AD68.
PRIDE	P0AD68.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC73195; AAC73195; b0084. BAB96652; BAB96652; BAB96652.
GeneID	12932643. 944799.
KEGG	ecj:Y75_p0083. eco:b0084.
PATRIC	32115273. VBIEscCol129921_0088.
Organism-specific databases
EchoBASE	EB0337.
EcoGene	EG10341. ftsI.
Phylogenomic databases
eggNOG	COG0768.
HOGENOM	HOG000049554.
KO	K03587.
OMA	PDGKYIN.
ProtClustDB	PRK15105.
Enzyme and pathway databases
BioCyc	EcoCyc:EG10341-MONOMER. ECOL316407:JW0082-MONOMER. MetaCyc:EG10341-MONOMER.
UniPathway	UPA00219.
Gene expression databases
Genevestigator	P0AD68.
Family and domain databases
Gene3D	3.40.710.10. 1 hit.
InterPro	IPR012338. Beta-lactam/transpept-like. IPR005311. PBP_dimer. IPR001460. PCN-bd_Tpept. [Graphical view]
Pfam	PF03717. PBP_dimer. 1 hit. PF00905. Transpeptidase. 1 hit. [Graphical view]
SUPFAM	SSF56519. PBP_dimer. 1 hit. SSF56601. PBP_transp_fold. 1 hit.
ProtoNet	Search...
Other
ChEMBL	CHEMBL1799.

Entry information

Entry name

FTSI_ECOLI

Accession

Primary (citable) accession number: P0AD68
Secondary accession number(s): P04286

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 1987
Last sequence update:	March 20, 1987
Last modified:	May 1, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents