Peptidoglycan synthase FtsI precursor - Escherichia coli O157:H7

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P0AD69 (FTSI_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 62. History...

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

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·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:	Z0094, ECs0088

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [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	Inferred from homology

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 By similarity.
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 By similarity. Note: The bulk of the molecule, except for the N-terminal membrane anchor region, protrudes into the periplasmic space, where it acts on murein By similarity.
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) By similarity.
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
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW 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
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	penicillin binding Inferred from electronic annotation. Source: InterPro peptidoglycan glycosyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 577

577

Peptidoglycan synthase FtsI

PRO_0000043363

Propeptide

578 – 588

By similarity

PRO_0000043364

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 By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P0AD69 [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

[1]	"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. Blattner F.R. Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]	"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005174 Genomic DNA. Translation: AAG54388.1. BA000007 Genomic DNA. Translation: BAB33511.1.
PIR	H85490. H90639.
RefSeq	NP_285780.1. NC_002655.2. NP_308115.1. NC_002695.1.
3D structure databases
ProteinModelPortal	P0AD69.
SMR	P0AD69. Positions 67-568.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-1031936.
STRING	155864.Z0094.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAG54388; AAG54388; Z0094. BAB33511; BAB33511; BAB33511.
GeneID	913535. 956770.
KEGG	ece:Z0094. ecs:ECs0088.
PATRIC	18349118. VBIEscCol44059_0089.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0768.
HOGENOM	HOG000049554.
KO	K03587.
OMA	PDGKYIN.
ProtClustDB	PRK15105.
Enzyme and pathway databases
BioCyc	ECOL386585:GJFA-86-MONOMER.
UniPathway	UPA00219.
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...

Entry information

Entry name

FTSI_ECO57

Accession

Primary (citable) accession number: P0AD69
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 62 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents