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ECOLI:FTSI

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) ftsI (synonyms: pbpB)
Protein Name(s) Peptidoglycan synthase FtsI

Penicillin-binding protein 3 PBP-3 Peptidoglycan glycosyltransferase 3

External Links
UniProt P0AD68
EMBL K00137
X55034
U00096
AP009048
S49802
S49875
X55814
PIR A93123
RefSeq NP_414626.1
YP_488389.1
ProteinModelPortal P0AD68
SMR P0AD68
DIP DIP-47950N
IntAct P0AD68
MINT MINT-1031950
STRING 511145.b0084
ChEMBL CHEMBL2354204
DrugBank DB01327
DB01413
DB00267
DB00274
DB01328
DB01329
DB01331
DB00430
DB01416
DB00438
DB01415
DB01332
DB00303
PaxDb P0AD68
PRIDE P0AD68
EnsemblBacteria AAC73195
BAB96652
GeneID 12932643
944799
KEGG ecj:Y75_p0083
eco:b0084
PATRIC 32115273
EchoBASE EB0337
EcoGene EG10341
eggNOG COG0768
HOGENOM HOG000049554
InParanoid P0AD68
KO K03587
OMA NSFLKWR
OrthoDB EOG6N0HHV
PhylomeDB P0AD68
BioCyc EcoCyc:EG10341-MONOMER
ECOL316407:JW0082-MONOMER
MetaCyc:EG10341-MONOMER
UniPathway UPA00219
PRO PR:P0AD68
Proteomes UP000000318
UP000000625
Genevestigator P0AD68
GO GO:0032153
GO:0005887
GO:0031226
GO:0008658
GO:0008955
GO:0007049
GO:0051301
GO:0071555
GO:0009252
GO:0008360
GO:0046677
GO:0042493
Gene3D 3.40.710.10
InterPro IPR012338
IPR005311
IPR001460
Pfam PF03717
PF00905
SUPFAM SSF56519
SSF56601

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0051301

cell division

PMID:12670962[1]

ECO:0000314

P

The yeast-two hybrid system, the in vivo protein-protein interactions of the individual subunits of the ClpYQ protease involved in self-oligomerization, as well as in recognition of specific substrates.

complete

involved_in

GO:0071555

cell wall organization

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10606
PANTHER:PTN000771406

P

Seeded From UniProt

complete

enables

GO:0008658

penicillin binding

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10341
EcoGene:EG10606
PANTHER:PTN000771406

F

Seeded From UniProt

complete

part_of

GO:0005887

integral component of plasma membrane

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10341
EcoGene:EG10606
PANTHER:PTN000771406

C

Seeded From UniProt

complete

involved_in

GO:0051301

cell division

PMID:1103132[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0042493

response to drug

PMID:1103132[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0032153

cell division site

PMID:9603865[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0031226

intrinsic component of plasma membrane

PMID:3881388[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0008955

peptidoglycan glycosyltransferase activity

PMID:6450748[6]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008955

peptidoglycan glycosyltransferase activity

PMID:7030331[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008658

penicillin binding

PMID:1103132[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005887

integral component of plasma membrane

PMID:319999[8]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0009252

peptidoglycan biosynthetic process

PMID:27525505[9]

ECO:0000245

automatically integrated combinatorial evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005887

integral component of plasma membrane

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR037532

C

Seeded From UniProt

complete

enables

GO:0008658

penicillin binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001460
InterPro:IPR005311
InterPro:IPR036138
InterPro:IPR037532

F

Seeded From UniProt

complete

enables

GO:0008955

peptidoglycan glycosyltransferase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR037532

F

Seeded From UniProt

complete

involved_in

GO:0009252

peptidoglycan biosynthetic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR037532

P

Seeded From UniProt

complete

involved_in

GO:0051301

cell division

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR037532

P

Seeded From UniProt

complete

enables

GO:0009002

serine-type D-Ala-D-Ala carboxypeptidase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:3.4.16.4

F

Seeded From UniProt

complete

involved_in

GO:0043093

FtsZ-dependent cytokinesis

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000432218

P

Seeded From UniProt

complete

enables

GO:0009002

serine-type D-Ala-D-Ala carboxypeptidase activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000432218

F

Seeded From UniProt

complete

involved_in

GO:0009252

peptidoglycan biosynthetic process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000432218

P

Seeded From UniProt

complete

part_of

GO:0005887

integral component of plasma membrane

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000432218

C

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

P

Seeded From UniProt

complete

enables

GO:0008233

peptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

F

Seeded From UniProt

complete

involved_in

GO:0008360

regulation of cell shape

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0133

P

Seeded From UniProt

complete

involved_in

GO:0071555

cell wall organization

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0961

P

Seeded From UniProt

complete

involved_in

GO:0051301

cell division

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0132

P

Seeded From UniProt

complete

enables

GO:0004180

carboxypeptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0121

F

Seeded From UniProt

complete

involved_in

GO:0009252

peptidoglycan biosynthetic process

GO_REF:0000037
GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0573
UniPathway:UPA00219

P

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

GO_REF:0000037
GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1003
UniProtKB-KW:KW-0997
UniProtKB-SubCell:SL-0037

C

Seeded From UniProt

complete

involved_in

GO:0007049

cell cycle

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0131

P

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

involved_in

GO:0000917

division septum assembly

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0717

P

Seeded From UniProt

complete

part_of

GO:0016021

integral component of membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0812

C

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Lee, YY et al. (2003) Subunit oligomerization and substrate recognition of the Escherichia coli ClpYQ (HslUV) protease implicated by in vivo protein-protein interactions in the yeast two-hybrid system. J. Bacteriol. 185 2393-401 PubMed GONUTS page
  2. 2.0 2.1 2.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  3. 3.0 3.1 3.2 Spratt, BG (1975) Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12. Proc. Natl. Acad. Sci. U.S.A. 72 2999-3003 PubMed GONUTS page
  4. Wang, L et al. (1998) FtsI and FtsW are localized to the septum in Escherichia coli. J. Bacteriol. 180 2810-6 PubMed GONUTS page
  5. Rodríguez-Tébar, A et al. (1985) Location of some proteins involved in peptidoglycan synthesis and cell division in the inner and outer membranes of Escherichia coli. J. Bacteriol. 161 243-8 PubMed GONUTS page
  6. Botta, GA & Park, JT (1981) Evidence for involvement of penicillin-binding protein 3 in murein synthesis during septation but not during cell elongation. J. Bacteriol. 145 333-40 PubMed GONUTS page
  7. Ishino, F & Matsuhashi, M (1981) Peptidoglycan synthetic enzyme activities of highly purified penicillin-binding protein 3 in Escherichia coli: a septum-forming reaction sequence. Biochem. Biophys. Res. Commun. 101 905-11 PubMed GONUTS page
  8. Spratt, BG (1977) Properties of the penicillin-binding proteins of Escherichia coli K12,. Eur. J. Biochem. 72 341-52 PubMed GONUTS page
  9. Meeske, AJ et al. (2016) SEDS proteins are a widespread family of bacterial cell wall polymerases. Nature 537 634-638 PubMed GONUTS page