ECOLI:FTSI

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	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
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Notes

References

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

↑ 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
↑ ^2.0 ^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
↑ ^3.0 ^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
↑ Wang, L et al. (1998) FtsI and FtsW are localized to the septum in Escherichia coli. J. Bacteriol. 180 2810-6 PubMed GONUTS page
↑ 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
↑ 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
↑ 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
↑ Spratt, BG (1977) Properties of the penicillin-binding proteins of Escherichia coli K12,. Eur. J. Biochem. 72 341-52 PubMed GONUTS page
↑ Meeske, AJ et al. (2016) SEDS proteins are a widespread family of bacterial cell wall polymerases. Nature 537 634-638 PubMed GONUTS page

[PMID:12670962-1] 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

[PMID:21873635-2] 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

[PMID:1103132-3] 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

[PMID:9603865-4] Wang, L et al. (1998) FtsI and FtsW are localized to the septum in Escherichia coli. J. Bacteriol. 180 2810-6 PubMed GONUTS page

[PMID:3881388-5] 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

[PMID:6450748-6] 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

[PMID:7030331-7] 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

[PMID:319999-8] Spratt, BG (1977) Properties of the penicillin-binding proteins of Escherichia coli K12,. Eur. J. Biochem. 72 341-52 PubMed GONUTS page

[PMID:27525505-9] Meeske, AJ et al. (2016) SEDS proteins are a widespread family of bacterial cell wall polymerases. Nature 537 634-638 PubMed GONUTS page

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ECOLI:FTSI

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