ECOLI:SEQA

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	seqA (ECO:0000255 with HAMAP-Rule:MF_00908)
Protein Name(s)	Negative modulator of initiation of replication (ECO:0000255 with HAMAP-Rule:MF_00908)
External Links
UniProt	P0AFY8
EMBL	U07651 U00096 AP009048
PIR	A54296
RefSeq	NP_415213.1 YP_488967.1
PDB	1IU3 1J3E 1LRR 1XRX 2CH3 3FMT
PDBsum	1IU3 1J3E 1LRR 1XRX 2CH3 3FMT
ProteinModelPortal	P0AFY8
SMR	P0AFY8
DIP	DIP-48017N
IntAct	P0AFY8
MINT	MINT-1238758
STRING	511145.b0687
PaxDb	P0AFY8
PRIDE	P0AFY8
EnsemblBacteria	AAC73781 BAA35336
GeneID	12932913 945272
KEGG	ecj:Y75_p0666 eco:b0687
PATRIC	32116567
EchoBASE	EB2114
EcoGene	EG12197
eggNOG	COG3057
HOGENOM	HOG000275226
KO	K03645
OMA	MVEHIMQ
OrthoDB	EOG6XSZTV
BioCyc	EcoCyc:EG12197-MONOMER ECOL316407:JW0674-MONOMER
EvolutionaryTrace	P0AFY8
PRO	PR:P0AFY8
Proteomes	UP000000318 UP000000625
Genevestigator	P0AFY8
GO	GO:0005737 GO:0003677 GO:0042802 GO:0032297 GO:0006355
Gene3D	1.10.1220.10 1.20.1380.10
HAMAP	MF_00908
InterPro	IPR013321 IPR005621 IPR010985 IPR026577
Pfam	PF03925
PIRSF	PIRSF019401
SUPFAM	SSF47598 SSF82808

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
enables	GO:0042802	identical protein binding	PMID:24561554^[1]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0AFY8	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:15933720^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0AFY8	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:12379844^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0AFY8	F	Seeded From UniProt	complete
part_of	GO:1990097	SeqA-DNA complex	PMID:7553853^[4]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0090143	nucleoid organization	PMID:10540294^[5]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P22523	P	Seeded From UniProt	complete
involved_in	GO:0051289	protein homotetramerization	PMID:11457824^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0044729	hemi-methylated DNA-binding	PMID:7664748^[7]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0032297	negative regulation of DNA-dependent DNA replication initiation	PMID:8011018^[8]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P03004	P	Seeded From UniProt	complete
involved_in	GO:0032297	negative regulation of DNA-dependent DNA replication initiation	PMID:7891562^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0010385	double-stranded methylated DNA binding	PMID:7553853^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0009314	response to radiation	PMID:27718375^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007062	sister chromatid cohesion	PMID:23990792^[11]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P20083	P	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:18304323^[12]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0003688	DNA replication origin binding	PMID:7664748^[7]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR005621 InterPro:IPR026577 InterPro:IPR036835	F	Seeded From UniProt	complete
involved_in	GO:0006355	regulation of transcription, DNA-templated	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR010985 InterPro:IPR013321	P	Seeded From UniProt	complete
involved_in	GO:0032297	negative regulation of DNA-dependent DNA replication initiation	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR005621	P	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000100339	F	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000100339	C	Seeded From UniProt	complete
involved_in	GO:0032297	negative regulation of DNA-dependent DNA replication initiation	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000100339	P	Seeded From UniProt	complete
involved_in	GO:0008156	negative regulation of DNA replication	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0236	P	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0238	F	Seeded From UniProt	complete
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Notes

References

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

↑ Rajagopala, SV et al. (2014) The binary protein-protein interaction landscape of Escherichia coli. Nat. Biotechnol. 32 285-90 PubMed GONUTS page
↑ Guarné, A et al. (2005) Crystal structure of a SeqA-N filament: implications for DNA replication and chromosome organization. EMBO J. 24 1502-11 PubMed GONUTS page
↑ Guarné, A et al. (2002) Insights into negative modulation of E. coli replication initiation from the structure of SeqA-hemimethylated DNA complex. Nat. Struct. Biol. 9 839-43 PubMed GONUTS page
↑ ^4.0 ^4.1 Slater, S et al. (1995) E. coli SeqA protein binds oriC in two different methyl-modulated reactions appropriate to its roles in DNA replication initiation and origin sequestration. Cell 82 927-36 PubMed GONUTS page
↑ Weitao, T et al. (1999) Mutual suppression of mukB and seqA phenotypes might arise from their opposing influences on the Escherichia coli nucleoid structure. Mol. Microbiol. 34 157-68 PubMed GONUTS page
↑ Lee, H et al. (2001) SeqA protein aggregation is necessary for SeqA function. J. Biol. Chem. 276 34600-6 PubMed GONUTS page
↑ ^7.0 ^7.1 Brendler, T et al. (1995) A protein that binds to the P1 origin core and the oriC 13mer region in a methylation-specific fashion is the product of the host seqA gene. EMBO J. 14 4083-9 PubMed GONUTS page
↑ Lu, M et al. (1994) SeqA: a negative modulator of replication initiation in E. coli. Cell 77 413-26 PubMed GONUTS page
↑ von Freiesleben, U et al. (1994) SeqA limits DnaA activity in replication from oriC in Escherichia coli. Mol. Microbiol. 14 763-72 PubMed GONUTS page
↑ Sargentini, NJ et al. () Screen for genes involved in radiation survival of Escherichia coli and construction of a reference database. Mutat. Res. 793-794 1-14 PubMed GONUTS page
↑ Joshi, MC et al. (2013) Regulation of sister chromosome cohesion by the replication fork tracking protein SeqA. PLoS Genet. 9 e1003673 PubMed GONUTS page
↑ Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page

[PMID:24561554-1] Rajagopala, SV et al. (2014) The binary protein-protein interaction landscape of Escherichia coli. Nat. Biotechnol. 32 285-90 PubMed GONUTS page

[PMID:15933720-2] Guarné, A et al. (2005) Crystal structure of a SeqA-N filament: implications for DNA replication and chromosome organization. EMBO J. 24 1502-11 PubMed GONUTS page

[PMID:12379844-3] Guarné, A et al. (2002) Insights into negative modulation of E. coli replication initiation from the structure of SeqA-hemimethylated DNA complex. Nat. Struct. Biol. 9 839-43 PubMed GONUTS page

[PMID:7553853-4] 4.0 ^4.1 Slater, S et al. (1995) E. coli SeqA protein binds oriC in two different methyl-modulated reactions appropriate to its roles in DNA replication initiation and origin sequestration. Cell 82 927-36 PubMed GONUTS page

[PMID:10540294-5] Weitao, T et al. (1999) Mutual suppression of mukB and seqA phenotypes might arise from their opposing influences on the Escherichia coli nucleoid structure. Mol. Microbiol. 34 157-68 PubMed GONUTS page

[PMID:11457824-6] Lee, H et al. (2001) SeqA protein aggregation is necessary for SeqA function. J. Biol. Chem. 276 34600-6 PubMed GONUTS page

[PMID:7664748-7] 7.0 ^7.1 Brendler, T et al. (1995) A protein that binds to the P1 origin core and the oriC 13mer region in a methylation-specific fashion is the product of the host seqA gene. EMBO J. 14 4083-9 PubMed GONUTS page

[PMID:8011018-8] Lu, M et al. (1994) SeqA: a negative modulator of replication initiation in E. coli. Cell 77 413-26 PubMed GONUTS page

[PMID:7891562-9] von Freiesleben, U et al. (1994) SeqA limits DnaA activity in replication from oriC in Escherichia coli. Mol. Microbiol. 14 763-72 PubMed GONUTS page

[PMID:27718375-10] Sargentini, NJ et al. () Screen for genes involved in radiation survival of Escherichia coli and construction of a reference database. Mutat. Res. 793-794 1-14 PubMed GONUTS page

[PMID:23990792-11] Joshi, MC et al. (2013) Regulation of sister chromosome cohesion by the replication fork tracking protein SeqA. PLoS Genet. 9 e1003673 PubMed GONUTS page

[PMID:18304323-12] Ishihama, Y et al. (2008) Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics 9 102 PubMed GONUTS page

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ECOLI:SEQA

Contents

Annotations

Notes

References

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