MYCTU:CLPX

Species (Taxon ID)	Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv). (83332)
Gene Name(s)	clpX (ECO:0000255 with HAMAP-Rule:MF_00175)
Protein Name(s)	ATP-dependent Clp protease ATP-binding subunit ClpX (ECO:0000255 with HAMAP-Rule:MF_00175)
External Links
UniProt	P9WPB9
EMBL	AL123456
PIR	H70864
RefSeq	NP_216973.1 YP_006515894.1
ProteinModelPortal	P9WPB9
SMR	P9WPB9
GeneID	13319167 888167
KEGG	mtu:Rv2457c mtv:RVBD_2457c
TubercuList	Rv2457c
KO	K03544
OMA	HYKRINT
PhylomeDB	P9WPB9
Proteomes	UP000001584
GO	GO:0005618 GO:0005524 GO:0008270 GO:0040007 GO:0006457
Gene3D	3.40.50.300
HAMAP	MF_00175
InterPro	IPR003593 IPR003959 IPR019489 IPR004487 IPR027417 IPR010603
Pfam	PF07724 PF10431 PF06689
SMART	SM00382 SM01086 SM00994
SUPFAM	SSF52540
TIGRFAMs	TIGR00382

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0051302	regulation of cell division	PMID:20625433	ECO:0000314			P		Figure 2A is a light scatter assay that shows the amount of FtsZ polymerization. FtsZ polymerization is necessary for FtsZ ring formation and cell division. Figure 2A shows that for M. tuberculosis mutant without a function ClpX gene has a higher level of FtsZ polymerization than the wild type strain. This indicates that ClpX inhibits cell division.	complete CACAO 4941
	GO:0032272	negative regulation of protein polymerization	PMID:20625433	ECO:0000314			P		Figure 2 show that ClpX inhibits FtsZ polymerization activity. Ftsz interacts directly with Clpx. And ClpX inhibition of FtsZ assembly is independent of the GTP hydrolysis activity of FtsZ	complete CACAO 6909
	GO:0051301	cell division	PMID:20625433	ECO:0000315			P		Fig 6C	complete CACAO 6910
involved_in	GO:0051301	cell division	PMID:20625433	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032272	negative regulation of protein polymerization	PMID:20625433	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005618	cell wall	PMID:15525680	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0051301	cell division		ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10159 PANTHER:PTN000137358 UniProtKB:P9WPB9	P		Seeded From UniProt	complete
involved_in	GO:0030163	protein catabolic process		ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000137292 UniProtKB:P50866	P		Seeded From UniProt	complete
part_of	GO:0005759	mitochondrial matrix		ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000137292 SGD:S000000431 TAIR:locus:2154257 UniProtKB:O76031	C		Seeded From UniProt	complete
enables	GO:0005524	ATP binding		ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10159 MGI:MGI:1346017 PANTHER:PTN000137292 SGD:S000000431	F		Seeded From UniProt	complete
enables	GO:0004176	ATP-dependent peptidase activity		ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10159 PANTHER:PTN000137292 UniProtKB:O76031	F		Seeded From UniProt	complete
involved_in	GO:0006508	proteolysis	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0004176	P		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR003959 InterPro:IPR004487	F		Seeded From UniProt	complete
involved_in	GO:0006457	protein folding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004487	P		Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR010603	F		Seeded From UniProt	complete
enables	GO:0046983	protein dimerization activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR010603	F		Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR004487	F		Seeded From UniProt	complete
involved_in	GO:0006457	protein folding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000001454	P		Seeded From UniProt	complete
enables	GO:0051082	unfolded protein binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000001454	F		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000001454	F		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F		Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F		Seeded From UniProt	complete
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References

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