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PSYA2:CLPX

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Species (Taxon ID) Psychrobacter arcticus (strain DSM 17307 / 273-4). (259536)
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 Q4FQB8
EMBL CP000082
RefSeq YP_265224.1
ProteinModelPortal Q4FQB8
SMR Q4FQB8
STRING 259536.Psyc_1942
PRIDE Q4FQB8
EnsemblBacteria AAZ19790
GeneID 3515912
KEGG par:Psyc_1942
PATRIC 23058781
eggNOG COG1219
HOGENOM HOG000010093
KO K03544
OMA HYKRINT
OrthoDB EOG625JZK
BioCyc PARC259536:GI3A-1987-MONOMER
Proteomes UP000000546
GO GO:0005524
GO:0008270
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

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

GO:0008270

zinc ion binding

PMID:11278349[1]

ECO:0000315

F

Fig. 1 shows that when you increase the amount of clpX, the amount of zinc increases as well.

complete
CACAO 9567

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

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

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: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: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

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

Notes

References

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

  1. Banecki, B et al. (2001) Structure-function analysis of the zinc-binding region of the Clpx molecular chaperone. J. Biol. Chem. 276 18843-8 PubMed GONUTS page