Q9JYQ8 (CLPB_NEIMB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chaperone protein ClpB

Gene names

Name:	clpB
Ordered Locus Names:	NMB1472

Organism

Neisseria meningitidis serogroup B (strain MC58) [Reference proteome] [HAMAP]

Taxonomic identifier

122586 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria › Neisseria meningitidis › Neisseria meningitidis serogroup B

Protein attributes

Sequence length	859 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK By similarity.
Subunit structure	Homohexamer. The oligomerization is ATP-dependent By similarity.
Subcellular location	Cytoplasm Probable.
Domain	The N-terminal domain probably functions as a substrate-discriminating domain, recruiting aggregated proteins to the ClpB hexamer and/or stabilizing bound proteins. The NBD2 domain is responsible for oligomerization, whereas the NBD1 domain stabilizes the hexamer probably in an ATP-dependent manner. The movement of the coiled-coil domain is essential for ClpB ability to rescue proteins from an aggregated state, probably by pulling apart large aggregated proteins, which are bound between the coiled-coils motifs of adjacent ClpB subunits in the functional hexamer By similarity.
Sequence similarities	Belongs to the clpA/clpB family.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Cytoplasm
Domain	Coiled coil Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chaperone
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein processing Inferred from electronic annotation. Source: InterPro response to heat Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW nucleoside-triphosphatase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 859	859	Chaperone protein ClpB		PRO_0000191148
Regions
	Nucleotide binding	206 – 213	8	ATP 1 By similarity
	Nucleotide binding	609 – 616	8	ATP 2 By similarity
	Region	1 – 143	143	N-terminal By similarity
	Region	159 – 340	182	NBD1 By similarity
	Region	341 – 549	209	Linker By similarity
	Region	559 – 768	210	NBD2 By similarity
	Region	769 – 859	91	C-terminal By similarity
	Coiled coil	391 – 525	135	By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9JYQ8 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 80B00D0E7CD119E8	FASTA	859	95,195
	10 20 30 40 50 60 MRYDKLTAKF QQALAEAQSL ALAADGSYLE AGFVLKALLD DQNSGAAALL AHAGVNVPQV 70 80 90 100 110 120 KQRLQQHLNS LPKVSGQGGD ILPSRELQAV LNLMDKAATK RSDAYIASEL FLLALVQQND 130 140 150 160 170 180 ATGKILKEAG ATEQNINAAI DAVRGGQNVN DANAEDQRDA LKKYTLDLTQ RARDGKLDPV 190 200 210 220 230 240 IGRDDEIRRA IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPE SLRNKRLLVL 250 260 270 280 290 300 DLAALIAGAK YRGEFEERLK GVLNDLAKDD GNTLIFIDEI HTLVGAGKTD GAMDAGNMLK 310 320 330 340 350 360 PALARGELHC IGATTLDEYR QYIEKDAALE RRFQKVLVGE PSVEDTIAIL RGLQERYEIH 370 380 390 400 410 420 HGIDITDPAI VAAAELSDRY ITDRFLPDKA IDLIDEAASR VKMEKETKPE AMDKIDRRLI 430 440 450 460 470 480 QLRMEKAHVE KEKDDASKKR LELIDEEING LQKEYADLDE IWKAEKAISD GAANIKKQID 490 500 510 520 530 540 EVKIKIEQAK RQGDLALASK LMYEDLEHLE KQRAAAERAD TDSTKPANKL LRNNVGAEEI 550 560 570 580 590 600 AEVVSRMTGI PVSKMMEGER DKLLKMEEVL HRRVVGQDEA VRAVSDAIRR SRSGLADPNK 610 620 630 640 650 660 PYGSFLFLGP TGVGKTELCK ALAGFLFDSE DHLIRIDMSE YMEKHAVARL IGAPPGYVGY 670 680 690 700 710 720 EEGGYLTEQV RRKPYSVILL DEVEKAHPDV FNILLQVLDD GRLTDGQGRT VDFKNTVIVM 730 740 750 760 770 780 TSNIGSQHIQ QMGIQDYEAV KEVVMEDVKE HFRPEMINRI DEVVVFHGLD QDNIRNIAKI 790 800 810 820 830 840 QLKGLEKRLE KQNLRLAVSD AALDIIAKAG FDPIYGARPL KRAIQSEIEN PLAKALLAGN 850 YAPESEIRVE ADGDRLKFA

References

[1]

"Complete genome sequence of Neisseria meningitidis serogroup B strain MC58." Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H., Salzberg S.L., White O. , Fleischmann R.D., Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C. Science 287:1809-1815(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MC58.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE002098 Genomic DNA. Translation: AAF41829.1.
PIR	F81078.
RefSeq	NP_274481.1. NC_003112.2.
3D structure databases
ProteinModelPortal	Q9JYQ8.
SMR	Q9JYQ8. Positions 160-351.
ModBase	Search...
Protein-protein interaction databases
STRING	122586.NMB1472.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAF41829; AAF41829; NMB1472.
GeneID	903894.
KEGG	nme:NMB1472.
PATRIC	20358709. VBINeiMen85645_1864.
Phylogenomic databases
eggNOG	COG0542.
HOGENOM	HOG000218211.
KO	K03695.
OMA	RAGLHSH.
ProtClustDB	CLSK878077.
Enzyme and pathway databases
BioCyc	NMEN122586:GHGG-1512-MONOMER.
Family and domain databases
Gene3D	1.10.1780.10. 1 hit.
InterPro	IPR003593. AAA+_ATPase. IPR013093. ATPase_AAA-2. IPR003959. ATPase_AAA_core. IPR018368. Chaperonin_ClpA/B_CS. IPR017730. Chaperonin_ClpB. IPR001270. Chaprnin_ClpA/B. IPR019489. Clp_ATPase_C. IPR004176. Clp_N. IPR023150. Dbl_Clp-N. IPR027417. P-loop_NTPase. [Graphical view]
Pfam	PF00004. AAA. 1 hit. PF07724. AAA_2. 1 hit. PF02861. Clp_N. 2 hits. PF10431. ClpB_D2-small. 1 hit. [Graphical view]
PRINTS	PR00300. CLPPROTEASEA.
SMART	SM00382. AAA. 2 hits. SM01086. ClpB_D2-small. 1 hit. [Graphical view]
SUPFAM	SSF52540. SSF52540. 2 hits.
TIGRFAMs	TIGR03346. chaperone_ClpB. 1 hit.
PROSITE	PS00870. CLPAB_1. 1 hit. PS00871. CLPAB_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CLPB_NEIMB

Accession

Primary (citable) accession number: Q9JYQ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 1, 2000
Last modified:	May 29, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program