P39070 (CLPQ_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP-dependent protease subunit ClpQ
EC=3.4.21.-

Gene names

Name:	clpQ
Synonyms:	codW, hslV
Ordered Locus Names:	BSU16150

Organism

Bacillus subtilis

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	181 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Protease subunit of a proteasome-like degradation complex. Ref.4
Subunit structure	A double ring-shaped homohexamer of ClpQ is capped on each side by a ring-shaped ClpY homohexamer. The assembly of the ClpQ/ClpY complex is dependent on binding of ATP By similarity.
Subcellular location	Cytoplasm By similarity HAMAP MF_00248.
Sequence similarities	Belongs to the peptidase T1B family. HslV subfamily.
Mass spectrometry	Molecular mass is 19345.7 Da from positions 2 - 181. Ref.4

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	Metal-binding Sodium
Molecular function	Hydrolase Protease Serine protease
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	proteolysis involved in cellular protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	HslUV protease complex Inferred from electronic annotation. Source: InterPro proteasome core complex Inferred from electronic annotation. Source: InterPro
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW serine-type peptidase activity Inferred from electronic annotation. Source: UniProtKB-KW threonine-type endopeptidase 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

Initiator methionine

1

1

Removed Ref.4

Chain

2 – 181

180

ATP-dependent protease subunit ClpQ HAMAP MF_00248

PRO_0000026678

Sites

Active site

2

1

Metal binding

165

1

Sodium; via carbonyl oxygen

Metal binding

168

1

Sodium; via carbonyl oxygen

Metal binding

171

1

Sodium; via carbonyl oxygen

Experimental info

Mutagenesis

2

1

S → A or T: Complete loss of protease activity. Ref.4

Mutagenesis

6

1

A → G: No effect. Ref.4

Mutagenesis

7

1

T → A: Complete loss of protease activity. The mutant is only found as a monomer; when associated with A-8. Ref.4

Mutagenesis

8

1

T → A: Complete loss of protease activity. The mutant is only found as a monomer; when associated with A-7. Ref.4

Sequence conflict

2 – 5

4

Missing in CAA83919. Ref.2

Sequence conflict

60

1

A → R in CAA83919. Ref.2

Sequence conflict

72

1

E → K in CAA83919. Ref.2

Secondary structure

1

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181

Helix Strand Turn

Details...

Beta strand

9 – 14

6

Beta strand

17 – 22

6

Beta strand

26 – 28

3

Turn

29 – 31

3

Beta strand

32 – 36

5

Beta strand

41 – 44

4

Turn

45 – 48

4

Beta strand

49 – 53

5

Helix

57 – 73

17

Turn

74 – 76

3

Helix

78 – 91

14

Beta strand

93 – 95

3

Beta strand

102 – 108

7

Beta strand

110 – 113

4

Beta strand

125 – 130

6

Helix

133 – 147

15

Turn

148 – 150

3

Helix

153 – 167

15

Beta strand

176 – 180

5

Sequences

	Sequence		Length	Mass (Da)
	P39070 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 95DC72474A41A97D	FASTA	181	19,478
	10 20 30 40 50 60 MSSFHATTIF AVQHKGRSAM SGDGQVTFGQ AVVMKHTARK VRKLFNGKVL AGFAGSVADA 70 80 90 100 110 120 FTLFEKFEAK LEEYNGNLKR AAVELAKEWR SDKVLRKLEA MLIVMNQDTL LLVSGTGEVI 130 140 150 160 170 180 EPDDGILAIG SGGNYALAAG RALKKHAGES MSASEIARAA LETAGEICVY TNDQIILEEL E

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A gene required for nutritional repression of the Bacillus subtilis dipeptide permease operon." Slack F.J., Serror P., Joyce E., Sonenshein A.L. Mol. Microbiol. 15:689-702(1995) [PubMed: 7783641] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / JH642.
[2]	Walther T., Hofemeister J. Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: PY143.
[3]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[4]	"The ATP-dependent CodWX (HslVU) protease in Bacillus subtilis is an N-terminal serine protease." Kang M.S., Lim B.K., Seong I.S., Seol J.H., Tanahashi N., Tanaka K., Chung C.H. EMBO J. 20:734-742(2001) [PubMed: 11179218] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-8, CATALYTIC ACTIVITY, FUNCTION AS A SERINE PROTEASE, MUTAGENESIS OF SER-2; ALA-6; THR-7 AND THR-8, MASS SPECTROMETRY.
[5]	"Correction of X-ray intensities from an HslV-HslU co-crystal containing lattice-translocation defects." Wang J., Rho S.H., Park H.H., Eom S.H. Acta Crystallogr. D 61:932-941(2005) [PubMed: 15983416] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (4.16 ANGSTROMS) IN COMPLEX WITH E.COLI HSLU AND ADP.
[6]	"Crystal structure of Bacillus subtilis CodW, a noncanonical HslV-like peptidase with an impaired catalytic apparatus." Rho S.H., Park H.H., Kang G.B., Im Y.J., Kang M.S., Lim B.K., Seong I.S., Seol J., Chung C.H., Wang J., Eom S.H. Proteins 71:1020-1026(2008) [PubMed: 17979190] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-181 IN COMPLEX WITH SODIUM IONS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U13634 Genomic DNA. Translation: AAB03370.1.
Z33639 Genomic DNA. Translation: CAA83919.1.
AL009126 Genomic DNA. Translation: CAB13488.1.

PIR

S61494.

RefSeq

NP_389497.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YYF	X-ray	4.16	C/D	1-181	[»]
2Z3A	X-ray	3.00	A/B/C/D/E/F/G/H/I/J/K/L	2-181	[»]
2Z3B	X-ray	2.50	A/B/C/D/E/F/G/H/I/J/K/L	2-181	[»]

ProteinModelPortal

P39070.

SMR

P39070. Positions 2-181.

ModBase

Search...

Protein family/group databases

MEROPS

T01.007.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBBACT00000002715; EBBACP00000002715; EBBACG00000002710.

GeneID

938111.

GenomeReviews

Gene locus BSU16150 in contig AL009126_GR.

KEGG

bsu:BSU16150.

NMPDR

fig|224308.1.peg.1617.

PATRIC

18975035. VBIBacSub10457_1709.

Organism-specific databases

GenoList

BSU16150. [Micado]

Phylogenomic databases

GeneTree

EBGT00050000002074.

HOGENOM

HBG288822.

OMA

WRTDKYL.

PhylomeDB

P39070.

ProtClustDB

PRK05456.

Enzyme and pathway databases

BioCyc

BSUB:BSU16150-MONOMER.

Family and domain databases

HAMAP

MF_00248. HslV. Divergent sequence.
[Tree]

InterPro

IPR022281. ATP-dep_Prtase_HsIV_su.
IPR001353. Proteasome_sua/b.
[Graphical view]

KO

K01419.

PANTHER

PTHR11599:SF38. PTHR11599:SF38. 1 hit.

Pfam

PF00227. Proteasome. 1 hit.
[Graphical view]

TIGRFAMs

TIGR03692. ATP_dep_HslV. 1 hit.

ProtoNet

Search...

Entry information

Entry name

CLPQ_BACSU

Accession

Primary (citable) accession number: P39070

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	January 25, 2012
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program