P25144 (CCPA_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Catabolite control protein A

Alternative name(s):
Glucose-resistance amylase regulator

Gene names

Name:	ccpA
Synonyms:	alsA, amyR, graR
Ordered Locus Names:	BSU29740

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

Protein attributes

Sequence length	334 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Global transcriptional regulator of carbon catabolite repression (CCR) and carbon catabolite activation (CCA), which ensures optimal energy usage under diverse conditions. Interacts with either P-Ser-HPr or P-Ser-Crh, leading to the formation of a complex that binds to DNA at the catabolite-response elements (cre). Binding to DNA allows activation or repression of many different genes and operons. Ref.1 Ref.4 Ref.5 Ref.6 Ref.9
Subunit structure	Homodimer. Interacts with P-Ser-HPr and P-Ser-Crh. Ref.4
Sequence similarities	Contains 1 HTH lacI-type DNA-binding domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Ligand	DNA-binding
Molecular function	Activator Repressor
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	intracellular Inferred from electronic annotation. Source: InterPro
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW sequence-specific DNA binding transcription factor 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 – 334

334

Catabolite control protein A

PRO_0000107925

Regions

Domain

1 – 58

58

HTH lacI-type

DNA binding

6 – 25

20

H-T-H motif By similarity

Secondary structure

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334

Helix Strand Turn

Details...

Helix

6 – 13

8

Helix

17 – 25

9

Helix

32 – 45

14

Helix

51 – 58

8

Beta strand

63 – 69

7

Helix

74 – 89

16

Beta strand

93 – 98

6

Helix

103 – 115

13

Beta strand

119 – 123

5

Helix

130 – 138

9

Beta strand

139 – 141

3

Beta strand

143 – 147

5

Beta strand

157 – 159

3

Helix

162 – 175

14

Beta strand

179 – 186

8

Beta strand

188 – 190

3

Helix

191 – 194

4

Helix

197 – 207

11

Helix

214 – 216

3

Beta strand

217 – 219

3

Helix

224 – 234

11

Beta strand

237 – 239

3

Beta strand

242 – 248

7

Helix

249 – 261

13

Turn

266 – 269

4

Beta strand

271 – 276

6

Helix

279 – 281

3

Beta strand

283 – 286

4

Beta strand

289 – 292

4

Helix

295 – 310

16

Beta strand

318 – 321

4

Beta strand

325 – 327

3

Sequences

	Sequence		Length	Mass (Da)
	P25144 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: 62AD6CA7294E1FAA	FASTA	334	36,940
	10 20 30 40 50 60 MSNITIYDVA REANVSMATV SRVVNGNPNV KPTTRKKVLE AIERLGYRPN AVARGLASKK 70 80 90 100 110 120 TTTVGVIIPD ISSIFYSELA RGIEDIATMY KYNIILSNSD QNMEKELHLL NTMLGKQVDG 130 140 150 160 170 180 IVFMGGNITD EHVAEFKRSP VPIVLAASVE EQEETPSVAI DYEQAIYDAV KLLVDKGHTD 190 200 210 220 230 240 IAFVSGPMAE PINRSKKLQG YKRALEEANL PFNEQFVAEG DYTYDSGLEA LQHLMSLDKK 250 260 270 280 290 300 PTAILSATDE MALGIIHAAQ DQGLSIPEDL DIIGFDNTRL SLMVRPQLST VVQPTYDIGA 310 320 330 VAMRLLTKLM NKEPVEEHIV ELPHRIELRK STKS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Catabolite repression of alpha-amylase gene expression in Bacillus subtilis involves a trans-acting gene product homologous to the Escherichia coli lacl and galR repressors." Henkin T.M., Grundy F.J., Nicholson W.L., Chambliss G.H. Mol. Microbiol. 5:575-584(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]	"Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region." Lapidus A., Galleron N., Sorokin A., Ehrlich S.D. Microbiology 143:3431-3441(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[4]	"Specificity of DNA binding activity of the Bacillus subtilis catabolite control protein CcpA." Kim J.H., Guvener Z.T., Cho J.Y., Chung K.C., Chambliss G.H. J. Bacteriol. 177:5129-5134(1995) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DNA-BINDING, SUBUNIT.
[5]	"Role of CcpA in regulation of the central pathways of carbon catabolism in Bacillus subtilis." Tobisch S., Zuhlke D., Bernhardt J., Stulke J., Hecker M. J. Bacteriol. 181:6996-7004(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"The Bacillus subtilis catabolite control protein CcpA exerts all its regulatory functions by DNA-binding." Ludwig H., Stulke J. FEMS Microbiol. Lett. 203:125-129(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION. Strain: 168.
[7]	"Phosphoprotein Crh-Ser46-P displays altered binding to CcpA to effect carbon catabolite regulation." Schumacher M.A., Seidel G., Hillen W., Brennan R.G. J. Biol. Chem. 281:6793-6800(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.98 ANGSTROMS) OF 5-333 IN COMPLEX WITH P-SER-CRH.
[8]	"Structural analysis of B. subtilis CcpA effector binding site." Chaptal V., Gueguen-Chaignon V., Poncet S., Lecampion C., Meyer P., Deutscher J., Galinier A., Nessler S., Morera S. Proteins 64:814-816(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 58-334 IN COMPLEX WITH P-SER-HPR.
[9]	"Structures of carbon catabolite protein A-(HPr-Ser46-P) bound to diverse catabolite response element sites reveal the basis for high-affinity binding to degenerate DNA operators." Schumacher M.A., Sprehe M., Bartholomae M., Hillen W., Brennan R.G. Nucleic Acids Res. 39:2931-2942(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.96 ANGSTROMS) OF 3-333 IN COMPLEXES WITH P-SER-HPR AND DIVERSE CATABOLITE-RESPONSE ELEMENTS, FUNCTION, DNA-BINDING.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M85182 Genomic DNA. Translation: AAA22501.1.
AF008220 Genomic DNA. Translation: AAC00299.1.
AL009126 Genomic DNA. Translation: CAB14952.1.

PIR

S15318.

RefSeq

NP_390852.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ZVV	X-ray	2.98	A/B/G	5-333	[»]
2FEP	X-ray	2.45	A	58-334	[»]
3OQM	X-ray	2.96	A/C	3-333	[»]
3OQN	X-ray	3.30	A/C	3-333	[»]
3OQO	X-ray	2.97	A/C	3-333	[»]

ProteinModelPortal

P25144.

SMR

P25144. Positions 3-333.

ModBase

Search...

Protein-protein interaction databases

IntAct

P25144. 1 interaction.

STRING

224308.BSU29740.

Proteomic databases

PaxDb

P25144.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAB14952; CAB14952; BSU29740.

GeneID

935942.

KEGG

bsu:BSU29740.

PATRIC

18977856. VBIBacSub10457_3116.

Organism-specific databases

GenoList

BSU29740. [Micado]

Phylogenomic databases

eggNOG

COG1609.

HOGENOM

HOG000220180.

KO

K02529.

OMA

IFYSELA.

ProtClustDB

CLSK2393395.

Enzyme and pathway databases

BioCyc

BSUB:BSU29740-MONOMER.

Family and domain databases

Gene3D

1.10.260.40. 1 hit.

InterPro

IPR006377. CcpA.
IPR010982. Lambda_DNA-bd_dom.
IPR000843. Tscrpt_reg_HTH_LacI.
[Graphical view]

Pfam

PF00356. LacI. 1 hit.
[Graphical view]

PRINTS

PR00036. HTHLACI.

SMART

SM00354. HTH_LACI. 1 hit.
[Graphical view]

SUPFAM

SSF47413. Lambda_like_DNA. 1 hit.

TIGRFAMs

TIGR01481. ccpA. 1 hit.

PROSITE

PS00356. HTH_LACI_1. 1 hit.
PS50932. HTH_LACI_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P25144.

Entry information

Entry name

CCPA_BACSU

Accession

Primary (citable) accession number: P25144

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	May 1, 2013
This is version 114 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program