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Protein

Catabolite control protein A

Gene

ccpA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.5 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi6 – 2520H-T-H motifPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciBSUB:BSU29740-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Catabolite control protein A
Alternative name(s):
Glucose-resistance amylase regulator
Gene namesi
Name:ccpA
Synonyms:alsA, amyR, graR
Ordered Locus Names:BSU29740
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 334334Catabolite control protein APRO_0000107925Add
BLAST

Proteomic databases

PaxDbiP25144.

Expressioni

Gene expression databases

CollecTFiEXPREG_000009c0.

Interactioni

Subunit structurei

Homodimer. Interacts with P-Ser-HPr and P-Ser-Crh.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
codYP397793EBI-5247535,EBI-7827914
ptsHP088773EBI-5247535,EBI-1034482
rpoAP204295EBI-5247535,EBI-5247865

Protein-protein interaction databases

IntActiP25144. 222 interactions.
MINTiMINT-8363378.
STRINGi224308.Bsubs1_010100016226.

Structurei

Secondary structure

1
334
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 138Combined sources
Helixi17 – 259Combined sources
Helixi32 – 4514Combined sources
Helixi51 – 588Combined sources
Beta strandi63 – 697Combined sources
Helixi74 – 8916Combined sources
Beta strandi93 – 986Combined sources
Helixi103 – 11513Combined sources
Beta strandi119 – 1235Combined sources
Helixi130 – 1389Combined sources
Beta strandi139 – 1413Combined sources
Beta strandi143 – 1475Combined sources
Beta strandi157 – 1593Combined sources
Helixi162 – 17514Combined sources
Beta strandi179 – 1868Combined sources
Beta strandi188 – 1903Combined sources
Helixi191 – 1944Combined sources
Helixi197 – 20711Combined sources
Helixi214 – 2163Combined sources
Beta strandi217 – 2193Combined sources
Helixi224 – 23411Combined sources
Beta strandi237 – 2393Combined sources
Beta strandi242 – 2487Combined sources
Helixi249 – 26113Combined sources
Turni266 – 2694Combined sources
Beta strandi271 – 2766Combined sources
Helixi279 – 2813Combined sources
Beta strandi283 – 2864Combined sources
Beta strandi289 – 2924Combined sources
Helixi295 – 31016Combined sources
Beta strandi318 – 3214Combined sources
Beta strandi325 – 3273Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZVVX-ray2.98A/B/G5-333[»]
2FEPX-ray2.45A58-334[»]
3OQMX-ray2.96A/C3-334[»]
3OQNX-ray3.30A/C3-334[»]
3OQOX-ray2.97A/C3-333[»]
ProteinModelPortaliP25144.
SMRiP25144. Positions 3-333.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25144.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 5858HTH lacI-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 HTH lacI-type DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4105ETE. Bacteria.
COG1609. LUCA.
HOGENOMiHOG000220180.
InParanoidiP25144.
KOiK02529.
OMAiCSEYPES.
OrthoDBiEOG6SJJMM.
PhylomeDBiP25144.

Family and domain databases

Gene3Di1.10.260.40. 1 hit.
InterProiIPR006377. CcpA.
IPR010982. Lambda_DNA-bd_dom.
IPR028082. Peripla_BP_I.
IPR000843. Tscrpt_reg_HTH_LacI.
[Graphical view]
PfamiPF00356. LacI. 1 hit.
[Graphical view]
PRINTSiPR00036. HTHLACI.
SMARTiSM00354. HTH_LACI. 1 hit.
[Graphical view]
SUPFAMiSSF47413. SSF47413. 1 hit.
SSF53822. SSF53822. 1 hit.
TIGRFAMsiTIGR01481. ccpA. 1 hit.
PROSITEiPS00356. HTH_LACI_1. 1 hit.
PS50932. HTH_LACI_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25144-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNITIYDVA REANVSMATV SRVVNGNPNV KPTTRKKVLE AIERLGYRPN
60 70 80 90 100
AVARGLASKK TTTVGVIIPD ISSIFYSELA RGIEDIATMY KYNIILSNSD
110 120 130 140 150
QNMEKELHLL NTMLGKQVDG IVFMGGNITD EHVAEFKRSP VPIVLAASVE
160 170 180 190 200
EQEETPSVAI DYEQAIYDAV KLLVDKGHTD IAFVSGPMAE PINRSKKLQG
210 220 230 240 250
YKRALEEANL PFNEQFVAEG DYTYDSGLEA LQHLMSLDKK PTAILSATDE
260 270 280 290 300
MALGIIHAAQ DQGLSIPEDL DIIGFDNTRL SLMVRPQLST VVQPTYDIGA
310 320 330
VAMRLLTKLM NKEPVEEHIV ELPHRIELRK STKS
Length:334
Mass (Da):36,940
Last modified:May 1, 1992 - v1
Checksum:i62AD6CA7294E1FAA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M85182 Genomic DNA. Translation: AAA22501.1.
AF008220 Genomic DNA. Translation: AAC00299.1.
AL009126 Genomic DNA. Translation: CAB14952.1.
PIRiS15318.
RefSeqiNP_390852.1. NC_000964.3.
WP_003229285.1. NZ_JNCM01000036.1.

Genome annotation databases

EnsemblBacteriaiCAB14952; CAB14952; BSU29740.
GeneIDi935942.
KEGGibsu:BSU29740.
PATRICi18977856. VBIBacSub10457_3116.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M85182 Genomic DNA. Translation: AAA22501.1.
AF008220 Genomic DNA. Translation: AAC00299.1.
AL009126 Genomic DNA. Translation: CAB14952.1.
PIRiS15318.
RefSeqiNP_390852.1. NC_000964.3.
WP_003229285.1. NZ_JNCM01000036.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZVVX-ray2.98A/B/G5-333[»]
2FEPX-ray2.45A58-334[»]
3OQMX-ray2.96A/C3-334[»]
3OQNX-ray3.30A/C3-334[»]
3OQOX-ray2.97A/C3-333[»]
ProteinModelPortaliP25144.
SMRiP25144. Positions 3-333.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP25144. 222 interactions.
MINTiMINT-8363378.
STRINGi224308.Bsubs1_010100016226.

Proteomic databases

PaxDbiP25144.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB14952; CAB14952; BSU29740.
GeneIDi935942.
KEGGibsu:BSU29740.
PATRICi18977856. VBIBacSub10457_3116.

Phylogenomic databases

eggNOGiENOG4105ETE. Bacteria.
COG1609. LUCA.
HOGENOMiHOG000220180.
InParanoidiP25144.
KOiK02529.
OMAiCSEYPES.
OrthoDBiEOG6SJJMM.
PhylomeDBiP25144.

Enzyme and pathway databases

BioCyciBSUB:BSU29740-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP25144.
PROiP25144.

Gene expression databases

CollecTFiEXPREG_000009c0.

Family and domain databases

Gene3Di1.10.260.40. 1 hit.
InterProiIPR006377. CcpA.
IPR010982. Lambda_DNA-bd_dom.
IPR028082. Peripla_BP_I.
IPR000843. Tscrpt_reg_HTH_LacI.
[Graphical view]
PfamiPF00356. LacI. 1 hit.
[Graphical view]
PRINTSiPR00036. HTHLACI.
SMARTiSM00354. HTH_LACI. 1 hit.
[Graphical view]
SUPFAMiSSF47413. SSF47413. 1 hit.
SSF53822. SSF53822. 1 hit.
TIGRFAMsiTIGR01481. ccpA. 1 hit.
PROSITEiPS00356. HTH_LACI_1. 1 hit.
PS50932. HTH_LACI_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiCCPA_BACSU
AccessioniPrimary (citable) accession number: P25144
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: February 17, 2016
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.