CCPA_BACSU
ID CCPA_BACSU Reviewed; 334 AA.
AC P25144;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Catabolite control protein A;
DE AltName: Full=Glucose-resistance amylase regulator;
GN Name=ccpA; Synonyms=alsA, amyR, graR; OrderedLocusNames=BSU29740;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=1904524; DOI=10.1111/j.1365-2958.1991.tb00728.x;
RA Henkin T.M., Grundy F.J., Nicholson W.L., Chambliss G.H.;
RT "Catabolite repression of alpha-amylase gene expression in Bacillus
RT subtilis involves a trans-acting gene product homologous to the Escherichia
RT coli lacl and galR repressors.";
RL Mol. Microbiol. 5:575-584(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT 200 kb rrnB-dnaB region.";
RL Microbiology 143:3431-3441(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP FUNCTION, DNA-BINDING, AND SUBUNIT.
RX PubMed=7665492; DOI=10.1128/jb.177.17.5129-5134.1995;
RA Kim J.H., Guvener Z.T., Cho J.Y., Chung K.C., Chambliss G.H.;
RT "Specificity of DNA binding activity of the Bacillus subtilis catabolite
RT control protein CcpA.";
RL J. Bacteriol. 177:5129-5134(1995).
RN [5]
RP FUNCTION.
RX PubMed=10559165; DOI=10.1128/jb.181.22.6996-7004.1999;
RA Tobisch S., Zuhlke D., Bernhardt J., Stulke J., Hecker M.;
RT "Role of CcpA in regulation of the central pathways of carbon catabolism in
RT Bacillus subtilis.";
RL J. Bacteriol. 181:6996-7004(1999).
RN [6]
RP FUNCTION.
RC STRAIN=168;
RX PubMed=11557150; DOI=10.1111/j.1574-6968.2001.tb10830.x;
RA Ludwig H., Stulke J.;
RT "The Bacillus subtilis catabolite control protein CcpA exerts all its
RT regulatory functions by DNA-binding.";
RL FEMS Microbiol. Lett. 203:125-129(2001).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.98 ANGSTROMS) OF 5-333 IN COMPLEX WITH P-SER-CRH.
RX PubMed=16316990; DOI=10.1074/jbc.m509977200;
RA Schumacher M.A., Seidel G., Hillen W., Brennan R.G.;
RT "Phosphoprotein Crh-Ser46-P displays altered binding to CcpA to effect
RT carbon catabolite regulation.";
RL J. Biol. Chem. 281:6793-6800(2006).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 58-334 IN COMPLEX WITH P-SER-HPR.
RX PubMed=16755587; DOI=10.1002/prot.21001;
RA Chaptal V., Gueguen-Chaignon V., Poncet S., Lecampion C., Meyer P.,
RA Deutscher J., Galinier A., Nessler S., Morera S.;
RT "Structural analysis of B. subtilis CcpA effector binding site.";
RL Proteins 64:814-816(2006).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.96 ANGSTROMS) OF 3-333 IN COMPLEXES WITH P-SER-HPR
RP AND DIVERSE CATABOLITE-RESPONSE ELEMENTS, FUNCTION, AND DNA-BINDING.
RX PubMed=21106498; DOI=10.1093/nar/gkq1177;
RA Schumacher M.A., Sprehe M., Bartholomae M., Hillen W., Brennan R.G.;
RT "Structures of carbon catabolite protein A-(HPr-Ser46-P) bound to diverse
RT catabolite response element sites reveal the basis for high-affinity
RT binding to degenerate DNA operators.";
RL Nucleic Acids Res. 39:2931-2942(2011).
CC -!- FUNCTION: Global transcriptional regulator of carbon catabolite
CC repression (CCR) and carbon catabolite activation (CCA), which ensures
CC optimal energy usage under diverse conditions. Interacts with either P-
CC Ser-HPr or P-Ser-Crh, leading to the formation of a complex that binds
CC to DNA at the catabolite-response elements (cre). Binding to DNA allows
CC activation or repression of many different genes and operons.
CC {ECO:0000269|PubMed:10559165, ECO:0000269|PubMed:11557150,
CC ECO:0000269|PubMed:1904524, ECO:0000269|PubMed:21106498,
CC ECO:0000269|PubMed:7665492}.
CC -!- SUBUNIT: Homodimer. Interacts with P-Ser-HPr and P-Ser-Crh.
CC {ECO:0000269|PubMed:16316990, ECO:0000269|PubMed:16755587,
CC ECO:0000269|PubMed:7665492}.
CC -!- INTERACTION:
CC P25144; P39779: codY; NbExp=3; IntAct=EBI-5247535, EBI-7827914;
CC P25144; P08877: ptsH; NbExp=3; IntAct=EBI-5247535, EBI-1034482;
CC P25144; P20429: rpoA; NbExp=5; IntAct=EBI-5247535, EBI-5247865;
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M85182; AAA22501.1; -; Genomic_DNA.
DR EMBL; AF008220; AAC00299.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14952.1; -; Genomic_DNA.
DR PIR; S15318; S15318.
DR RefSeq; NP_390852.1; NC_000964.3.
DR RefSeq; WP_003229285.1; NZ_JNCM01000036.1.
DR PDB; 1ZVV; X-ray; 2.98 A; A/B/G=5-333.
DR PDB; 2FEP; X-ray; 2.45 A; A=58-334.
DR PDB; 3OQM; X-ray; 2.96 A; A/C=3-334.
DR PDB; 3OQN; X-ray; 3.30 A; A/C=3-334.
DR PDB; 3OQO; X-ray; 2.97 A; A/C=3-333.
DR PDBsum; 1ZVV; -.
DR PDBsum; 2FEP; -.
DR PDBsum; 3OQM; -.
DR PDBsum; 3OQN; -.
DR PDBsum; 3OQO; -.
DR AlphaFoldDB; P25144; -.
DR SMR; P25144; -.
DR IntAct; P25144; 222.
DR MINT; P25144; -.
DR STRING; 224308.BSU29740; -.
DR jPOST; P25144; -.
DR PaxDb; P25144; -.
DR PRIDE; P25144; -.
DR EnsemblBacteria; CAB14952; CAB14952; BSU_29740.
DR GeneID; 935942; -.
DR KEGG; bsu:BSU29740; -.
DR PATRIC; fig|224308.179.peg.3232; -.
DR eggNOG; COG1609; Bacteria.
DR InParanoid; P25144; -.
DR OMA; HSEFVFM; -.
DR PhylomeDB; P25144; -.
DR BioCyc; BSUB:BSU29740-MON; -.
DR EvolutionaryTrace; P25144; -.
DR PRO; PR:P25144; -.
DR Proteomes; UP000001570; Chromosome.
DR CollecTF; EXPREG_000009c0; -.
DR GO; GO:0032993; C:protein-DNA complex; IMP:CollecTF.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IMP:CollecTF.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IPI:CollecTF.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IMP:CollecTF.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:CACAO.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEP:CollecTF.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd01392; HTH_LacI; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR InterPro; IPR006377; CcpA.
DR InterPro; IPR000843; HTH_LacI.
DR InterPro; IPR046335; LacI/GalR-like_sensor.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR028082; Peripla_BP_I.
DR Pfam; PF00356; LacI; 1.
DR Pfam; PF13377; Peripla_BP_3; 1.
DR PRINTS; PR00036; HTHLACI.
DR SMART; SM00354; HTH_LACI; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
DR TIGRFAMs; TIGR01481; ccpA; 1.
DR PROSITE; PS00356; HTH_LACI_1; 1.
DR PROSITE; PS50932; HTH_LACI_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; DNA-binding; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..334
FT /note="Catabolite control protein A"
FT /id="PRO_0000107925"
FT DOMAIN 1..58
FT /note="HTH lacI-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00111"
FT DNA_BIND 6..25
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00111"
FT HELIX 6..13
FT /evidence="ECO:0007829|PDB:3OQM"
FT HELIX 17..25
FT /evidence="ECO:0007829|PDB:3OQM"
FT HELIX 32..45
FT /evidence="ECO:0007829|PDB:3OQM"
FT HELIX 51..58
FT /evidence="ECO:0007829|PDB:3OQM"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:2FEP"
FT HELIX 74..89
FT /evidence="ECO:0007829|PDB:2FEP"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:2FEP"
FT HELIX 103..115
FT /evidence="ECO:0007829|PDB:2FEP"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:2FEP"
FT HELIX 130..138
FT /evidence="ECO:0007829|PDB:2FEP"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:2FEP"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:2FEP"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:2FEP"
FT HELIX 162..175
FT /evidence="ECO:0007829|PDB:2FEP"
FT STRAND 179..186
FT /evidence="ECO:0007829|PDB:2FEP"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:3OQM"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:2FEP"
FT HELIX 197..207
FT /evidence="ECO:0007829|PDB:2FEP"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:2FEP"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:2FEP"
FT HELIX 224..234
FT /evidence="ECO:0007829|PDB:2FEP"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:2FEP"
FT STRAND 242..248
FT /evidence="ECO:0007829|PDB:2FEP"
FT HELIX 249..261
FT /evidence="ECO:0007829|PDB:2FEP"
FT TURN 266..269
FT /evidence="ECO:0007829|PDB:2FEP"
FT STRAND 271..276
FT /evidence="ECO:0007829|PDB:2FEP"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:2FEP"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:2FEP"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:2FEP"
FT HELIX 295..310
FT /evidence="ECO:0007829|PDB:2FEP"
FT STRAND 318..321
FT /evidence="ECO:0007829|PDB:2FEP"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:2FEP"
SQ SEQUENCE 334 AA; 36940 MW; 62AD6CA7294E1FAA CRC64;
MSNITIYDVA REANVSMATV SRVVNGNPNV KPTTRKKVLE AIERLGYRPN AVARGLASKK
TTTVGVIIPD ISSIFYSELA RGIEDIATMY KYNIILSNSD QNMEKELHLL NTMLGKQVDG
IVFMGGNITD EHVAEFKRSP VPIVLAASVE EQEETPSVAI DYEQAIYDAV KLLVDKGHTD
IAFVSGPMAE PINRSKKLQG YKRALEEANL PFNEQFVAEG DYTYDSGLEA LQHLMSLDKK
PTAILSATDE MALGIIHAAQ DQGLSIPEDL DIIGFDNTRL SLMVRPQLST VVQPTYDIGA
VAMRLLTKLM NKEPVEEHIV ELPHRIELRK STKS
