CCPA_PRIMG
ID CCPA_PRIMG Reviewed; 332 AA.
AC P46828;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Catabolite control protein A;
DE AltName: Full=Catabolite control protein;
DE AltName: Full=Glucose-resistance amylase regulator;
GN Name=ccpA;
OS Priestia megaterium (Bacillus megaterium).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Priestia.
OX NCBI_TaxID=1404;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8200532; DOI=10.1016/0378-1119(94)90621-1;
RA Hueck C., Kraus A., Hillen W.;
RT "Sequences of ccpA and two downstream Bacillus megaterium genes with
RT homology to the motAB operon from Bacillus subtilis.";
RL Gene 143:147-148(1994).
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. {ECO:0000250}.
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DR EMBL; L26052; AAA22295.1; -; Genomic_DNA.
DR PIR; I39800; I39800.
DR PDB; 1RZR; X-ray; 2.80 A; A/C/D/G=1-332.
DR PDB; 1SXG; X-ray; 2.75 A; A/B/D/F/I/P=53-332.
DR PDB; 1SXH; X-ray; 2.75 A; A/D=53-332.
DR PDB; 1SXI; X-ray; 3.00 A; A/B/D/G/I/K/L/M/N/R/T/W=53-332.
DR PDB; 2HSG; X-ray; 2.50 A; A=1-332.
DR PDB; 2JCG; X-ray; 2.60 A; A=1-332.
DR PDB; 2NZU; X-ray; 2.50 A; G=53-332.
DR PDB; 2NZV; X-ray; 3.00 A; G=53-332.
DR PDB; 2OEN; X-ray; 3.17 A; G=53-332.
DR PDBsum; 1RZR; -.
DR PDBsum; 1SXG; -.
DR PDBsum; 1SXH; -.
DR PDBsum; 1SXI; -.
DR PDBsum; 2HSG; -.
DR PDBsum; 2JCG; -.
DR PDBsum; 2NZU; -.
DR PDBsum; 2NZV; -.
DR PDBsum; 2OEN; -.
DR AlphaFoldDB; P46828; -.
DR SMR; P46828; -.
DR DrugBank; DB02283; 2-Phenylamino-Ethanesulfonic Acid.
DR EvolutionaryTrace; P46828; -.
DR PRO; PR:P46828; -.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
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; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..332
FT /note="Catabolite control protein A"
FT /id="PRO_0000107924"
FT DOMAIN 1..57
FT /note="HTH lacI-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00111"
FT DNA_BIND 5..24
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00111"
FT HELIX 5..11
FT /evidence="ECO:0007829|PDB:2HSG"
FT HELIX 16..23
FT /evidence="ECO:0007829|PDB:2HSG"
FT HELIX 31..44
FT /evidence="ECO:0007829|PDB:2HSG"
FT HELIX 50..55
FT /evidence="ECO:0007829|PDB:2HSG"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:2HSG"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:2JCG"
FT HELIX 74..89
FT /evidence="ECO:0007829|PDB:2HSG"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:2HSG"
FT HELIX 101..111
FT /evidence="ECO:0007829|PDB:2HSG"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:2JCG"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:2HSG"
FT HELIX 129..135
FT /evidence="ECO:0007829|PDB:2HSG"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:2HSG"
FT STRAND 142..146
FT /evidence="ECO:0007829|PDB:2HSG"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:2HSG"
FT HELIX 161..173
FT /evidence="ECO:0007829|PDB:2HSG"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:2HSG"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:2HSG"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:1RZR"
FT HELIX 190..193
FT /evidence="ECO:0007829|PDB:2HSG"
FT HELIX 196..205
FT /evidence="ECO:0007829|PDB:2HSG"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:2HSG"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:2HSG"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:2HSG"
FT HELIX 223..235
FT /evidence="ECO:0007829|PDB:2HSG"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:2HSG"
FT STRAND 241..247
FT /evidence="ECO:0007829|PDB:2HSG"
FT HELIX 248..260
FT /evidence="ECO:0007829|PDB:2HSG"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:2HSG"
FT STRAND 270..275
FT /evidence="ECO:0007829|PDB:2HSG"
FT HELIX 278..281
FT /evidence="ECO:0007829|PDB:2HSG"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:2HSG"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:2HSG"
FT HELIX 294..309
FT /evidence="ECO:0007829|PDB:2HSG"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:2HSG"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:2HSG"
SQ SEQUENCE 332 AA; 36645 MW; FED354B07E86A136 CRC64;
MNVTIYDVAR EASVSMATVS RVVNGNPNVK PSTRKKVLET IERLGYRPNA VARGLASKKT
TTVGVIIPDI SNIFYAELAR GIEDIATMYK YNIILSNSDQ NQDKELHLLN NMLGKQVDGI
IFMSGNVTEE HVEELKKSPV PVVLAASIES TNQIPSVTID YEQAAFDAVQ SLIDSGHKNI
AFVSGTLEEP INHAKKVKGY KRALTESGLP VRDSYIVEGD YTYDSGIEAV EKLLEEDEKP
TAIFVGTDEM ALGVIHGAQD RGLNVPNDLE IIGFDNTRLS TMVRPQLTSV VQPMYDIGAV
AMRLLTKYMN KETVDSSIVQ LPHRIEFRQS TK
