CCPA_STRMU
ID CCPA_STRMU Reviewed; 333 AA.
AC O07329;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Catabolite control protein A;
GN Name=ccpA; OrderedLocusNames=SMU_1591;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=GS-5;
RA Albone E.F., Burne R.A.;
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT11;
RA Simpson C.L., Russell R.R.B.;
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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; AF001316; AAB58798.1; -; Genomic_DNA.
DR EMBL; AF014460; AAC46294.1; -; Genomic_DNA.
DR EMBL; AE014133; AAN59234.1; -; Genomic_DNA.
DR RefSeq; NP_721928.1; NC_004350.2.
DR RefSeq; WP_002262797.1; NC_004350.2.
DR AlphaFoldDB; O07329; -.
DR SMR; O07329; -.
DR STRING; 210007.SMU_1591; -.
DR PRIDE; O07329; -.
DR EnsemblBacteria; AAN59234; AAN59234; SMU_1591.
DR KEGG; smu:SMU_1591; -.
DR PATRIC; fig|210007.7.peg.1416; -.
DR eggNOG; COG1609; Bacteria.
DR HOGENOM; CLU_037628_6_0_9; -.
DR OMA; HSEFVFM; -.
DR PhylomeDB; O07329; -.
DR Proteomes; UP000002512; Chromosome.
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 3: Inferred from homology;
KW Activator; DNA-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..333
FT /note="Catabolite control protein A"
FT /id="PRO_0000107935"
FT DOMAIN 7..61
FT /note="HTH lacI-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00111"
FT DNA_BIND 9..28
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00111"
FT CONFLICT 264
FT /note="K -> R (in Ref. 1; AAB58798)"
FT /evidence="ECO:0000305"
FT CONFLICT 327..328
FT /note="RE -> KK (in Ref. 1; AAB58798)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="T -> P (in Ref. 2; AAC46294)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 333 AA; 36614 MW; 22A600D1147029F7 CRC64;
MNTDDTITIY DVAREAGVSM ATVSRVVNGN KNVKENTRKK VLEVIDRLDY RPNAVARGLA
SKKTTTVGVV IPNIANAYFS ILAKGIDDIA TMYKYNIVLA SSDEDDDKEV NVINTLFAKQ
VDGIIFMGHH LTEKIRAEFS RARTPVVLSG TVDLEHQLPS VNIDHSKAAQ DAVALLAKHH
DKIAFVSGPL IDDINGKVRL AGYKEGLKKK GLPFKEGLVF EAQYKYQEGY QLAQRVINSG
ATAAYVAEDE LAAGLLNGLF AAGKKVPEDF EIITSNDSTI ALYTRPNMTS ISQPIYDLGA
VAMRMLTKIM NKEELEEKEI VLNHGIRERG TTK