ID H3SMX2_9BACL Unreviewed; 321 AA.
AC H3SMX2;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Catabolite control protein A {ECO:0000256|ARBA:ARBA00019435, ECO:0000256|RuleBase:RU368079};
GN ORFNames=PDENDC454_24595 {ECO:0000313|EMBL:EHQ59577.1};
OS Paenibacillus dendritiformis C454.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1131935 {ECO:0000313|EMBL:EHQ59577.1, ECO:0000313|Proteomes:UP000003900};
RN [1] {ECO:0000313|EMBL:EHQ59577.1, ECO:0000313|Proteomes:UP000003900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C454 {ECO:0000313|EMBL:EHQ59577.1,
RC ECO:0000313|Proteomes:UP000003900};
RX PubMed=22461558; DOI=10.1128/JB.00158-12;
RA Sirota-Madi A., Olender T., Helman Y., Brainis I., Finkelshtein A.,
RA Roth D., Hagai E., Leshkowitz D., Brodsky L., Galatenko V., Nikolaev V.,
RA Gutnick D.L., Lancet D., Ben-Jacob E.;
RT "Genome Sequence of the Pattern-Forming Social Bacterium Paenibacillus
RT dendritiformis C454 Chiral Morphotype.";
RL J. Bacteriol. 194:2127-2128(2012).
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.
CC {ECO:0000256|RuleBase:RU368079}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHQ59577.1}.
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DR EMBL; AHKH01000115; EHQ59577.1; -; Genomic_DNA.
DR AlphaFoldDB; H3SMX2; -.
DR STRING; 1131935.PDENDC454_24595; -.
DR PATRIC; fig|1131935.3.peg.5117; -.
DR Proteomes; UP000003900; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:UniProtKB-UniRule.
DR CDD; cd01392; HTH_LacI; 1.
DR CDD; cd06298; PBP1_CcpA; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 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 NCBIfam; TIGR01481; ccpA; 1.
DR PANTHER; PTHR30146:SF110; HTH-TYPE TRANSCRIPTIONAL REPRESSOR CYTR; 1.
DR PANTHER; PTHR30146; LACI-RELATED TRANSCRIPTIONAL REPRESSOR; 1.
DR Pfam; PF00356; LacI; 1.
DR Pfam; PF13377; Peripla_BP_3; 1.
DR SMART; SM00354; HTH_LACI; 1.
DR SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 1.
DR SUPFAM; SSF53822; Periplasmic binding protein-like I; 1.
DR PROSITE; PS50932; HTH_LACI_2; 1.
PE 4: Predicted;
KW Activator {ECO:0000256|RuleBase:RU368079};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU368079};
KW Reference proteome {ECO:0000313|Proteomes:UP000003900};
KW Repressor {ECO:0000256|ARBA:ARBA00022491, ECO:0000256|RuleBase:RU368079};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU368079};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|RuleBase:RU368079}.
FT DOMAIN 1..42
FT /note="HTH lacI-type"
FT /evidence="ECO:0000259|PROSITE:PS50932"
SQ SEQUENCE 321 AA; 35348 MW; 794101C1231A3FA2 CRC64;
MATVSRVVNN NPNVKPQTRK KVYEAIERLG YRPNAVARGL ASKKTTTVGV VIPDISNSIF
AEVARGIEDI ANMYHYNIIL CNADKKKEKE IRVINTLLEK QVDGLVFMGG VVTEDHIQAF
RTASVPIVLC ATTDENGSIP SVDIDHEGAA FDAVNTLIRH GHRDIAMISG TLQDPANGFA
RFQGYKKALE GAGIEYKEDL VRIGNYRYES GVEAMKYFLG LKKRPTAIFA ATDEMAIGAI
HCIQDAGLKV PDDFSVISVD NIRMASMVRP QLTTVAQPMY DIGAVAMRLL TKLMKKENVE
NSQVVLPHET ILRLSVSQVN E
//