DEGA_BACSU
ID DEGA_BACSU Reviewed; 337 AA.
AC P37947; O06729;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=HTH-type transcriptional regulator DegA;
DE AltName: Full=Degradation activator;
GN Name=degA; OrderedLocusNames=BSU10840;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-20.
RC STRAIN=168 / DB104;
RX PubMed=8407808; DOI=10.1128/jb.175.19.6348-6353.1993;
RA Bussey L.B., Switzer R.L.;
RT "The degA gene product accelerates degradation of Bacillus subtilis
RT phosphoribosylpyrophosphate amidotransferase in Escherichia coli.";
RL J. Bacteriol. 175:6348-6353(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Oudega B., Koningstein G., Duesterhoeft A.;
RT "Bacillus subtilis genome project, DNA sequence from yucA to yucH.";
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9353932; DOI=10.1099/00221287-143-10-3309;
RA Roche B., Autret S., Levine A., Vannier F., Medina N., Seror S.J.;
RT "A Bacillus subtilis chromosome segment at the 100 degrees to 102 degrees
RT position encoding 11 membrane proteins.";
RL Microbiology 143:3309-3312(1997).
RN [4]
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).
CC -!- FUNCTION: Involved in the control of degradation of B.subtilis
CC amidophosphoribosyltransferase (purF). Probably activates the gene for
CC a degradative protease.
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DR EMBL; L08822; AAA03541.1; -; Unassigned_DNA.
DR EMBL; Y09476; CAA70647.1; -; Genomic_DNA.
DR EMBL; Z93940; CAB07961.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12923.1; -; Genomic_DNA.
DR PIR; G69613; A36940.
DR RefSeq; NP_388964.1; NC_000964.3.
DR AlphaFoldDB; P37947; -.
DR SMR; P37947; -.
DR STRING; 224308.BSU10840; -.
DR PaxDb; P37947; -.
DR PRIDE; P37947; -.
DR EnsemblBacteria; CAB12923; CAB12923; BSU_10840.
DR GeneID; 936363; -.
DR KEGG; bsu:BSU10840; -.
DR PATRIC; fig|224308.43.peg.1130; -.
DR eggNOG; COG1609; Bacteria.
DR InParanoid; P37947; -.
DR BioCyc; BSUB:BSU10840-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
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; 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 PROSITE; PS00356; HTH_LACI_1; 1.
DR PROSITE; PS50932; HTH_LACI_2; 1.
PE 1: Evidence at protein level;
KW Activator; Direct protein sequencing; DNA-binding; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..337
FT /note="HTH-type transcriptional regulator DegA"
FT /id="PRO_0000107942"
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 REGION 300..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 300..311
FT /note="AERHRTAGRSNR -> RSVIELLAEAIE (in Ref. 3; CAA70647)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 337 AA; 36663 MW; 0A92EB0E72CE3D97 CRC64;
MKTTIYDVAK AAGVSITTVS RVINNTGRIS DKTRQKVMNV MNEMAYTPNV HAAALTGKRT
NMIALVAPDI SNPFYGELAK SIEERADELG FQMLICSTDY DPKKETKYFS VLKQKKVDGI
IFATGIESHD SMSALEEIAS EQIPIAMISQ DKPLLPMDIV VIDDVRGGYE AAKHLLSLGH
TNIACIIGDG STTGEKNRIK GFRQAMEEAG VPIDESLIIQ TRFSLESGKE EAGKLLDRNA
PTAIFAFNDV LACAAIQAAR IRGIKVPDDL SIIGFDNTIL AEMAAPPLTT VAQPIKEMGA
ERHRTAGRSN RGKRKAKQKI VLPPELVVRH STSPLNT