(data stored in ACNUC7421 zone)

SWISSPROT: GABR_BACSU

ID   GABR_BACSU              Reviewed;         479 AA.
AC   P94426; Q797N6;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   11-DEC-2019, entry version 131.
DE   RecName: Full=HTH-type transcriptional regulatory protein GabR;
GN   Name=gabR; Synonyms=ycnF; OrderedLocusNames=BSU03890;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969502; DOI=10.1099/13500872-142-11-3047;
RA   Yamane K., Kumano M., Kurita K.;
RT   "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT   determination of the sequence of a 146 kb segment and identification of 113
RT   genes.";
RL   Microbiology 142:3047-3056(1996).
RN   [2]
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   [3]
RP   FUNCTION, AND GENE FAMILY.
RX   PubMed=12123465; DOI=10.1046/j.1365-2958.2002.03036.x;
RA   Belitsky B.R., Sonenshein A.L.;
RT   "GabR, a member of a novel protein family, regulates the utilization of
RT   gamma-aminobutyrate in Bacillus subtilis.";
RL   Mol. Microbiol. 45:569-583(2002).
RN   [4]
RP   FUNCTION IN TRANSCRIPTION REGULATION, DNA-BINDING, AND COFACTOR.
RX   PubMed=15223311; DOI=10.1016/j.jmb.2004.05.020;
RA   Belitsky B.R.;
RT   "Bacillus subtilis GabR, a protein with DNA-binding and aminotransferase
RT   domains, is a PLP-dependent transcriptional regulator.";
RL   J. Mol. Biol. 340:655-664(2004).
CC   -!- FUNCTION: Activates the transcription of the gabTD operon. Is also a
CC       repressor of its own expression, both in the presence and absence of
CC       GABA. Binds specifically to the DNA region overlapping the -35 region
CC       of the gabT promoter and the -10 and +1 regions of the gabR promoter.
CC       Principally regulates the utilization of gamma-aminobutyrate.
CC       {ECO:0000269|PubMed:12123465, ECO:0000269|PubMed:15223311}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:15223311};
CC   -!- SIMILARITY: In the C-terminal section; belongs to the class-I
CC       pyridoxal-phosphate-dependent aminotransferase family. {ECO:0000305}.
DR   EMBL; D50453; BAA09020.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12197.1; -; Genomic_DNA.
DR   PIR; B69764; B69764.
DR   RefSeq; NP_388271.1; NC_000964.3.
DR   RefSeq; WP_003246571.1; NZ_JNCM01000031.1.
DR   PDB; 4MGR; X-ray; 2.55 A; A/B/C/D=1-479.
DR   PDB; 4N0B; X-ray; 2.70 A; A/B/C/D=1-479.
DR   PDB; 4TV7; X-ray; 2.05 A; A/B/C/D=1-479.
DR   PDB; 5T4J; X-ray; 2.23 A; B=107-471.
DR   PDB; 5T4K; X-ray; 2.25 A; A=107-471.
DR   PDB; 5X03; X-ray; 2.00 A; A=108-470, B=108-471.
DR   PDBsum; 4MGR; -.
DR   PDBsum; 4N0B; -.
DR   PDBsum; 4TV7; -.
DR   PDBsum; 5T4J; -.
DR   PDBsum; 5T4K; -.
DR   PDBsum; 5X03; -.
DR   SMR; P94426; -.
DR   IntAct; P94426; 1.
DR   STRING; 224308.BSU03890; -.
DR   PaxDb; P94426; -.
DR   PRIDE; P94426; -.
DR   EnsemblBacteria; CAB12197; CAB12197; BSU03890.
DR   GeneID; 938271; -.
DR   KEGG; bsu:BSU03890; -.
DR   PATRIC; fig|224308.179.peg.412; -.
DR   eggNOG; COG1167; LUCA.
DR   HOGENOM; HOG000223052; -.
DR   InParanoid; P94426; -.
DR   KO; K00375; -.
DR   OMA; VSTYYKD; -.
DR   PhylomeDB; P94426; -.
DR   BioCyc; BSUB:BSU03890-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   CDD; cd07377; WHTH_GntR; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR000524; Tscrpt_reg_HTH_GntR.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   Pfam; PF00392; GntR; 1.
DR   SMART; SM00345; HTH_GNTR; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS50949; HTH_GNTR; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P94426.
DR   SWISS-2DPAGE; P94426.
KW   3D-structure; Activator; Aminotransferase; DNA-binding;
KW   Pyridoxal phosphate; Reference proteome; Repressor; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN           1..479
FT                   /note="HTH-type transcriptional regulatory protein GabR"
FT                   /id="PRO_0000305244"
FT   DOMAIN          14..82
FT                   /note="HTH gntR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00307"
FT   DNA_BIND        42..61
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00307"
FT   MOD_RES         312
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   HELIX           16..29
FT                   /evidence="ECO:0000244|PDB:4TV7"
FT   STRAND          31..33
FT                   /evidence="ECO:0000244|PDB:4MGR"
FT   HELIX           42..48
FT                   /evidence="ECO:0000244|PDB:4TV7"
FT   HELIX           53..65
FT                   /evidence="ECO:0000244|PDB:4TV7"
FT   STRAND          68..72
FT                   /evidence="ECO:0000244|PDB:4TV7"
FT   TURN            73..75
FT                   /evidence="ECO:0000244|PDB:4TV7"
FT   STRAND          76..79
FT                   /evidence="ECO:0000244|PDB:4TV7"
FT   HELIX           97..99
FT                   /evidence="ECO:0000244|PDB:4TV7"
FT   STRAND          110..114
FT                   /evidence="ECO:0000244|PDB:5X03"
FT   HELIX           119..121
FT                   /evidence="ECO:0000244|PDB:5X03"
FT   HELIX           124..137
FT                   /evidence="ECO:0000244|PDB:5X03"
FT   TURN            139..143
FT                   /evidence="ECO:0000244|PDB:5X03"
FT   HELIX           152..166
FT                   /evidence="ECO:0000244|PDB:5X03"
FT   HELIX           172..174
FT                   /evidence="ECO:0000244|PDB:5X03"
FT   STRAND          175..180
FT                   /evidence="ECO:0000244|PDB:5X03"
FT   HELIX           181..191
FT                   /evidence="ECO:0000244|PDB:5X03"
FT   STRAND          198..203
FT                   /evidence="ECO:0000244|PDB:5X03"
FT   HELIX           206..214
FT                   /evidence="ECO:0000244|PDB:5X03"
FT   STRAND          219..225
FT                   /evidence="ECO:0000244|PDB:5X03"
FT   HELIX           231..237
FT                   /evidence="ECO:0000244|PDB:5X03"
FT   STRAND          240..244
FT                   /evidence="ECO:0000244|PDB:5X03"
FT   TURN            250..252
FT                   /evidence="ECO:0000244|PDB:5X03"
FT   HELIX           258..270
FT                   /evidence="ECO:0000244|PDB:5X03"
FT   STRAND          271..273
FT                   /evidence="ECO:0000244|PDB:5T4J"
FT   STRAND          275..279
FT                   /evidence="ECO:0000244|PDB:5X03"
FT   STRAND          286..289
FT                   /evidence="ECO:0000244|PDB:5X03"
FT   HELIX           295..298
FT                   /evidence="ECO:0000244|PDB:5X03"
FT   STRAND          300..302
FT                   /evidence="ECO:0000244|PDB:4TV7"
FT   STRAND          304..310
FT                   /evidence="ECO:0000244|PDB:5X03"
FT   TURN            311..313
FT                   /evidence="ECO:0000244|PDB:5X03"
FT   HELIX           316..318
FT                   /evidence="ECO:0000244|PDB:5T4J"
FT   STRAND          321..324
FT                   /evidence="ECO:0000244|PDB:5X03"
FT   HELIX           327..334
FT                   /evidence="ECO:0000244|PDB:5X03"
FT   HELIX           345..356
FT                   /evidence="ECO:0000244|PDB:5X03"
FT   HELIX           359..385
FT                   /evidence="ECO:0000244|PDB:5X03"
FT   TURN            386..388
FT                   /evidence="ECO:0000244|PDB:5X03"
FT   STRAND          390..394
FT                   /evidence="ECO:0000244|PDB:5X03"
FT   STRAND          396..405
FT                   /evidence="ECO:0000244|PDB:5X03"
FT   STRAND          407..409
FT                   /evidence="ECO:0000244|PDB:5X03"
FT   HELIX           411..420
FT                   /evidence="ECO:0000244|PDB:5X03"
FT   HELIX           428..431
FT                   /evidence="ECO:0000244|PDB:5X03"
FT   STRAND          444..448
FT                   /evidence="ECO:0000244|PDB:5X03"
FT   HELIX           454..456
FT                   /evidence="ECO:0000244|PDB:5X03"
FT   HELIX           457..469
FT                   /evidence="ECO:0000244|PDB:5X03"
SQ   SEQUENCE   479 AA;  55166 MW;  B8138FD28A276A4E CRC64;
     MDITITLDRS EQADYIYQQI YQKLKKEILS RNLLPHSKVP SKRELAENLK VSVNSVNSAY
     QQLLAEGYLY AIERKGFFVE ELDMFSAEEH PPFALPDDLK EIHIDQSDWI SFSHMSSDTD
     HFPIKSWFRC EQKAASRSYR TLGDMSHPQG IYEVRAAITR LISLTRGVKC RPEQMIIGAG
     TQVLMQLLTE LLPKEAVYAM EEPGYRRMYQ LLKNAGKQVK TIMLDEKGMS IAEITRQQPD
     VLVTTPSHQF PSGTIMPVSR RIQLLNWAAE EPRRYIIEDD YDSEFTYDVD SIPALQSLDR
     FQNVIYMGTF SKSLLPGLRI SYMVLPPELL RAYKQRGYDL QTCSSLTQLT LQEFIESGEY
     QKHIKKMKQH YKEKRERLIT ALEAEFSGEV TVKGANAGLH FVTEFDTRRT EQDILSHAAG
     LQLEIFGMSR FNLKENKRQT GRPALIIGFA RLKEEDIQEG VQRLFKAVYG HKKIPVTGD
//

If you have problems or comments...

PBIL Back to PBIL home page