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 03-AUG-2022, entry version 143.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 PDB; 6UXZ; X-ray; 2.80 A; B/C=107-470.
DR PDBsum; 4MGR; -.
DR PDBsum; 4N0B; -.
DR PDBsum; 4TV7; -.
DR PDBsum; 5T4J; -.
DR PDBsum; 5T4K; -.
DR PDBsum; 5X03; -.
DR PDBsum; 6UXZ; -.
DR AlphaFoldDB; P94426; -.
DR SMR; P94426; -.
DR IntAct; P94426; 1.
DR STRING; 224308.BSU03890; -.
DR PaxDb; P94426; -.
DR PRIDE; P94426; -.
DR EnsemblBacteria; CAB12197; CAB12197; BSU_03890.
DR GeneID; 938271; -.
DR KEGG; bsu:BSU03890; -.
DR PATRIC; fig|224308.179.peg.412; -.
DR eggNOG; COG1167; Bacteria.
DR InParanoid; P94426; -.
DR OMA; DFPTLAW; -.
DR PhylomeDB; P94426; -.
DR BioCyc; BSUB:BSU03890-MON; -.
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;
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:0007829|PDB:4TV7"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:4MGR"
FT HELIX 42..48
FT /evidence="ECO:0007829|PDB:4TV7"
FT HELIX 53..65
FT /evidence="ECO:0007829|PDB:4TV7"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:4TV7"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:4TV7"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:4TV7"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:4TV7"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:5X03"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:5X03"
FT HELIX 124..137
FT /evidence="ECO:0007829|PDB:5X03"
FT TURN 139..143
FT /evidence="ECO:0007829|PDB:5X03"
FT HELIX 152..166
FT /evidence="ECO:0007829|PDB:5X03"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:5X03"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:5X03"
FT HELIX 181..191
FT /evidence="ECO:0007829|PDB:5X03"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:5X03"
FT HELIX 206..214
FT /evidence="ECO:0007829|PDB:5X03"
FT STRAND 219..225
FT /evidence="ECO:0007829|PDB:5X03"
FT HELIX 231..237
FT /evidence="ECO:0007829|PDB:5X03"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:5X03"
FT TURN 250..252
FT /evidence="ECO:0007829|PDB:5X03"
FT HELIX 258..270
FT /evidence="ECO:0007829|PDB:5X03"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:5T4J"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:5X03"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:5X03"
FT HELIX 295..298
FT /evidence="ECO:0007829|PDB:5X03"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:4TV7"
FT STRAND 304..310
FT /evidence="ECO:0007829|PDB:5X03"
FT TURN 311..313
FT /evidence="ECO:0007829|PDB:5X03"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:5T4J"
FT STRAND 321..324
FT /evidence="ECO:0007829|PDB:5X03"
FT HELIX 327..334
FT /evidence="ECO:0007829|PDB:5X03"
FT HELIX 345..356
FT /evidence="ECO:0007829|PDB:5X03"
FT HELIX 359..385
FT /evidence="ECO:0007829|PDB:5X03"
FT TURN 386..388
FT /evidence="ECO:0007829|PDB:5X03"
FT STRAND 390..394
FT /evidence="ECO:0007829|PDB:5X03"
FT STRAND 396..405
FT /evidence="ECO:0007829|PDB:5X03"
FT STRAND 407..409
FT /evidence="ECO:0007829|PDB:5X03"
FT HELIX 411..420
FT /evidence="ECO:0007829|PDB:5X03"
FT HELIX 428..431
FT /evidence="ECO:0007829|PDB:5X03"
FT STRAND 444..448
FT /evidence="ECO:0007829|PDB:5X03"
FT HELIX 454..456
FT /evidence="ECO:0007829|PDB:5X03"
FT HELIX 457..469
FT /evidence="ECO:0007829|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
