HUTP_BACSU
ID HUTP_BACSU Reviewed; 148 AA.
AC P10943;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Hut operon positive regulatory protein;
GN Name=hutP; OrderedLocusNames=BSU39340;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2454913; DOI=10.1128/jb.170.7.3199-3205.1988;
RA Oda M., Sugishita A., Furukawa K.;
RT "Cloning and nucleotide sequences of histidase and regulatory genes in the
RT Bacillus subtilis hut operon and positive regulation of the operon.";
RL J. Bacteriol. 170:3199-3205(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / BGSC1A1;
RX PubMed=7704263; DOI=10.1099/13500872-141-2-337;
RA Yoshida K., Sano H., Seki S., Oda M., Fujimura M., Fujita Y.;
RT "Cloning and sequencing of a 29 kb region of the Bacillus subtilis genome
RT containing the hut and wapA loci.";
RL Microbiology 141:337-343(1995).
RN [3]
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 [4]
RP PROTEIN SEQUENCE OF 2-8, AND CHARACTERIZATION.
RC STRAIN=168;
RX PubMed=10712704; DOI=10.1046/j.1365-2958.2000.01795.x;
RA Oda M., Kobayashi N., Ito A., Kurusu Y., Taira K.;
RT "Cis-acting regulatory sequences for antitermination in the transcript of
RT the Bacillus subtilis hut operon and histidine-dependent binding of HutP to
RT the transcript containing the regulatory sequences.";
RL Mol. Microbiol. 35:1244-1254(2000).
RN [5]
RP CHARACTERIZATION OF RNA-BINDING SITES, AND MUTAGENESIS OF N-TERMINAL
RP RESIDUES.
RX PubMed=14763987; DOI=10.1046/j.1365-2958.2003.03891.x;
RA Oda M., Kobayashi N., Fujita M., Miyazaki Y., Sadaie Y., Kurusu Y.,
RA Nishikawa S.;
RT "Analysis of HutP-dependent transcription antitermination in the Bacillus
RT subtilis hut operon: identification of HutP binding sites on hut
RT antiterminator RNA and the involvement of the N-terminus of HutP in binding
RT of HutP to the antiterminator RNA.";
RL Mol. Microbiol. 51:1155-1168(2004).
RN [6]
RP CRYSTALLIZATION, AND MUTAGENESIS OF VAL-51.
RX PubMed=12217662; DOI=10.1016/s1047-8477(02)00024-2;
RA Kumarevel T.S., Fujimoto Z., Padmanabhan B., Oda M., Nishikawa S.,
RA Mizuno H., Kumar P.K.R.;
RT "Crystallization and preliminary X-ray diffraction studies of HutP protein:
RT an RNA-binding protein that regulates the transcription of hut operon in
RT Bacillus subtilis.";
RL J. Struct. Biol. 138:237-240(2002).
CC -!- FUNCTION: Antiterminator that binds to cis-acting regulatory sequences
CC on the mRNA in the presence of histidine, thereby suppressing
CC transcription termination and activating the hut operon for histidine
CC utilization.
CC -!- SUBUNIT: Homohexamer.
CC -!- SIMILARITY: Belongs to the HutP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA22537.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA06645.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M20659; AAA22537.1; ALT_INIT; Genomic_DNA.
DR EMBL; D31856; BAA06645.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB15970.2; -; Genomic_DNA.
DR PIR; S18809; RGBSHP.
DR RefSeq; NP_391813.1; NC_000964.3.
DR RefSeq; WP_003243875.1; NZ_JNCM01000034.1.
DR PDB; 1VEA; X-ray; 2.80 A; A/B=1-148.
DR PDB; 1WMQ; X-ray; 1.60 A; A/B=2-148.
DR PDB; 1WPS; X-ray; 2.80 A; A/B=2-148.
DR PDB; 1WPT; X-ray; 2.70 A; A/B=2-148.
DR PDB; 1WPU; X-ray; 1.48 A; A/B=2-148.
DR PDB; 1WPV; X-ray; 1.70 A; A/B/C=2-148.
DR PDB; 1WRN; X-ray; 2.30 A; A/B/C=2-148.
DR PDB; 1WRO; X-ray; 2.35 A; A/B/C=2-148.
DR PDB; 1WRQ; X-ray; 2.20 A; A/B=2-148.
DR PDB; 3BOY; X-ray; 1.70 A; A/B/C=2-148.
DR PDB; 4H4L; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=1-148.
DR PDBsum; 1VEA; -.
DR PDBsum; 1WMQ; -.
DR PDBsum; 1WPS; -.
DR PDBsum; 1WPT; -.
DR PDBsum; 1WPU; -.
DR PDBsum; 1WPV; -.
DR PDBsum; 1WRN; -.
DR PDBsum; 1WRO; -.
DR PDBsum; 1WRQ; -.
DR PDBsum; 3BOY; -.
DR PDBsum; 4H4L; -.
DR AlphaFoldDB; P10943; -.
DR SMR; P10943; -.
DR STRING; 224308.BSU39340; -.
DR DrugBank; DB01938; L-Histidine Beta Naphthylamide.
DR PaxDb; P10943; -.
DR PRIDE; P10943; -.
DR EnsemblBacteria; CAB15970; CAB15970; BSU_39340.
DR GeneID; 937529; -.
DR KEGG; bsu:BSU39340; -.
DR PATRIC; fig|224308.179.peg.4259; -.
DR eggNOG; ENOG502ZFIH; Bacteria.
DR OMA; REMHALY; -.
DR BioCyc; BSUB:BSU39340-MON; -.
DR EvolutionaryTrace; P10943; -.
DR PRO; PR:P10943; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0003729; F:mRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006547; P:histidine metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.1510.10; -; 1.
DR HAMAP; MF_00779; HutP; 1.
DR InterPro; IPR015111; Regulatory_HutP.
DR InterPro; IPR023552; Regulatory_HutP_bacillales.
DR InterPro; IPR036482; Regulatory_HutP_sf.
DR Pfam; PF09021; HutP; 1.
DR SUPFAM; SSF111064; SSF111064; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Direct protein sequencing; Histidine metabolism;
KW Reference proteome; RNA-binding; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10712704"
FT CHAIN 2..148
FT /note="Hut operon positive regulatory protein"
FT /id="PRO_0000203791"
FT MUTAGEN 2
FT /note="T->A: Great decrease in binding affinity for mRNA."
FT /evidence="ECO:0000269|PubMed:14763987"
FT MUTAGEN 3
FT /note="L->A: Great decrease in binding affinity for mRNA."
FT /evidence="ECO:0000269|PubMed:14763987"
FT MUTAGEN 4
FT /note="H->A: Decrease in binding affinity for mRNA."
FT /evidence="ECO:0000269|PubMed:14763987"
FT MUTAGEN 5
FT /note="K->A: No effect."
FT /evidence="ECO:0000269|PubMed:14763987"
FT MUTAGEN 5
FT /note="K->R: No effect."
FT /evidence="ECO:0000269|PubMed:14763987"
FT MUTAGEN 6
FT /note="E->A: No effect."
FT /evidence="ECO:0000269|PubMed:14763987"
FT MUTAGEN 7
FT /note="R->A: Decrease in binding affinity for mRNA."
FT /evidence="ECO:0000269|PubMed:14763987"
FT MUTAGEN 7
FT /note="R->K: Slight decrease in binding affinity for mRNA."
FT /evidence="ECO:0000269|PubMed:14763987"
FT MUTAGEN 8
FT /note="R->A,K: No effect."
FT /evidence="ECO:0000269|PubMed:14763987"
FT MUTAGEN 8
FT /note="R->P: Great decrease in binding affinity for mRNA."
FT /evidence="ECO:0000269|PubMed:14763987"
FT MUTAGEN 9
FT /note="I->A: Great decrease in binding affinity for mRNA."
FT /evidence="ECO:0000269|PubMed:14763987"
FT MUTAGEN 10
FT /note="G->A: Decrease in binding affinity for mRNA."
FT /evidence="ECO:0000269|PubMed:14763987"
FT MUTAGEN 11
FT /note="R->A,K: No effect."
FT /evidence="ECO:0000269|PubMed:14763987"
FT MUTAGEN 11
FT /note="R->A: No effect."
FT /evidence="ECO:0000269|PubMed:14763987"
FT MUTAGEN 13
FT /note="S->A: No effect."
FT /evidence="ECO:0000269|PubMed:14763987"
FT MUTAGEN 14
FT /note="V->A: No effect."
FT /evidence="ECO:0000269|PubMed:14763987"
FT MUTAGEN 15
FT /note="L->A: Decrease in binding affinity for mRNA."
FT /evidence="ECO:0000269|PubMed:14763987"
FT MUTAGEN 16
FT /note="L->A: No effect."
FT /evidence="ECO:0000269|PubMed:14763987"
FT MUTAGEN 17
FT /note="L->A: Decrease in binding affinity for mRNA."
FT /evidence="ECO:0000269|PubMed:14763987"
FT MUTAGEN 18
FT /note="L->A: Great decrease in binding affinity for mRNA."
FT /evidence="ECO:0000269|PubMed:14763987"
FT MUTAGEN 19
FT /note="N->A: No effect."
FT /evidence="ECO:0000269|PubMed:14763987"
FT MUTAGEN 20
FT /note="E->A: No effect."
FT /evidence="ECO:0000269|PubMed:14763987"
FT MUTAGEN 22
FT /note="E->A: No effect."
FT /evidence="ECO:0000269|PubMed:14763987"
FT MUTAGEN 23
FT /note="E->A: No effect."
FT /evidence="ECO:0000269|PubMed:14763987"
FT MUTAGEN 24
FT /note="S->A: No effect."
FT /evidence="ECO:0000269|PubMed:14763987"
FT MUTAGEN 25
FT /note="T->A: No effect."
FT /evidence="ECO:0000269|PubMed:14763987"
FT MUTAGEN 26
FT /note="Q->A: Decrease in binding affinity for mRNA."
FT /evidence="ECO:0000269|PubMed:14763987"
FT MUTAGEN 32
FT /note="R->A: No effect."
FT /evidence="ECO:0000269|PubMed:14763987"
FT MUTAGEN 35
FT /note="W->A: Great decrease in binding affinity for mRNA."
FT /evidence="ECO:0000269|PubMed:14763987"
FT MUTAGEN 51
FT /note="V->I: Increased ability to bind to hut mRNA in the
FT presence of histidine."
FT /evidence="ECO:0000269|PubMed:12217662"
FT HELIX 5..7
FT /evidence="ECO:0007829|PDB:1WPU"
FT HELIX 9..17
FT /evidence="ECO:0007829|PDB:1WPU"
FT HELIX 26..32
FT /evidence="ECO:0007829|PDB:1WPU"
FT STRAND 36..45
FT /evidence="ECO:0007829|PDB:1WPU"
FT HELIX 47..60
FT /evidence="ECO:0007829|PDB:1WPU"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:1WRN"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:1WPU"
FT HELIX 70..87
FT /evidence="ECO:0007829|PDB:1WPU"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:1WPU"
FT STRAND 99..109
FT /evidence="ECO:0007829|PDB:1WPU"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:1WPU"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:1WPU"
FT STRAND 120..133
FT /evidence="ECO:0007829|PDB:1WPU"
FT STRAND 136..147
FT /evidence="ECO:0007829|PDB:1WPU"
SQ SEQUENCE 148 AA; 16196 MW; 33876C6E8489116F CRC64;
MTLHKERRIG RLSVLLLLNE AEESTQVEEL ERDGWKVCLG KVGSMDAHKV VAAIETASKK
SGVIQSEGYR ESHALYHATM EALHGVTRGE MLLGSLLRTV GLRFAVLRGN PYESEAEGDW
IAVSLYGTIG APIKGLEHET FGVGINHI
