HUTP_GEOTN
ID HUTP_GEOTN Reviewed; 149 AA.
AC A4IK89;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Hut operon positive regulatory protein {ECO:0000255|HAMAP-Rule:MF_00779};
GN Name=hutP {ECO:0000255|HAMAP-Rule:MF_00779}; OrderedLocusNames=GTNG_0361;
OS Geobacillus thermodenitrificans (strain NG80-2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=420246;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NG80-2;
RX PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA Han W., Peng X., Liu R., Wang L.;
RT "Genome and proteome of long-chain alkane degrading Geobacillus
RT thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
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. {ECO:0000255|HAMAP-Rule:MF_00779}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_00779}.
CC -!- SIMILARITY: Belongs to the HutP family. {ECO:0000255|HAMAP-
CC Rule:MF_00779}.
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DR EMBL; CP000557; ABO65743.1; -; Genomic_DNA.
DR RefSeq; WP_008881231.1; NC_009328.1.
DR PDB; 4OK9; X-ray; 1.91 A; A/B=1-149.
DR PDB; 4OKQ; X-ray; 2.50 A; A/B=1-149.
DR PDBsum; 4OK9; -.
DR PDBsum; 4OKQ; -.
DR AlphaFoldDB; A4IK89; -.
DR SMR; A4IK89; -.
DR STRING; 420246.GTNG_0361; -.
DR EnsemblBacteria; ABO65743; ABO65743; GTNG_0361.
DR KEGG; gtn:GTNG_0361; -.
DR eggNOG; ENOG502ZFIH; Bacteria.
DR HOGENOM; CLU_148478_0_0_9; -.
DR OMA; REMHALY; -.
DR OrthoDB; 1589374at2; -.
DR Proteomes; UP000001578; 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; Histidine metabolism; RNA-binding; Transcription;
KW Transcription regulation.
FT CHAIN 1..149
FT /note="Hut operon positive regulatory protein"
FT /id="PRO_1000148466"
FT HELIX 9..18
FT /evidence="ECO:0007829|PDB:4OK9"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:4OK9"
FT HELIX 25..34
FT /evidence="ECO:0007829|PDB:4OK9"
FT STRAND 37..47
FT /evidence="ECO:0007829|PDB:4OK9"
FT HELIX 48..61
FT /evidence="ECO:0007829|PDB:4OK9"
FT HELIX 70..88
FT /evidence="ECO:0007829|PDB:4OK9"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:4OKQ"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:4OK9"
FT STRAND 100..110
FT /evidence="ECO:0007829|PDB:4OK9"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:4OK9"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:4OK9"
FT STRAND 120..131
FT /evidence="ECO:0007829|PDB:4OK9"
FT STRAND 137..149
FT /evidence="ECO:0007829|PDB:4OK9"
SQ SEQUENCE 149 AA; 16280 MW; 146EFC90C2C3F5B7 CRC64;
MGKEKSVRIG RQALLLAMLD EGEEGAILDE LRASNWRYCQ GRVGAMEPQK IVAAIETAAK
RHEVVDGSLY RDMHALYHAI LEAVHGVTRG QVELGDLLRT AGLRFAVVRG TPYEQPKEGE
WIAVALYGTI GAPVRGLEHE AVGLGINHI
