ID Q9KU59_VIBCH Unreviewed; 444 AA.
AC Q9KU59;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 138.
DE SubName: Full=Sigma-54 dependent transcriptional regulator {ECO:0000313|EMBL:AAF93830.1};
GN OrderedLocusNames=VC_0665 {ECO:0000313|EMBL:AAF93830.1};
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277 {ECO:0000313|EMBL:AAF93830.1, ECO:0000313|Proteomes:UP000000584};
RN [1] {ECO:0000313|EMBL:AAF93830.1, ECO:0000313|Proteomes:UP000000584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961
RC {ECO:0000313|Proteomes:UP000000584};
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D., Ermolaeva M.D.,
RA Vamathevan J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.,
RA Utterback T., Fleishmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [2] {ECO:0007829|PDB:7V2B, ECO:0007829|PDB:7V2V}
RP X-RAY CRYSTALLOGRAPHY (3.19 ANGSTROMS) OF 1-382 IN COMPLEX WITH ATP AND
RP GTP.
RX PubMed=34774564; DOI=10.1016/j.jmb.2021.167354;
RA Chakrabortty T., Roy Chowdhury S., Ghosh B., Sen U.;
RT "Crystal Structure of VpsR Revealed Novel Dimeric Architecture and c-di-GMP
RT Binding Site: Mechanistic Implications in Oligomerization, ATPase Activity
RT and DNA Binding.";
RL J. Mol. Biol. 434:167354-167354(2022).
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; AE003852; AAF93830.1; -; Genomic_DNA.
DR PIR; B82296; B82296.
DR RefSeq; NP_230314.1; NC_002505.1.
DR RefSeq; WP_000107102.1; NZ_LT906614.1.
DR PDB; 7V2B; X-ray; 3.20 A; A/D=1-382.
DR PDB; 7V2V; X-ray; 3.19 A; A/D=1-382.
DR PDB; 7V3W; X-ray; 3.21 A; A/D=1-382.
DR PDB; 7V4E; X-ray; 4.00 A; A/D=1-382.
DR AlphaFoldDB; Q9KU59; -.
DR SMR; Q9KU59; -.
DR STRING; 243277.VC_0665; -.
DR DNASU; 2615454; -.
DR EnsemblBacteria; AAF93830; AAF93830; VC_0665.
DR GeneID; 69720579; -.
DR KEGG; vch:VC_0665; -.
DR PATRIC; fig|243277.26.peg.637; -.
DR eggNOG; COG2204; Bacteria.
DR HOGENOM; CLU_000445_0_6_6; -.
DR Proteomes; UP000000584; Chromosome 1.
DR CollecTF; EXPREG_00001750; -.
DR GO; GO:0032993; C:protein-DNA complex; IMP:CollecTF.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0001216; F:DNA-binding transcription activator activity; IMP:CollecTF.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IMP:CollecTF.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEP:CollecTF.
DR CDD; cd00009; AAA; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR002197; HTH_Fis.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002078; Sigma_54_int.
DR InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR InterPro; IPR025944; Sigma_54_int_dom_CS.
DR InterPro; IPR045343; VpsR.
DR PANTHER; PTHR32071; TRANSCRIPTIONAL REGULATORY PROTEIN; 1.
DR PANTHER; PTHR32071:SF117; TRANSCRIPTIONAL REGULATORY PROTEIN; 1.
DR Pfam; PF02954; HTH_8; 1.
DR Pfam; PF00158; Sigma54_activat; 1.
DR Pfam; PF20161; VpsR; 1.
DR PRINTS; PR01590; HTHFIS.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00675; SIGMA54_INTERACT_1; 1.
DR PROSITE; PS00688; SIGMA54_INTERACT_3; 1.
DR PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:7V2B, ECO:0007829|PDB:7V2V};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0007829|PDB:7V3W};
KW GTP-binding {ECO:0007829|PDB:7V2B};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0007829|PDB:7V2B};
KW Reference proteome {ECO:0000313|Proteomes:UP000000584};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 146..368
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000259|PROSITE:PS50045"
FT BINDING 176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:7V3W"
FT BINDING 177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:7V3W"
FT BINDING 177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:7V3W"
FT BINDING 177
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0007829|PDB:7V2B"
FT BINDING 178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:7V3W"
FT BINDING 178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:7V3W"
FT BINDING 178
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0007829|PDB:7V2B"
FT BINDING 179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:7V3W"
FT BINDING 179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:7V3W"
FT BINDING 179
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0007829|PDB:7V2B"
FT BINDING 180
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:7V3W"
FT BINDING 180
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:7V3W"
FT BINDING 180
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0007829|PDB:7V2B"
FT BINDING 181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:7V3W"
FT BINDING 181
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0007829|PDB:7V2B"
FT BINDING 182
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0007829|PDB:7V2B"
FT BINDING 185
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0007829|PDB:7V2B"
FT BINDING 202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:7V3W"
FT BINDING 240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:7V3W"
FT BINDING 357
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:7V3W"
FT BINDING 357
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0007829|PDB:7V2B"
FT BINDING 360
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:7V3W"
SQ SEQUENCE 444 AA; 49715 MW; 0D9B94EE6E638CD7 CRC64;
MSTQFRMDSV PGSLVVVGGT YEPWLAVLEK VGWRCTQVAD LRKADALFVE TGPCIGIVDL
SHDEFSLNGI ANLVSSHKQV RWLAFIREAQ LSSDTICQFI VNFCIDFFTA PIPDAQLLST
IGHQLGMLKL EKKVWPHFGS AGNMGLIGES MPMKRLRDQI KRIGPTDVSI LIYGESGTGK
ETVAKAIHKT SSRAQKPFIS VNCRAMSEKR LESELFGLGE TEEGQQPFLL QADGGTLLLN
DILTLPKSQQ LNLLRFLQEG TVETRQGVRA VDVRILAANS SDIEKALIDG DFNEELYHYI
NVLRINVPSL KERASDIVLL AKHFLQEYSK EYNAQARSFS DDAVRGLTRY HWPGNVRELM
NQIKRVVLMS DTVVLDESQL DLPKRSDGRR SLKSIRERSE RDALLLVLES HSGQVSTAAK
ELGVSRATMY RLLNKHNLIT DENF
//