ID Q2YPW6_BRUA2 Unreviewed; 453 AA.
AC Q2YPW6;
DT 07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 07-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 123.
DE SubName: Full=CbxX/CfqX superfamily:Chaperonin clpA/B:Response regulator receiver:Sigma-54 factor interaction domain:Helix-turn-helix, Fis {ECO:0000313|EMBL:CAJ11094.1};
GN OrderedLocusNames=BAB1_1138 {ECO:0000313|EMBL:CAJ11094.1};
OS Brucella abortus (strain 2308).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391 {ECO:0000313|EMBL:CAJ11094.1, ECO:0000313|Proteomes:UP000002719};
RN [1] {ECO:0000313|EMBL:CAJ11094.1, ECO:0000313|Proteomes:UP000002719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308 {ECO:0000313|EMBL:CAJ11094.1,
RC ECO:0000313|Proteomes:UP000002719};
RX PubMed=16299333; DOI=10.1128/IAI.73.12.8353-8361.2005;
RG Microbial Genomics Group;
RG Lawrence Livermore National Laboratory;
RG and the Genome Analysis Group;
RG Oak Ridge National Laboratory;
RA Chain P., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(2005).
RN [2] {ECO:0007829|PDB:4D6X, ECO:0007829|PDB:4D6Y}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-126 IN COMPLEX WITH MAGNESIUM.
RX PubMed=26113057; DOI=10.1016/J.JMB.2015.06.010;
RA Fernandez I., Otero L.H., Klinke S., Carrica M.d.e.l. .C., Goldbaum F.A.;
RT "Snapshots of Conformational Changes Shed Light into the NtrX Receiver
RT Domain Signal Transduction Mechanism.";
RL J. Mol. Biol. 427:3258-3272(2015).
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DR EMBL; AM040264; CAJ11094.1; -; Genomic_DNA.
DR RefSeq; WP_002964243.1; NZ_KN046823.1.
DR PDB; 4D6X; X-ray; 2.11 A; A/B/C/D=1-126.
DR PDB; 4D6Y; X-ray; 1.70 A; A/B=1-126.
DR PDBsum; 4D6X; -.
DR PDBsum; 4D6Y; -.
DR AlphaFoldDB; Q2YPW6; -.
DR SMR; Q2YPW6; -.
DR STRING; 359391.BAB1_1138; -.
DR GeneID; 45124492; -.
DR KEGG; bmf:BAB1_1138; -.
DR PATRIC; fig|359391.11.peg.37; -.
DR HOGENOM; CLU_000445_0_6_5; -.
DR PhylomeDB; Q2YPW6; -.
DR Proteomes; UP000002719; Chromosome I.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR CDD; cd17550; REC_NtrX-like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.2300; -; 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; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR002078; Sigma_54_int.
DR InterPro; IPR025943; Sigma_54_int_dom_ATP-bd_2.
DR InterPro; IPR025944; Sigma_54_int_dom_CS.
DR PANTHER; PTHR32071:SF17; TRANSCRIPTIONAL REGULATOR (NTRC FAMILY); 1.
DR PANTHER; PTHR32071; TRANSCRIPTIONAL REGULATORY PROTEIN; 1.
DR Pfam; PF02954; HTH_8; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00158; Sigma54_activat; 1.
DR PRINTS; PR01590; HTHFIS.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00448; REC; 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; PS50110; RESPONSE_REGULATORY; 1.
DR PROSITE; PS00676; SIGMA54_INTERACT_2; 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:4D6X, ECO:0007829|PDB:4D6Y};
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0007829|PDB:4D6Y};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000002719};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 4..120
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 142..367
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000259|PROSITE:PS50045"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007829|PDB:4D6Y"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007829|PDB:4D6Y"
FT BINDING 53
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007829|PDB:4D6Y"
FT BINDING 55
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0007829|PDB:4D6Y"
FT MOD_RES 53
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 453 AA; 50155 MW; B21EBE40CDD392C6 CRC64;
MAADILVVDD EVDIRDLVAG ILSDEGHETR TAFDADSALA AINDRAPRLV FLDIWLQGSR
LDGLALLDEI KKQHPELPVV MISGHGNIET AVSAIRRGAY DFIEKPFKAD RLILVAERAL
ETSKLKREVS DLRKRTGDQL ELVGTSLAMN QLRQTIERVA PTNSRIMITG PSGAGKELVA
RAIHAQSSRA NGPFVTVNAA TITPERMEIE LFGTEMDGGE RKVGALEEAH GGILYLDEVA
DMPRETQNKI LRVLVDQQFE RVGGTKRVKV DVRIISSTAQ NLEGMIAEGT FREDLFHRLS
VVPVQVPALA ARREDIPSLV EFFMKQIAEQ AGIKPRKIGP DAMAVLQAHS WPGNLRQLRN
NVERLMILTR GDDPDELVTA DLLPAEIGDT LPRAPTESDQ HIMALPLREA RERFEKEYLI
AQINRFGGNI SRTAEFVGME RSALHRKLKS LGV
//
