CHVI_SINFN
ID CHVI_SINFN Reviewed; 241 AA.
AC P50351; C3MBB4;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Transcriptional regulatory protein ChvI;
GN Name=chvI; OrderedLocusNames=NGR_c33930;
OS Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=394;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7559334; DOI=10.1128/jb.177.19.5485-5494.1995;
RA Oesteraas M., Stanley J., Finan T.M.;
RT "Identification of Rhizobium-specific intergenic mosaic elements within an
RT essential two-component regulatory system of Rhizobium species.";
RL J. Bacteriol. 177:5485-5494(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234;
RX PubMed=19376903; DOI=10.1128/aem.00515-09;
RA Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT systems.";
RL Appl. Environ. Microbiol. 75:4035-4045(2009).
CC -!- FUNCTION: Member of a two-component regulatory system ChvG(ExoS)/ChvI
CC involved in regulating the production of succinoglycan. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000305};
CC -!- PATHWAY: Glycan metabolism; exopolysaccharide biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- PTM: Phosphorylated by ChvG. {ECO:0000305}.
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DR EMBL; U32869; AAB07687.1; -; Genomic_DNA.
DR EMBL; CP001389; ACP27123.1; -; Genomic_DNA.
DR RefSeq; WP_012709870.1; NC_012587.1.
DR RefSeq; YP_002827876.1; NC_012587.1.
DR AlphaFoldDB; P50351; -.
DR SMR; P50351; -.
DR STRING; 394.NGR_c33930; -.
DR EnsemblBacteria; ACP27123; ACP27123; NGR_c33930.
DR KEGG; rhi:NGR_c33930; -.
DR PATRIC; fig|394.7.peg.6242; -.
DR eggNOG; COG0745; Bacteria.
DR HOGENOM; CLU_000445_30_4_5; -.
DR OMA; FSLCRWV; -.
DR OrthoDB; 817710at2; -.
DR UniPathway; UPA00631; -.
DR Proteomes; UP000001054; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00383; trans_reg_C; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR001867; OmpR/PhoB-type_DNA-bd.
DR InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR039420; WalR-like.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR48111; PTHR48111; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00486; Trans_reg_C; 1.
DR SMART; SM00448; REC; 1.
DR SMART; SM00862; Trans_reg_C; 1.
DR SUPFAM; SSF46894; SSF46894; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS51755; OMPR_PHOB; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW Cytoplasm; DNA-binding; Exopolysaccharide synthesis; Magnesium;
KW Metal-binding; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Two-component regulatory system.
FT CHAIN 1..241
FT /note="Transcriptional regulatory protein ChvI"
FT /id="PRO_0000081060"
FT DOMAIN 3..116
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT DNA_BIND 140..239
FT /note="OmpR/PhoB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01091"
FT BINDING 8
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 52
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT MOD_RES 52
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT CONFLICT 34..35
FT /note="GA -> R (in Ref. 1; AAB07687)"
FT /evidence="ECO:0000305"
FT CONFLICT 120..132
FT /note="PARDAAAAGVAGA -> SGPRRSRPGSPGR (in Ref. 1;
FT AAB07687)"
FT /evidence="ECO:0000305"
FT CONFLICT 137..152
FT /note="DAPSRSLERGQLVMDQ -> RHPIARWSTAGHGP (in Ref. 1;
FT AAB07687)"
FT /evidence="ECO:0000305"
FT CONFLICT 176..180
FT /note="SLAQR -> FAGTA (in Ref. 1; AAB07687)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="A -> G (in Ref. 1; AAB07687)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 241 AA; 27106 MW; 27A8FE1E7E7BBD7D CRC64;
MQTIALVDDD RNILTSVSIA LEAEGYKVET YTDGASALEG LLARPPHLAI FDIKMPRMDG
MELLRRLRQK SDLPVIFLTS KDEEIDELFG LKMGADDFIT KPFSQRLLVE RVKAILRRAP
ARDAAAAGVA GAAKSADAPS RSLERGQLVM DQERHTCTWK SEPVTLTVTE FLILHSLAQR
PGVVKSRDAL MDAAYDEQVY VDDRTIDSHI KRLRKKFKMV DVDFDMIETL YGVGYRFRES
A
