RRF1_DESVH
ID RRF1_DESVH Reviewed; 138 AA.
AC P33394;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Protein Rrf1;
GN Name=rrf1; OrderedLocusNames=DVU_0530;
OS Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS B-1760 / Hildenborough).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
OX NCBI_TaxID=882;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8335628; DOI=10.1128/jb.175.15.4699-4711.1993;
RA Rossi M., Pollock W.B.R., Reij M.W., Keon R.G., Fu R., Voordouw G.;
RT "The hmc operon of Desulfovibrio vulgaris subsp. vulgaris Hildenborough
RT encodes a potential transmembrane redox protein complex.";
RL J. Bacteriol. 175:4699-4711(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX PubMed=15077118; DOI=10.1038/nbt959;
RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA Wall J.D., Voordouw G., Fraser C.M.;
RT "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT Desulfovibrio vulgaris Hildenborough.";
RL Nat. Biotechnol. 22:554-559(2004).
CC -!- FUNCTION: May be involved in regulation of gene transcription. Belongs
CC to the family of response regulators, and members of this family
CC involved in the regulation of gene transcription are two-domain
CC proteins. This protein contains only the N-terminal phosphorylation
CC domain and not the C-terminal DNA-binding domain but it may bind to
CC Rrf2 protein and the latter may bind to DNA.
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DR EMBL; L16784; AAA72000.1; -; Unassigned_DNA.
DR EMBL; AE017285; AAS95012.1; -; Genomic_DNA.
DR PIR; G40605; G40605.
DR RefSeq; WP_010937836.1; NZ_CABHLV010000001.1.
DR RefSeq; YP_009753.1; NC_002937.3.
DR AlphaFoldDB; P33394; -.
DR SMR; P33394; -.
DR STRING; 882.DVU_0530; -.
DR PaxDb; P33394; -.
DR EnsemblBacteria; AAS95012; AAS95012; DVU_0530.
DR KEGG; dvu:DVU_0530; -.
DR PATRIC; fig|882.5.peg.506; -.
DR eggNOG; COG2204; Bacteria.
DR HOGENOM; CLU_000445_69_17_7; -.
DR OMA; PEAYIEK; -.
DR PhylomeDB; P33394; -.
DR Proteomes; UP000002194; Chromosome.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; SSF52172; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 3: Inferred from homology;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Two-component regulatory system.
FT CHAIN 1..138
FT /note="Protein Rrf1"
FT /id="PRO_0000081221"
FT DOMAIN 4..116
FT /note="Response regulatory"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MOD_RES 13
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT MOD_RES 53
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 138 AA; 14797 MW; BDC99E00D1647C45 CRC64;
MPARILVVQE DPDIAAYLVS LFRQAGYKAD AATEGPDAVE MVQASRPDVV FLDLALPQRW
GPRFYSWMVT QPGCGNVPVV LVTDFAGLEL MVPNAVGTVD KPFDPVLLLA LVDRALATYA
KGTPDTPDTT GAPAPDNR
