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InterPro Inc duf1127 proteins
Duf1127 Proteins, supplied by InterPro Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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InterPro Inc duf1127 proteins
Duf1127 Proteins, supplied by InterPro Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/duf1127 proteins/product/InterPro Inc
Average 90 stars, based on 1 article reviews
duf1127 proteins - by Bioz Stars, 2026-04
90/100 stars
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90
InterPro Inc duf1127 protein
Seven <t>DUF1127</t> proteins are predicted and produced in A. tumefaciens. (A) Characteristics of three SDPs and four LDPs. *, protein annotation was incorrect and adjusted at the N terminus (see Fig. S2B in the supplemental material). (B) Western blot analysis of chromosomally integrated C-terminal 3×FLAG fusions of all seven DUF1127 proteins at different growth phases in YEB medium at 30°C. A heat shock was applied for 20 min at 42°C and cold shock for 20 min at 17°C.
Duf1127 Protein, supplied by InterPro Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/duf1127 protein/product/InterPro Inc
Average 90 stars, based on 1 article reviews
duf1127 protein - by Bioz Stars, 2026-04
90/100 stars
  Buy from Supplier

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Seven DUF1127 proteins are predicted and produced in A. tumefaciens. (A) Characteristics of three SDPs and four LDPs. *, protein annotation was incorrect and adjusted at the N terminus (see Fig. S2B in the supplemental material). (B) Western blot analysis of chromosomally integrated C-terminal 3×FLAG fusions of all seven DUF1127 proteins at different growth phases in YEB medium at 30°C. A heat shock was applied for 20 min at 42°C and cold shock for 20 min at 17°C.

Journal: Journal of Bacteriology

Article Title: Arginine-Rich Small Proteins with a Domain of Unknown Function, DUF1127, Play a Role in Phosphate and Carbon Metabolism of Agrobacterium tumefaciens

doi: 10.1128/JB.00309-20

Figure Lengend Snippet: Seven DUF1127 proteins are predicted and produced in A. tumefaciens. (A) Characteristics of three SDPs and four LDPs. *, protein annotation was incorrect and adjusted at the N terminus (see Fig. S2B in the supplemental material). (B) Western blot analysis of chromosomally integrated C-terminal 3×FLAG fusions of all seven DUF1127 proteins at different growth phases in YEB medium at 30°C. A heat shock was applied for 20 min at 42°C and cold shock for 20 min at 17°C.

Article Snippet: These ORFs were translated into the corresponding amino acid sequences, and all sequences exceeding the length of 23 aa, which corresponds to the previously shortest annotated DUF1127 protein in InterPro (UniProt accession no. A0A370WQ23 ) were subjected to further analyses.

Techniques: Produced, Western Blot

DUF1127 proteins can be divided into clusters. (A) SDPs from A. tumefaciens show a high sequence similarity. Identical residues are marked with an asterisk, residues with highly similar properties are marked with a colon, and weakly conserved residues are marked with a period. Arginine residues are shaded in black. (B) The homology tree of all seven DUF1127 proteins from A. tumefaciens and YjiS from E. coli was calculated by Clustal Omega (109). (C) Subdivision of DUF1127 proteins. The stacked bar chart shows the absolute frequency for the lengths of all DUF1127 proteins from InterPro. A kernel density estimation (dashed line) was superimposed. DUF1127 proteins were divided into subclasses according to sequence similarity to either SDPs from A. tumefaciens or to YjiS from E. coli.

Journal: Journal of Bacteriology

Article Title: Arginine-Rich Small Proteins with a Domain of Unknown Function, DUF1127, Play a Role in Phosphate and Carbon Metabolism of Agrobacterium tumefaciens

doi: 10.1128/JB.00309-20

Figure Lengend Snippet: DUF1127 proteins can be divided into clusters. (A) SDPs from A. tumefaciens show a high sequence similarity. Identical residues are marked with an asterisk, residues with highly similar properties are marked with a colon, and weakly conserved residues are marked with a period. Arginine residues are shaded in black. (B) The homology tree of all seven DUF1127 proteins from A. tumefaciens and YjiS from E. coli was calculated by Clustal Omega (109). (C) Subdivision of DUF1127 proteins. The stacked bar chart shows the absolute frequency for the lengths of all DUF1127 proteins from InterPro. A kernel density estimation (dashed line) was superimposed. DUF1127 proteins were divided into subclasses according to sequence similarity to either SDPs from A. tumefaciens or to YjiS from E. coli.

Article Snippet: These ORFs were translated into the corresponding amino acid sequences, and all sequences exceeding the length of 23 aa, which corresponds to the previously shortest annotated DUF1127 protein in InterPro (UniProt accession no. A0A370WQ23 ) were subjected to further analyses.

Techniques: Sequencing

Cooccurrence of DUF1127 proteins with LsrB and cuckoo sRNAs. The tree shows the phylogenetic relations of a selection of alpha- (α-proteo.) and gammaproteobacteria (γ-proteo.). For each strain, the numbers of SDPs, YjiS-like proteins, and LDPs are given. BLAST searches identified the proteins with the highest similarity to LsrB from A. tumefaciens (A9CI74, B5ZXG9, A0A068SS95, A0A081MRV5, C3MD12, W8I232, G7D4X2, Q2YRP4, Q3J274, Q9I1F9, A1JKA5, A0A0H2UWZ6, A0A0H3GNP2, P30864, and Q8ZRM6). Red and blue colors represent proteins with higher and lower sequence identity than 40%, respectively A genomic neighborhood to a trxB homolog is indicated by a check mark. Putative cuckoo sRNA sequences were extracted from each genome by searching for the pattern (CCTCCTCCC-N20–50)≥1-CCTCCTCCC. The numbers of sequences encoding two, three, or four CCUCCUCCC motifs are given.

Journal: Journal of Bacteriology

Article Title: Arginine-Rich Small Proteins with a Domain of Unknown Function, DUF1127, Play a Role in Phosphate and Carbon Metabolism of Agrobacterium tumefaciens

doi: 10.1128/JB.00309-20

Figure Lengend Snippet: Cooccurrence of DUF1127 proteins with LsrB and cuckoo sRNAs. The tree shows the phylogenetic relations of a selection of alpha- (α-proteo.) and gammaproteobacteria (γ-proteo.). For each strain, the numbers of SDPs, YjiS-like proteins, and LDPs are given. BLAST searches identified the proteins with the highest similarity to LsrB from A. tumefaciens (A9CI74, B5ZXG9, A0A068SS95, A0A081MRV5, C3MD12, W8I232, G7D4X2, Q2YRP4, Q3J274, Q9I1F9, A1JKA5, A0A0H2UWZ6, A0A0H3GNP2, P30864, and Q8ZRM6). Red and blue colors represent proteins with higher and lower sequence identity than 40%, respectively A genomic neighborhood to a trxB homolog is indicated by a check mark. Putative cuckoo sRNA sequences were extracted from each genome by searching for the pattern (CCTCCTCCC-N20–50)≥1-CCTCCTCCC. The numbers of sequences encoding two, three, or four CCUCCUCCC motifs are given.

Article Snippet: These ORFs were translated into the corresponding amino acid sequences, and all sequences exceeding the length of 23 aa, which corresponds to the previously shortest annotated DUF1127 protein in InterPro (UniProt accession no. A0A370WQ23 ) were subjected to further analyses.

Techniques: Selection, Sequencing

SDP and LDP genes are reciprocally regulated by the transcription factor LsrB. (A) Northern blot analyses of SDP- and LDP-encoding genes in the WT and lsrB mutant. Ethidium bromide (EtBr)-stained 16S or 23S rRNA served as a loading control. (B) Putative LsrB-binding sites marked in red match the TGC-N7-GCA motif, and orange sequences display the shorter TGC-N6-GCA motif. Previously described binding sites of the three DUF1127 genes from B. abortus (bab1_0914, bab2_0514, and bab2_0574) are underlined. The position relative to the transcriptional start site (+1) is indicated.

Journal: Journal of Bacteriology

Article Title: Arginine-Rich Small Proteins with a Domain of Unknown Function, DUF1127, Play a Role in Phosphate and Carbon Metabolism of Agrobacterium tumefaciens

doi: 10.1128/JB.00309-20

Figure Lengend Snippet: SDP and LDP genes are reciprocally regulated by the transcription factor LsrB. (A) Northern blot analyses of SDP- and LDP-encoding genes in the WT and lsrB mutant. Ethidium bromide (EtBr)-stained 16S or 23S rRNA served as a loading control. (B) Putative LsrB-binding sites marked in red match the TGC-N7-GCA motif, and orange sequences display the shorter TGC-N6-GCA motif. Previously described binding sites of the three DUF1127 genes from B. abortus (bab1_0914, bab2_0514, and bab2_0574) are underlined. The position relative to the transcriptional start site (+1) is indicated.

Article Snippet: These ORFs were translated into the corresponding amino acid sequences, and all sequences exceeding the length of 23 aa, which corresponds to the previously shortest annotated DUF1127 protein in InterPro (UniProt accession no. A0A370WQ23 ) were subjected to further analyses.

Techniques: Northern Blot, Mutagenesis, Staining, Control, Binding Assay