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bvrS from Brucella suis 1330

Victor ID 1113
Gene Name bvrS from Brucella suis 1330
Sequence Strain (Species/Organism) Brucella suis 1330
NCBI Gene ID 1167794
NCBI Protein GI 23502939
Locus Tag BR2091
Protein Accession NP_699066.1
Other Database IDs UniProtKB-ID: Q8FY03_BRUSU
UniRef100: UniRef100_Q8FY03
UniRef90: UniRef90_A6WX45
UniRef50: UniRef50_Q07737
UniParc: UPI00000DD7A5
EMBL: AE014291
EMBL-CDS: AAN30981.1
RefSeq_NT: NC_004310.3
HSSP: P02933
GenomeReviews: AE014291_GR
KEGG: bms:BR2091
NMPDR: fig|204722.1.peg.2023
TIGR: BR2091
HOGENOM: HBG294236
OMA: ILYLNQF
ProtClustDB: CLSK864189
BioCyc: BSUI204722:BR_2091-MONOMER
Taxonomy ID 204722
Chromosome No I
Gene Starting Position 2013888
Gene Ending Position 2015693
Gene Strand (Orientation) +
Protein Name sensor histidine kinase BvrS, putative
DNA Sequence
>gi|56968325:2013888-2015693 Brucella suis 1330 chromosome I, complete sequence
CATGGTCGCAGAGACCCAGAAAGATAGCCTTTCGGGGATGCGCGAGCGCAGAGCACGGCGGCAACGCTCG
GTGTTTCTGCGCCGCTTTCTGTCGCCCTTGCGCAAGTTTCTTGGGCAATATCTCTTTTCAAGCCTGACGC
GCCGCATCCTGTTTCTCAACCTGGCAGCACTGGCCGTTCTGGTTTCCGGCATTCTTTATATGAACCAGTT
CCGCGAGGGGCTGATCGACGCCAAGATCGAAAGCCTGCTGACGCAGGGCAAGATCATCGCTGCTGCGATT
TCTGCATCGGCTACGGTCGATACCAATTCGCTGCTGATCGACCCTGAAAAGCTTCTGGAGCTTCAGGCCG
GGCAGAGCATAACCCCCTCCCCCGATTCGCCGGATAATTGGGAATTTCCGATCAATCCCGAAAAGGTTTC
GCCGCTGCTGCGCCAGTTGATCTCTCCGACCAGCACGCGCGCGCGCATCTATGACCGCTATGCGAATAAG
CTGCTTGATTCGCGCGCGCTTTATTCGACAAGCTTCCCGTCCAGCGGGCCGGTCCTGCGCTATGACCTGC
CGCCGATAGAGGATGAGACGCCTGCCCTTTGGGAACGTATCGGCAGCTGGCTGTCGCGCCTTTTCTATGG
CGGTGGCCTGCCGCTCTACCAGGAGCAGCCGGGCGGAAACGGCCTTGCCTATCAGGAAATCGTCAAGGCG
CTGAGCGGCTCGCCGCAGATGGCACAGCGCCGCAATCAGCGCGGTGAGCTGATCGTTTCCGTGGCCGTTC
CTATCCAGCGCTCCCGTGCCATTCTGGGTGTTCTGCTTCTTTCTACCGAAGGCGATGATATCGACAAGAT
CGTTCAGGCCGAGCGTATGGCGGTTTTCCGCGTGTTCGGCGTTGTGTCGGCGGTCATGGTCATCCTGTCG
CTTTTCCTCGCCTCAACAATTGCCAACCCCTTGCGCAAGCTTTCGGCTGCGGCGGACCGGGTGCGCCATG
GCGTGAAAAACCGCGTGGAAATTCCCGATTTTTCCGAGCGTCAGGACGAGGTGGGCCACCTTTCCACCTC
CATCCGCGACATGACGGACGCGCTTTATACGCGCATCGAAGCCATTGAAAGCTTCGCAGCCGATGTCAGC
CATGAGCTGAAGAACCCCCTCACCTCGCTTCGCAGCGCAGTCGAAACCCTGCCGCTCGCCAAGACCGACG
AATCACGCAAGCGCCTGCTCGATGTCATCCAGCACGACGTGCGGCGGCTGGACCGCCTTATCACGGATAT
TTCCGACGTTTCGCGCCTCGATGCCGAGCTTGCGCGCGAACATATCGACCGCGTGGATATGAAAAAGCTT
CTCACCAGCCTTGTGACTGCCGCCCGCGAAGTGCGGCGCAACAAGGTCGGCACCGAAATCGTGTTCAACA
CGGGCAAGCTGCCTACCGGCAAGAAAGGCTTCTATGTCGCCGGCCACGATCTGCGTTTTGGGCAGGTGGT
AAGCAACCTTATCGAGAATGCGCGCTCCTTCGTGCCTGACGATACGGGCCGTATCGTCGTTACGCTGGCC
GGCGAAGGCAACCGGCTGCGCATTCTGGTCGAGGATAACGGCCCCGGCATTCCTATCGAGAATATCGAGC
GCATCTTCGAGCGTTTCTACACGGATCGCCCGGCATCGGAAGCATTCGGGCAGAATTCCGGCCTCGGCCT
GTCGATCAGCCGGCAGATCATCGAGGCGCATGGCGGCACGCTGACGGCGGAAAATATTACCGATCCGGAT
AAGCCGGATATTTTCAAGGGTGCCCGCTTTATCGTTGATCTTCCGGCCAGCGCATG
Protein Sequence
>gi|23502939|ref|NP_699066.1| sensor histidine kinase BvrS [Brucella suis 1330] MVAETQKDSLSGMRERRARRQRSVFLRRFLSPLRKFLGQYLFSSLTRRILFLNLAALAVLVSGILYMNQFREGLIDAKIESLLTQGKIIAAAISASATVDTNSLLIDPEKLLELQAGQSITPSPDSPDNWEFPINPEKVSPLLRQLISPTSTRARIYDRYANKLLDSRALYSTSFPSSGPVLRYDLPPIEDETPALWERIGSWLSRLFYGGGLPLYQEQPGGNGLAYQEIVKALSGSPQMAQRRNQRGELIVSVAVPIQRSRAILGVLLLSTEGDDIDKIVQAERMAVFRVFGVVSAVMVILSLFLASTIANPLRKLSAAADRVRHGVKNRVEIPDFSERQDEVGHLSTSIRDMTDALYTRIEAIESFAADVSHELKNPLTSLRSAVETLPLAKTDESRKRLLDVIQHDVRRLDRLITDISDVSRLDAELAREHIDRVDMKKLLTSLVTAAREVRRNKVGTEIVFNTGKLPTGKKGFYVAGHDLRFGQVVSNLIENARSFVPDDTGRIVVTLAGEGNRLRILVEDNGPGIPIENIERIFERFYTDRPASEAFGQNSGLGLSISRQIIEAHGGTLTAENITDPDKPDIFKGARFIVDLPASA
Molecule Role Virulence factor
Molecule Role Annotation MUTATION: The two-component BvrSBvrR system is essential for Brucella abortus virulence. Disruption of BvrSBvrR damages the outer membrane, thus contributing to the severe attenuation manifested by bvrS and bvrR mutants. The bvrS and bvrR mutants are avirulent in mice, show reduced invasiveness to epithelial cells and macrophages, and are incapable of inhibiting lysosome fusion and replicating intracellularly (Guzman-Verri et al., 2002).

Mutations in the bvrR or bvrS genes hamper the penetration of B abortus in non-phagocytic cells and impairs intracellular trafficking and virulence. BvrRBvrS mutants do not recruit small GTPases of the Rho subfamily required for actin polymerization and penetration to cells. Dysfunction of the BvrRBvrS system alters the outer membrane permeability, the expression of several group 3 outer membrane proteins and the pattern of lipid A acylation. Constructs of virulent B abortus chimeras containing heterologous LPS from the bvrS(-) mutant demonstrated an altered permeability to cationic peptides similar to that of the BvrRBvrS mutants. It is hypothesized that the Brucella BvrRBvrS is a system devoted to the homeostasis of the outer membrane and, therefore in the interface for cell invasion and mounting the required structures for intracellular parasitism (Guzman-Verri et al., 2002).

In contrast to S2308 and S19, bvrS and bvrR mutant strains poorly invade HeLa cells and are rapidly targeted to cathepsin D- containing compartments (Guzman-Verri et al., 2002).

B abortus bvrS bvrR mutants display reduced invasiveness and virulence (Guzman-Verri et al., 2002).

Brucella bvrS and bvrR null mutants are defective in several outer membrane proteins, mainly Omp3a (former Omp25) and Omp3b as well as in the structure of the LPS molecule, but the O chain seems to be intact (Guzman-Verri et al., 2002).

Because bvrR and bvrS mutants are also altered in cell-surface hydrophobicity, permeability, and sensitivity to surface- targeted bactericidal peptides, it is proposed that BvrRBvrS controls cell envelope changes necessary to transit between extracellular and intracellular environments (Guzman-Verri et al., 2002).

BvrR/BvrS mutants are avirulent in mice, show reduced invasiveness in cells, and are unable to inhibit lysosome fusion and to replicate intracellularly (Guzman-Verri et al., 2002).
COG COG0642T, under T: Signal transduction mechanisms
References
Guzman-Verri et al., 2002: Guzman-Verri C, Manterola L, Sola-Landa A, Parra A, Cloeckaert A, Garin J, Gorvel JP, Moriyon I, Moreno E, Lopez-Goni I. The two-component system BvrR/BvrS essential for Brucella abortus virulence regulates the expression of outer membrane proteins with counterparts in members of the Rhizobiaceae. Proceedings of the National Academy of Sciences of the United States of America. 2002; 99(19); 12375-12380. [PubMed: 12218183].