(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Bacteria: NE > Terrabacteria group: NE > Firmicutes: NE > Bacilli: NE > Lactobacillales: NE > Streptococcaceae: NE > Streptococcus: NE > Streptococcus agalactiae: NE
Warning: This entry is a compilation of different species or line or strain with more than 90% amino acide identity. You can retrieve all strain data
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) Streptococcus agalactiae COH1: N, E.
Streptococcus agalactiae serogroup III: N, E.
Streptococcus agalactiae serogroup V: N, E.
Streptococcus agalactiae serogroup Ia: N, E.
Streptococcus agalactiae 18RS21: N, E.
Streptococcus agalactiae 515: N, E.
Streptococcus agalactiae CJB111: N, E.
Streptococcus agalactiae H36B: N, E.
Streptococcus agalactiae ATCC 13813: N, E.
Streptococcus agalactiae 2603V/R: N, E.
Streptococcus agalactiae NEM316: N, E.
Streptococcus agalactiae FSL S3-026: N, E.
Streptococcus agalactiae FSL S3-170: N, E.
Streptococcus agalactiae FSL C1-494: N, E.
Streptococcus agalactiae FSL C1-487: N, E.
Streptococcus agalactiae FSL S3-586: N, E.
Streptococcus agalactiae FSL S3-251: N, E.
Streptococcus agalactiae MRI Z1-213: N, E.
Streptococcus agalactiae MRI Z1-214: N, E.
Streptococcus agalactiae MRI Z1-216: N, E.
Streptococcus agalactiae MRI Z1-217: N, E.
Streptococcus sp. HMSC069D09: N, E.
Molecular evidence
Database
No mutation 1 structure: 6OYC: Glycosylation Associate Protein (Gap123) complex from Streptococcus agalactiae (protein2 is Asp2) No kinetic
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MSKIKLTILQVGEENWATKENIPNNMEWLFIKPDQISDFVTTENNYLTSS KLLQKLPRKISALLLTEQTYGPELSSLSSFFEVYEVFYPKDKHATGITEE FLRSKMAQRYDSSSPDQLIRQFYKGLFIGQYGEKLQVSQIQIRNDFEGVV NYQGNNYLELEGQFGENYSFLLNFAYNIPFSSDFYNELFLEHIIEGDIDI RLVISLIVDGSVDDIAKEWYFEKEDLNQLISLESDISGSLAVKLFAKGKG IVKLGPLHRRNGRGGLGTFLLGGERHIDAIGHEFMTYFDPVDFKPPLTVY FSGFRSAEGFEGFWMMKSMKTPFMLICDPRLQGGAFYIGSKEYEQKIVDA IQEKLAFLNFSSDQLILSGLSMGTYGATYHGAKLNPHAIIIGKPIFNLGT VAQRERLERPDGFATSLDIQLLNQGDLTSSSSEKLNNYFWKSIEEGDFSN TTFALAYMKNDDYDATAFSDLLQYFRGKKHKILGRGWDGRHGDCSAEVGA WFTSQYRRMLSNDFGRKEE
The human and bovine bacterial pathogen Streptococcus agalactiae (Group B Streptococcus, GBS) expresses a thick polysaccharide capsule that constitutes a major virulence factor and vaccine target. GBS can be classified into ten distinct serotypes differing in the chemical composition of their capsular polysaccharide. However, non-typeable strains that do not react with anti-capsular sera are frequently isolated from colonized and infected humans and cattle. To gain a comprehensive insight into the molecular basis for the loss of capsule expression in GBS, a collection of well-characterized non-typeable strains was investigated by genome sequencing. Genome based phylogenetic analysis extended to a wide population of sequenced strains confirmed the recently observed high clonality among GBS lineages mainly containing human strains, and revealed a much higher degree of diversity in the bovine population. Remarkably, non-typeable strains were equally distributed in all lineages. A number of distinct mutations in the cps operon were identified that were apparently responsible for inactivation of capsule synthesis. The most frequent genetic alterations were point mutations leading to stop codons in the cps genes, and the main target was found to be cpsE encoding the portal glycosyl transferase of capsule biosynthesis. Complementation of strains carrying missense mutations in cpsE with a wild-type gene restored capsule expression allowing the identification of amino acid residues essential for enzyme activity.
Three vancomycin-resistant streptococcal strains carrying vanG elements (two invasive Streptococcus agalactiae isolates [GBS-NY and GBS-NM, both serotype II and multilocus sequence type 22] and one Streptococcus anginosus [Sa]) were examined. The 45,585-bp elements found within Sa and GBS-NY were nearly identical (together designated vanG-1) and shared near-identity over an ~15-kb overlap with a previously described vanG element from Enterococcus faecalis. Unexpectedly, vanG-1 shared much less homology with the 49,321-bp vanG-2 element from GBS-NM, with widely different levels (50% to 99%) of sequence identity shared among 44 related open reading frames. Immediately adjacent to both vanG-1 and vanG-2 were 44,670-bp and 44,680-bp integrative conjugative element (ICE)-like sequences, designated ICE-r, that were nearly identical in the two group B streptococcal (GBS) strains. The dual vanG and ICE-r elements from both GBS strains were inserted at the same position, between bases 1328 and 1329, within the identical RNA methyltransferase (rumA) genes. A GenBank search revealed that although most GBS strains contained insertions within this specific site, only sequence type 22 (ST22) GBS strains contained highly related ICE-r derivatives. The vanG-1 element in Sa was also inserted within this position corresponding to its rumA homolog adjacent to an ICE-r derivative. vanG-1 insertions were previously reported within the same relative position in the E. faecalis rumA homolog. An ICE-r sequence perfectly conserved with respect to its counterpart in GBS-NY was apparent within the same site of the rumA homolog of a Streptococcus dysgalactiae subsp. equisimilis strain. Additionally, homologous vanG-like elements within the conserved rumA target site were evident in Roseburia intestinalis. Importance: These three streptococcal strains represent the first known vancomycin-resistant strains of their species. The collective observations made from these strains reveal a specific hot spot for insertional elements that is conserved between streptococci and different Gram-positive species. The two GBS strains potentially represent a GBS lineage that is predisposed to insertion of vanG elements.
Streptococcus agalactiae. Uncharacterized protein
