Align BusAA, component of Uptake system for glycine-betaine (high affinity) and proline (low affinity) (OpuAA-OpuABC) or BusAA-ABC of Lactococcus lactis). BusAA, the ATPase subunit, has a C-terminal tandem cystathionine β-synthase (CBS) domain which is the cytoplasmic K+ sensor for osmotic stress (osmotic strength)while the BusABC subunit has the membrane and receptor domains fused to each other (Biemans-Oldehinkel et al., 2006; Mahmood et al., 2006; Gul et al. 2012). An N-terminal amphipathic α-helix of OpuA is necessary for high activity but is not critical for biogenesis or the ionic regulation of transport (characterized)
to candidate WP_022669727.1 G415_RS0101055 nitrate/sulfonate/bicarbonate ABC transporter ATP-binding protein
Query= TCDB::Q9RQ06 (407 letters) >NCBI__GCF_000420385.1:WP_022669727.1 Length = 424 Score = 152 bits (385), Expect = 1e-41 Identities = 102/284 (35%), Positives = 160/284 (56%), Gaps = 43/284 (15%) Query: 5 VKIEHLTKIFGKRIKTALTMVEQGEPKNEILKKTGATVGVYDTNFEINEGEIFVIMGLSG 64 +K+E++ IF +LT++E + + I EG+I I+G SG Sbjct: 4 IKLENINMIFPISKSESLTVLE-------------------NISLSIEEGKIVSILGPSG 44 Query: 65 SGKSTLLRLLNRLIEPTSGKIFIDDQDVATLNKEDLLQVRRKSMSMVFQNFGLFPHRTIL 124 GKSTLLR++ L++PT GK+F + + +N + M+MVFQNF LFP +T+ Sbjct: 45 CGKSTLLRIITGLLKPTKGKVFYKGKVQSGVNDK---------MAMVFQNFALFPWKTVW 95 Query: 125 ENTEYGL---EVQNVPKEERRKRAEKALDNANLLDFKDQYPKQLSGGMQQRVGLARALAN 181 +N G+ E++N K+E KR +D L F+D YPK LSGGM+QRVG+ARAL + Sbjct: 96 DNIAIGIRNREIRN--KDEMIKRV---IDIVGLEGFEDVYPKSLSGGMKQRVGIARALVS 150 Query: 182 DPEILLMDEAFSALDPLIRREMQDELLEL---QAKFQKTIIFVSHDLNEALRIGDRIAIM 238 +PEIL MDE FSALD L +++EL++L + K I+ V+H++ EA+ + D I IM Sbjct: 151 NPEILCMDEPFSALDVLTAENLREELMDLWLSRKTSLKGIVIVTHNITEAVYMSDEIIIM 210 Query: 239 --KDGKIMQIGTGEEILTNPANDYVKTFVEDVDRAKVITAENIM 280 + G++ + + L+ P + F++ VD + +NI+ Sbjct: 211 ASRPGRVQLVYKNK--LSYPRDQNSADFLKIVDAIRNYLTKNII 252 Lambda K H 0.316 0.135 0.364 Gapped Lambda K H 0.267 0.0410 0.140 Matrix: BLOSUM62 Gap Penalties: Existence: 11, Extension: 1 Number of Sequences: 1 Number of Hits to DB: 414 Number of extensions: 21 Number of successful extensions: 3 Number of sequences better than 1.0e-02: 1 Number of HSP's gapped: 1 Number of HSP's successfully gapped: 1 Length of query: 407 Length of database: 424 Length adjustment: 31 Effective length of query: 376 Effective length of database: 393 Effective search space: 147768 Effective search space used: 147768 Neighboring words threshold: 11 Window for multiple hits: 40 X1: 16 ( 7.3 bits) X2: 38 (14.6 bits) X3: 64 (24.7 bits) S1: 41 (21.6 bits) S2: 50 (23.9 bits)
This GapMind analysis is from Apr 09 2024. The underlying query database was built on Sep 17 2021.
Each pathway is defined by a set of rules based on individual steps or genes. Candidates for each step are identified by using ublast (a fast alternative to protein BLAST) against a database of manually-curated proteins (most of which are experimentally characterized) or by using HMMer with enzyme models (usually from TIGRFam). Ublast hits may be split across two different proteins.
A candidate for a step is "high confidence" if either:
Otherwise, a candidate is "medium confidence" if either:
Other blast hits with at least 50% coverage are "low confidence."
Steps with no high- or medium-confidence candidates may be considered "gaps." For the typical bacterium that can make all 20 amino acids, there are 1-2 gaps in amino acid biosynthesis pathways. For diverse bacteria and archaea that can utilize a carbon source, there is a complete high-confidence catabolic pathway (including a transporter) just 38% of the time, and there is a complete medium-confidence pathway 63% of the time. Gaps may be due to:
GapMind relies on the predicted proteins in the genome and does not search the six-frame translation. In most cases, you can search the six-frame translation by clicking on links to Curated BLAST for each step definition (in the per-step page).
For more information, see:
If you notice any errors or omissions in the step descriptions, or any questionable results, please let us know
by Morgan Price, Arkin group, Lawrence Berkeley National Laboratory