SBPA_AZOBR
ID SBPA_AZOBR Reviewed; 357 AA.
AC P54083;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=Multiple sugar-binding periplasmic protein SbpA;
DE Short=Sugar-binding protein A;
DE Flags: Precursor;
GN Name=sbpA;
OS Azospirillum brasilense.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=192;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 83-101 AND 164-169,
RP AND FUNCTION IN CHEMOTAXIS TOWARDS SUGARS.
RC STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RX PubMed=10361275; DOI=10.1046/j.1365-2958.1999.01384.x;
RA Van Bastelaere E., Lambrecht M., Vermeiren H., Van Dommelen A., Keijers V.,
RA Proost P., Vanderleyden J.;
RT "Characterization of a sugar-binding protein from Azospirillum brasilense
RT mediating chemotaxis to and uptake of sugars.";
RL Mol. Microbiol. 32:703-714(1999).
CC -!- FUNCTION: Mediates chemotaxis towards D-galactose, L-arabinose and D-
CC fucose but not towards D-fructose. Probably part of a binding-protein
CC high affinity uptake system. {ECO:0000269|PubMed:10361275}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC -!- INDUCTION: Induced by D-galactose, L-arabinose and D-fucose. Not
CC induced by stress conditions such as nitrogen limitation, osmotic
CC stress, salt stress or temperature stress.
CC -!- MISCELLANEOUS: SbpA from A.brasilense cannot complement an
CC Agrobacterium chvE mutant with regard to vir gene expression.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 2 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U40823; AAA86621.1; -; Genomic_DNA.
DR AlphaFoldDB; P54083; -.
DR SMR; P54083; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR025997; SBP_2_dom.
DR Pfam; PF13407; Peripla_BP_4; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
PE 1: Evidence at protein level;
KW Chemotaxis; Direct protein sequencing; Periplasm; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..357
FT /note="Multiple sugar-binding periplasmic protein SbpA"
FT /id="PRO_0000031742"
SQ SEQUENCE 357 AA; 38247 MW; 99C077E5648347BB CRC64;
MSSSFTTTLA GMAVGMLVLA TGTNPTLAQD KPTVGIAMPT KSSARWIDDG NNMVKQFQAK
GYKTDLQYAE DDIPNQLAQI ETMVAKNSKV LVIAAIDGTT LTDVLQQAKD RGVKVIAYDR
LIRGSENVDY YATFDNFQVG VLQGSYIVDA LGLKDGKGPF NIELFGGSPD DNNAYFFYNG
AMSVLQPYID SGKLTVGSGQ VGMDKVSTLR WDGATAQARM DNLLSAFYGN RRVDAVLSPY
DGISIGIISS LKGVGYGSPS QPMPVVTGQD AEVPSIKSIL AGEQRATVFK DTRELARITV
EMVDAVLGGG TAVNDTKTYD NGKKVVPAYL LKPVSVDASN WKGTLVDSGY YTEAQFK