ID ALSB_ECOLI Reviewed; 311 AA. AC P39265; Q2M6L5; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 04-NOV-2026, entry version 176. DE RecName: Full=D-allose-binding periplasmic protein; DE Short=ALBP; DE Flags: Precursor; GN Name=alsB; Synonyms=yjcX; OrderedLocusNames=b4088, JW4049; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=7610040; DOI=10.1093/nar/23.12.2105; RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.; RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region RT from 92.8 through 100 minutes."; RL Nucleic Acids Res. 23:2105-2119(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-130. RC STRAIN=K12; RX PubMed=8576032; DOI=10.1128/jb.178.4.1003-1011.1996; RA Soerensen K.I., Hove-Jensen B.; RT "Ribose catabolism of Escherichia coli: characterization of the rpiB gene RT encoding ribose phosphate isomerase B and of the rpiR gene, which is RT involved in regulation of rpiB expression."; RL J. Bacteriol. 178:1003-1011(1996). RN [5] RP FUNCTION. RX PubMed=9401019; DOI=10.1128/jb.179.24.7631-7637.1997; RA Kim C., Song S., Park C.; RT "The D-allose operon of Escherichia coli K-12."; RL J. Bacteriol. 179:7631-7637(1997). RN [6] RP X-RAY CRYSTALLOGRAPHY. RX PubMed=10064713; DOI=10.1006/jmbi.1999.2571; RA Chaudhuri B.N., Ko J., Park C., Jones T.A., Mowbray S.L.; RT "Structure of D-allose binding protein from Escherichia coli bound to D- RT allose at 1.8-A resolution."; RL J. Mol. Biol. 286:1519-1531(1999). CC -!- FUNCTION: Part of the binding protein-dependent transport system AlsBAC CC for D-allose. {ECO:0000269|PubMed:9401019}. CC -!- SUBCELLULAR LOCATION: Periplasm. 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; U14003; AAA96987.1; -; Genomic_DNA. DR EMBL; U00096; AAC77049.1; -; Genomic_DNA. DR EMBL; AP009048; BAE78091.1; -; Genomic_DNA. DR EMBL; X82203; CAA57686.1; -; Genomic_DNA. DR PIR; S56316; S56316. DR RefSeq; NP_418512.1; NC_000913.3. DR RefSeq; WP_001046187.1; NZ_CP009789.1. DR PDB; 1GUB; X-ray; 3.10 A; A=24-311. DR PDB; 1GUD; X-ray; 1.70 A; A/B=24-311. DR PDB; 1RPJ; X-ray; 1.80 A; A=24-311. DR AlphaFoldDB; P39265; -. DR BMRB; P39265; -. DR MDposit; P39265; -. DR MDRepo; P39265; -. DR SMR; P39265; -. DR BioGRID; 4262681; 18. DR BioGRID; 852897; 2. DR ComplexPortal; CPX-4320; D-allose ABC transporter complex. DR FunCoup; P39265; 407. DR IntAct; P39265; 7. DR STRING; 511145.b4088; -. DR DrugBank; DB03989; D-Allopyranose. DR TCDB; 3.A.1.2.6; the atp-binding cassette (abc) superfamily. DR jPOST; P39265; -. DR PaxDb; 511145-b4088; -. DR EnsemblBacteria; AAC77049; AAC77049; b4088. DR GeneID; 948604; -. DR KEGG; ecj:JW4049; -. DR KEGG; eco:b4088; -. DR KEGG; ecoc:C3026_22100; -. DR PATRIC; fig|1411691.4.peg.2612; -. DR EchoBASE; EB2352; -. DR eggNOG; COG1879; Bacteria. DR HOGENOM; CLU_037628_3_2_6; -. DR InParanoid; P39265; -. DR OMA; AEMPLIT; -. DR OrthoDB; 9773673at2; -. DR PhylomeDB; P39265; -. DR BioCyc; EcoCyc:YJCX-MONOMER; -. DR BioCyc; MetaCyc:YJCX-MONOMER; -. DR BRENDA; 7.5.2.8; 2026. DR EvolutionaryTrace; P39265; -. DR PRO; PR:P39265; -. DR Proteomes; UP000000625; Chromosome. DR AbasyAtlas; P39265; -. DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; NAS:ComplexPortal. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc. DR GO; GO:0048029; F:monosaccharide binding; IPI:EcoCyc. DR GO; GO:0015754; P:D-allose transmembrane transport; EXP:EcoCyc. DR GO; GO:0015752; P:D-ribose transmembrane transport; NAS:ComplexPortal. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. DR CDD; cd06320; PBP1_allose_binding; 1. DR FunFam; 3.40.50.2300:FF:000198; D-allose-binding periplasmic protein (ALBP); 1. DR Gene3D; 3.40.50.2300; -; 2. DR InterPro; IPR028082; Peripla_BP_I. DR InterPro; IPR025997; SBP_2_dom. DR NCBIfam; NF007254; alsB; 1. DR PANTHER; PTHR46847; D-ALLOSE-BINDING PERIPLASMIC PROTEIN-RELATED; 1. DR PANTHER; PTHR46847:SF1; D-ALLOSE-BINDING PERIPLASMIC PROTEIN-RELATED; 1. DR Pfam; PF13407; Peripla_BP_4; 1. DR SUPFAM; SSF53822; Periplasmic binding protein-like I; 1. PE 1: Evidence at protein level; KW 3D-structure; Periplasm; Reference proteome; Signal; Sugar transport; KW Transport. FT SIGNAL 1..23 FT CHAIN 24..311 FT /note="D-allose-binding periplasmic protein" FT /id="PRO_0000031719" FT CONFLICT 16 FT /note="M -> I (in Ref. 4; CAA57686)" FT /evidence="ECO:0000305" FT CONFLICT 125..130 FT /note="AGGNVE -> LAQCGS (in Ref. 4; CAA57686)" FT /evidence="ECO:0000305" FT STRAND 26..32 FT /evidence="ECO:0007829|PDB:1GUD" FT STRAND 34..36 FT /evidence="ECO:0007829|PDB:1GUD" FT HELIX 37..53 FT /evidence="ECO:0007829|PDB:1GUD" FT STRAND 57..61 FT /evidence="ECO:0007829|PDB:1GUD" FT HELIX 68..79 FT /evidence="ECO:0007829|PDB:1GUD" FT STRAND 81..88 FT /evidence="ECO:0007829|PDB:1GUD" FT STRAND 91..94 FT /evidence="ECO:0007829|PDB:1GUD" FT HELIX 97..105 FT /evidence="ECO:0007829|PDB:1GUD" FT STRAND 109..115 FT /evidence="ECO:0007829|PDB:1GUD" FT HELIX 119..124 FT /evidence="ECO:0007829|PDB:1GUD" FT STRAND 130..134 FT /evidence="ECO:0007829|PDB:1GUD" FT HELIX 137..152 FT /evidence="ECO:0007829|PDB:1GUD" FT HELIX 153..155 FT /evidence="ECO:0007829|PDB:1GUD" FT STRAND 157..163 FT /evidence="ECO:0007829|PDB:1GUD" FT HELIX 169..183 FT /evidence="ECO:0007829|PDB:1GUD" FT STRAND 188..195 FT /evidence="ECO:0007829|PDB:1GUD" FT HELIX 200..213 FT /evidence="ECO:0007829|PDB:1GUD" FT STRAND 219..224 FT /evidence="ECO:0007829|PDB:1GUD" FT HELIX 225..237 FT /evidence="ECO:0007829|PDB:1GUD" FT TURN 241..243 FT /evidence="ECO:0007829|PDB:1GUD" FT STRAND 244..250 FT /evidence="ECO:0007829|PDB:1GUD" FT HELIX 253..261 FT /evidence="ECO:0007829|PDB:1GUD" FT STRAND 266..269 FT /evidence="ECO:0007829|PDB:1GUD" FT HELIX 272..288 FT /evidence="ECO:0007829|PDB:1GUD" FT STRAND 295..297 FT /evidence="ECO:0007829|PDB:1GUB" FT STRAND 300..303 FT /evidence="ECO:0007829|PDB:1GUD" FT STRAND 307..309 FT /evidence="ECO:0007829|PDB:1GUD" SQ SEQUENCE 311 AA; 32910 MW; 1A60E05BD1846068 CRC64; MNKYLKYFSG TLVGLMLSTS AFAAAEYAVV LKTLSNPFWV DMKKGIEDEA KTLGVSVDIF ASPSEGDFQS QLQLFEDLSN KNYKGIAFAP LSSVNLVMPV ARAWKKGIYL VNLDEKIDMD NLKKAGGNVE AFVTTDNVAV GAKGASFIID KLGAEGGEVA IIEGKAGNAS GEARRNGATE AFKKASQIKL VASQPADWDR IKALDVATNV LQRNPNIKAI YCANDTMAMG VAQAVANAGK TGKVLVVGTD GIPEARKMVE AGQMTATVAQ NPADIGATGL KLMVDAEKSG KVIPLDKAPE FKLVDSILVT Q //