ALSB_ECOLI
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 03-AUG-2022, entry version 160.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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 (1.8 ANGSTROMS).
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}.
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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_SSZK01000016.1.
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 PDBsum; 1GUB; -.
DR PDBsum; 1GUD; -.
DR PDBsum; 1RPJ; -.
DR AlphaFoldDB; P39265; -.
DR BMRB; P39265; -.
DR SMR; P39265; -.
DR BioGRID; 4262681; 15.
DR BioGRID; 852897; 2.
DR ComplexPortal; CPX-4320; D-allose ABC transporter complex.
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; P39265; -.
DR PRIDE; P39265; -.
DR EnsemblBacteria; AAC77049; AAC77049; b4088.
DR EnsemblBacteria; BAE78091; BAE78091; BAE78091.
DR GeneID; 948604; -.
DR KEGG; ecj:JW4049; -.
DR KEGG; eco:b4088; -.
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; IYAANEP; -.
DR PhylomeDB; P39265; -.
DR BioCyc; EcoCyc:YJCX-MON; -.
DR BioCyc; MetaCyc:YJCX-MON; -.
DR BRENDA; 7.5.2.8; 2026.
DR EvolutionaryTrace; P39265; -.
DR PRO; PR:P39265; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC: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:allose transmembrane transport; IC:ComplexPortal.
DR GO; GO:0015752; P:D-ribose transmembrane transport; IC:ComplexPortal.
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 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..260
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
