LAMB_ECOLI
ID LAMB_ECOLI Reviewed; 446 AA.
AC P02943; Q2M6R8;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Maltoporin {ECO:0000255|HAMAP-Rule:MF_01301};
DE AltName: Full=Maltose outer membrane channel {ECO:0000305};
DE AltName: Full=Maltose-inducible porin {ECO:0000255|HAMAP-Rule:MF_01301};
DE AltName: Full=Phage lambda receptor protein {ECO:0000303|PubMed:4201774};
DE Flags: Precursor;
GN Name=lamB {ECO:0000255|HAMAP-Rule:MF_01301}; Synonyms=malB;
GN OrderedLocusNames=b4036, JW3996;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=6086106; DOI=10.1016/0092-8674(81)90392-5;
RA Clement J.M., Hofnung M.;
RT "Gene sequence of the lambda receptor, an outer membrane protein of E. coli
RT K12.";
RL Cell 27:507-514(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-156, FUNCTION, AND MUTAGENESIS OF
RP ARG-33; TRP-99; ARG-107; TYR-143 AND ASP-146.
RX PubMed=3301537; DOI=10.1016/0378-1119(87)90018-7;
RA Heine H.G., Kyngdon J., Ferenci T.;
RT "Sequence determinants in the lamB gene of Escherichia coli influencing the
RT binding and pore selectivity of maltoporin.";
RL Gene 53:287-292(1987).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-35.
RX PubMed=161974;
RA Clement J.M., Hedgpeth J., Hofnung M., Jacob F.;
RT "DNA sequence encoding the signal peptide of the lambda receptor in E. coli
RT K 12.";
RL C. R. Hebd. Seances Acad. Sci., D, Sci. Nat. 289:1033-1036(1979).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-35.
RX PubMed=6446717; DOI=10.1073/pnas.77.5.2621;
RA Hedgpeth J., Clement J.M., Marchal C., Perrin D., Hofnung M.;
RT "DNA sequence encoding the NH2-terminal peptide involved in transport of
RT lambda receptor, an Escherichia coli secretory protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 77:2621-2625(1980).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 26-446, FUNCTION, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF ARG-33; SER-34; PRO-104; TYR-143; GLY-219;
RP ARG-385; PRO-386 AND 445-TRP-TRP-446.
RC STRAIN=Hfr G6;
RX PubMed=2832377; DOI=10.1128/jb.170.4.1730-1738.1988;
RA Heine H.G., Francis G., Lee K.S., Ferenci T.;
RT "Genetic analysis of sequences in maltoporin that contribute to binding
RT domains and pore structure.";
RL J. Bacteriol. 170:1730-1738(1988).
RN [9]
RP PROTEIN SEQUENCE OF 26-32, SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=Hfr G6;
RA Endermann R., Hindennach I., Henning U.;
RT "Major proteins of the Escherichia coli outer cell envelope membrane.";
RL FEBS Lett. 88:71-74(1978).
RN [10]
RP IDENTIFICATION AS PHAGE LAMBDA RECEPTOR, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=Hfr G6;
RX PubMed=4201774; DOI=10.1128/jb.116.3.1436-1446.1973;
RA Randall-Hazelbauer L., Schwartz M.;
RT "Isolation of the bacteriophage lambda receptor from Escherichia coli.";
RL J. Bacteriol. 116:1436-1446(1973).
RN [11]
RP SUBUNIT, SUBCELLULAR LOCATION, DISULFIDE BOND, AND MUTAGENESIS OF CYS-47
RP AND CYS-63.
RX PubMed=1988451; DOI=10.1016/s0021-9258(18)52373-5;
RA Luckey M., Ling R., Dose A., Malloy B.;
RT "Role of a disulfide bond in the thermal stability of the LamB protein
RT trimer in Escherichia coli outer membrane.";
RL J. Biol. Chem. 266:1866-1871(1991).
RN [12]
RP TOPOLOGY.
RX PubMed=1702781; DOI=10.1128/jb.173.1.262-275.1991;
RA Charbit A., Ronco J., Michel V., Werts C., Hofnung M.;
RT "Permissive sites and topology of an outer membrane protein with a reporter
RT epitope.";
RL J. Bacteriol. 173:262-275(1991).
RN [13]
RP TOPOLOGY.
RX PubMed=7925308; DOI=10.1002/j.1460-2075.1994.tb06790.x;
RA Klebba P.E., Hofnung M., Charbit A.;
RT "A model of maltodextrin transport through the sugar-specific porin, LamB,
RT based on deletion analysis.";
RL EMBO J. 13:4670-4675(1994).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS), FUNCTION, AND MUTAGENESIS OF
RP ARG-134; TYR-143 AND ASP-146.
RX PubMed=11742115; DOI=10.1093/protein/14.11.943;
RA Van Gelder P., Dutzler R., Dumas F., Koebnik R., Schirmer T.;
RT "Sucrose transport through maltoporin mutants of Escherichia coli.";
RL Protein Eng. 14:943-948(2001).
RN [15]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=BL21-DE3;
RX PubMed=16079137; DOI=10.1074/jbc.m506479200;
RA Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA von Heijne G., Daley D.O.;
RT "Protein complexes of the Escherichia coli cell envelope.";
RL J. Biol. Chem. 280:34409-34419(2005).
RN [16] {ECO:0007744|PDB:1MAL}
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS), FUNCTION, SUBUNIT, DISULFIDE BOND,
RP AND TOPOLOGY.
RX PubMed=7824948; DOI=10.1126/science.7824948;
RA Schirmer T., Keller T.A., Wang Y.-F., Rosenbusch J.P.;
RT "Structural basis for sugar translocation through maltoporin channels at
RT 3.1-A resolution.";
RL Science 267:512-514(1995).
RN [17] {ECO:0007744|PDB:1MPM, ECO:0007744|PDB:1MPN, ECO:0007744|PDB:1MPO}
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 26-446 IN COMPLEX WITH VARIOUS
RP SUBSTRATES, FUNCTION, AND SUBUNIT.
RX PubMed=8805519; DOI=10.1016/s0969-2126(96)00016-0;
RA Dutzler R., Wang Y.-F., Rizkallah P., Rosenbusch J.P., Schirmer T.;
RT "Crystal structures of various maltooligosaccharides bound to maltoporin
RT reveal a specific sugar translocation pathway.";
RL Structure 4:127-134(1996).
RN [18] {ECO:0007744|PDB:1AF6, ECO:0007744|PDB:1MPQ}
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 26-446 IN COMPLEX WITH FRUCTOSE
RP AND GLUCOSE, FUNCTION, AND SUBUNIT.
RX PubMed=9299337; DOI=10.1006/jmbi.1997.1224;
RA Wang Y.-F., Dutzler R., Rizkallah P.J., Rosenbusch J.P., Schirmer T.;
RT "Channel specificity: structural basis for sugar discrimination and
RT differential flux rates in maltoporin.";
RL J. Mol. Biol. 272:56-63(1997).
CC -!- FUNCTION: Involved in the transport of maltose and maltodextrins
CC (PubMed:3301537, PubMed:2832377, PubMed:11742115, PubMed:7824948,
CC PubMed:8805519, PubMed:9299337). Indispensable for translocation of
CC maltodextrins (alpha 1-4 linked polyglucosyls) containing more than
CC three glucosyl moieties. A hydrophobic path ('greasy slide') of
CC aromatic residues serves to guide and select the sugars for transport
CC through the channel (PubMed:7824948, PubMed:8805519, PubMed:9299337,
CC PubMed:11742115). Also acts as a receptor for several bacteriophages
CC including lambda (PubMed:4201774). Binds maltosaccharides; when LamB
CC binds starch in soft agar, it inhibits motility (PubMed:2832377).
CC {ECO:0000269|PubMed:11742115, ECO:0000269|PubMed:2832377,
CC ECO:0000269|PubMed:3301537, ECO:0000269|PubMed:4201774,
CC ECO:0000269|PubMed:7824948, ECO:0000269|PubMed:8805519,
CC ECO:0000269|PubMed:9299337}.
CC -!- SUBUNIT: Homotrimer formed of three 18-stranded antiparallel beta-
CC barrels, containing three independent channels (PubMed:1988451,
CC PubMed:16079137, PubMed:7824948, PubMed:8805519, PubMed:9299337) (By
CC similarity). An intrasubunit disulfide bond contributes to trimer
CC stability (PubMed:1988451). {ECO:0000255|HAMAP-Rule:MF_01301,
CC ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:1988451,
CC ECO:0000269|PubMed:7824948, ECO:0000269|PubMed:8805519,
CC ECO:0000269|PubMed:9299337}.
CC -!- INTERACTION:
CC P02943; P10408: secA; NbExp=3; IntAct=EBI-371309, EBI-543213;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_01301, ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:1988451,
CC ECO:0000269|PubMed:4201774, ECO:0000269|Ref.9}; Multi-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_01301, ECO:0000269|PubMed:16079137}.
CC -!- INDUCTION: By maltose. {ECO:0000255|HAMAP-Rule:MF_01301,
CC ECO:0000269|Ref.9}.
CC -!- DISRUPTION PHENOTYPE: Resistance to phage lambda (PubMed:4201774). No
CC growth on dextrins (PubMed:2832377). {ECO:0000269|PubMed:2832377,
CC ECO:0000269|PubMed:4201774}.
CC -!- SIMILARITY: Belongs to the porin LamB (TC 1.B.3) family.
CC {ECO:0000255|HAMAP-Rule:MF_01301}.
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DR EMBL; M16643; AAA24059.1; -; Genomic_DNA.
DR EMBL; M26131; AAA24060.1; -; Genomic_DNA.
DR EMBL; V00298; CAA23575.1; -; Genomic_DNA.
DR EMBL; J01648; AAB59058.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43130.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77006.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78038.1; -; Genomic_DNA.
DR EMBL; M24997; AAC41396.1; -; Genomic_DNA.
DR EMBL; V00297; CAA23574.1; -; Genomic_DNA.
DR PIR; A03443; QRECL.
DR RefSeq; NP_418460.1; NC_000913.3.
DR RefSeq; WP_000973663.1; NZ_SSZK01000016.1.
DR PDB; 1AF6; X-ray; 2.40 A; A/B/C=26-446.
DR PDB; 1MAL; X-ray; 3.10 A; A/B/C=26-446.
DR PDB; 1MPM; X-ray; 2.60 A; A/B/C=26-446.
DR PDB; 1MPN; X-ray; 3.20 A; A/B/C=26-446.
DR PDB; 1MPO; X-ray; 2.80 A; A/B/C=26-446.
DR PDB; 1MPQ; X-ray; 3.00 A; A/B/C=26-446.
DR PDBsum; 1AF6; -.
DR PDBsum; 1MAL; -.
DR PDBsum; 1MPM; -.
DR PDBsum; 1MPN; -.
DR PDBsum; 1MPO; -.
DR PDBsum; 1MPQ; -.
DR AlphaFoldDB; P02943; -.
DR SMR; P02943; -.
DR BioGRID; 4262663; 259.
DR DIP; DIP-10082N; -.
DR IntAct; P02943; 3.
DR STRING; 511145.b4036; -.
DR DrugBank; DB02379; Beta-D-Glucose.
DR DrugBank; DB04173; Fructose.
DR TCDB; 1.B.3.1.1; the sugar porin (sp) family.
DR jPOST; P02943; -.
DR PaxDb; P02943; -.
DR PRIDE; P02943; -.
DR EnsemblBacteria; AAC77006; AAC77006; b4036.
DR EnsemblBacteria; BAE78038; BAE78038; BAE78038.
DR GeneID; 948548; -.
DR KEGG; ecj:JW3996; -.
DR KEGG; eco:b4036; -.
DR PATRIC; fig|1411691.4.peg.2674; -.
DR EchoBASE; EB0523; -.
DR eggNOG; COG4580; Bacteria.
DR HOGENOM; CLU_032473_4_1_6; -.
DR OMA; DYGRANA; -.
DR PhylomeDB; P02943; -.
DR BioCyc; EcoCyc:EG10528-MON; -.
DR BioCyc; MetaCyc:EG10528-MON; -.
DR EvolutionaryTrace; P02943; -.
DR PRO; PR:P02943; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
DR GO; GO:0045203; C:integral component of cell outer membrane; IDA:EcoCyc.
DR GO; GO:0046930; C:pore complex; IDA:EcoCyc.
DR GO; GO:0015144; F:carbohydrate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042958; F:maltodextrin transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0015481; F:maltose transporting porin activity; IEA:InterPro.
DR GO; GO:0015288; F:porin activity; IDA:CACAO.
DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0042956; P:maltodextrin transmembrane transport; IDA:EcoCyc.
DR GO; GO:0015774; P:polysaccharide transport; IBA:GO_Central.
DR CDD; cd01346; Maltoporin-like; 1.
DR Gene3D; 2.40.170.10; -; 1.
DR HAMAP; MF_01301; LamB; 1.
DR InterPro; IPR023738; Maltoporin.
DR InterPro; IPR003192; Porin_LamB.
DR InterPro; IPR036998; Porin_LamB_sf.
DR Pfam; PF02264; LamB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Direct protein sequencing;
KW Disulfide bond; Host cell receptor for virus entry; Host-virus interaction;
KW Ion transport; Membrane; Porin; Receptor; Reference proteome; Signal;
KW Sugar transport; Transmembrane; Transmembrane beta strand; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|Ref.9"
FT CHAIN 26..446
FT /note="Maltoporin"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01301"
FT /id="PRO_0000025175"
FT TOPO_DOM 26
FT /note="Periplasmic"
FT TRANSMEM 27..40
FT /note="Beta stranded"
FT TOPO_DOM 41..64
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:7824948"
FT TRANSMEM 65..75
FT /note="Beta stranded"
FT TOPO_DOM 76..81
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:7824948"
FT TRANSMEM 82..93
FT /note="Beta stranded"
FT TOPO_DOM 94..104
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:7824948"
FT TRANSMEM 105..115
FT /note="Beta stranded"
FT TOPO_DOM 116..122
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:7824948"
FT TRANSMEM 123..130
FT /note="Beta stranded"
FT TOPO_DOM 131..156
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:7824948"
FT TRANSMEM 157..159
FT /note="Beta stranded"
FT TOPO_DOM 160..161
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:7824948"
FT TRANSMEM 162..173
FT /note="Beta stranded"
FT TOPO_DOM 174..191
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:7824948"
FT TRANSMEM 192..204
FT /note="Beta stranded"
FT TOPO_DOM 205..208
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:7824948"
FT TRANSMEM 209..222
FT /note="Beta stranded"
FT TOPO_DOM 223..234
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:7824948"
FT TRANSMEM 235..248
FT /note="Beta stranded"
FT TOPO_DOM 249..250
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:7824948"
FT TRANSMEM 251..263
FT /note="Beta stranded"
FT TOPO_DOM 264..290
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:7824948"
FT TRANSMEM 291..305
FT /note="Beta stranded"
FT TOPO_DOM 306..307
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:7824948"
FT TRANSMEM 308..323
FT /note="Beta stranded"
FT TOPO_DOM 324..326
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:7824948"
FT TRANSMEM 327..341
FT /note="Beta stranded"
FT TOPO_DOM 342..344
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:7824948"
FT TRANSMEM 345..359
FT /note="Beta stranded"
FT TOPO_DOM 360..362
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:7824948"
FT TRANSMEM 363..376
FT /note="Beta stranded"
FT TOPO_DOM 377..386
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:7824948"
FT TRANSMEM 387..399
FT /note="Beta stranded"
FT TOPO_DOM 400..430
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:7824948"
FT TRANSMEM 431..445
FT /note="Beta stranded"
FT TOPO_DOM 446
FT /note="Periplasmic"
FT SITE 31
FT /note="Greasy slide, important in sugar transport"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01301,
FT ECO:0000269|PubMed:7824948, ECO:0000269|PubMed:8805519"
FT SITE 66
FT /note="Greasy slide, important in sugar transport"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01301,
FT ECO:0000269|PubMed:7824948, ECO:0000269|PubMed:8805519"
FT SITE 99
FT /note="Greasy slide, important in sugar transport"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01301,
FT ECO:0000269|PubMed:7824948, ECO:0000269|PubMed:8805519"
FT SITE 143
FT /note="Important in sugar transport"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01301,
FT ECO:0000269|PubMed:8805519"
FT SITE 252
FT /note="Greasy slide, important in sugar transport"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01301,
FT ECO:0000269|PubMed:7824948, ECO:0000269|PubMed:8805519"
FT SITE 383
FT /note="Greasy slide, important in sugar transport"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01301,
FT ECO:0000269|PubMed:7824948, ECO:0000269|PubMed:8805519"
FT SITE 445
FT /note="Greasy slide, important in sugar transport"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01301,
FT ECO:0000269|PubMed:7824948, ECO:0000269|PubMed:8805519"
FT DISULFID 47..63
FT /evidence="ECO:0000269|PubMed:1988451,
FT ECO:0000305|PubMed:7824948"
FT MUTAGEN 33
FT /note="R->H: In lamB1040; reduces ligand affinity and pore
FT size, no longer selective for maltodextrins. Reduced starch
FT binding, grows on maltodextrins, no change in phage lambda
FT binding."
FT /evidence="ECO:0000269|PubMed:2832377,
FT ECO:0000269|PubMed:3301537"
FT MUTAGEN 34
FT /note="S->SGS: In lamB375; decreased protein at 37 but not
FT 30 degrees Celsius, reduced starch binding, no growth on
FT dextrins, decreased affinity for maltose, loss of phage
FT lambda binding."
FT /evidence="ECO:0000269|PubMed:2832377"
FT MUTAGEN 47
FT /note="C->S: Normal transport activity, assembled trimer is
FT less stable."
FT /evidence="ECO:0000269|PubMed:1988451"
FT MUTAGEN 63
FT /note="C->S: Normal transport activity, assembled trimer is
FT less stable."
FT /evidence="ECO:0000269|PubMed:1988451"
FT MUTAGEN 99
FT /note="W->R: Decreases starch affinity, slightly increases
FT maltose affinity."
FT /evidence="ECO:0000269|PubMed:3301537"
FT MUTAGEN 104
FT /note="P->PDP: In lamB147; decreased affinity for maltose,
FT grows on maltodextrins, no change in phage lambda binding."
FT /evidence="ECO:0000269|PubMed:2832377"
FT MUTAGEN 107
FT /note="R->S: Decreases maltodextrin affinity, increases
FT sucrose binding and transport."
FT /evidence="ECO:0000269|PubMed:3301537"
FT MUTAGEN 134
FT /note="R->A: Considerable increase in pore size and sucrose
FT transport, slight decrease in maltose transport; when
FT associated with A-143."
FT /evidence="ECO:0000269|PubMed:11742115"
FT MUTAGEN 134
FT /note="R->D,N: Slight increase in pore size; increase in
FT sucrose transport and slight decrease in maltose transport;
FT when associated with D-143 and F-146."
FT /evidence="ECO:0000269|PubMed:11742115"
FT MUTAGEN 143
FT /note="Y->F: Increases affinity for starch and maltose,
FT pore size and transport of maltohexaose."
FT /evidence="ECO:0000269|PubMed:11742115,
FT ECO:0000269|PubMed:3301537"
FT MUTAGEN 143
FT /note="Y->YY: In lamB203; reduced starch binding, no
FT maltose transport, no growth on dextrins, decreased protein
FT in outer membrane at 37 but not 30 degrees Celsius, no
FT change in phage lambda binding."
FT /evidence="ECO:0000269|PubMed:2832377"
FT MUTAGEN 146
FT /note="D->G: Increases affinity for large dextrins."
FT /evidence="ECO:0000269|PubMed:11742115,
FT ECO:0000269|PubMed:3301537"
FT MUTAGEN 219
FT /note="G->D: In lamB1002; decreased affinity for maltose,
FT loss of phage lambda binding."
FT /evidence="ECO:0000269|PubMed:2832377"
FT MUTAGEN 385
FT /note="R->C: In lamb1004; reduced starch binding, decreased
FT affinity for maltose, no change in phage lambda binding."
FT /evidence="ECO:0000269|PubMed:2832377"
FT MUTAGEN 386
FT /note="P->PDP: In lamB146; loss of starch binding, grows
FT poorly on maltodextrins, reduced affinity for somaltose."
FT /evidence="ECO:0000269|PubMed:2832377"
FT MUTAGEN 445..446
FT /note="Missing: In lamB1007; significantly less protein in
FT outer membrane, no growth on dextrins, reduced
FT susceptibility to phage lambda."
FT /evidence="ECO:0000269|PubMed:2832377"
FT CONFLICT 381
FT /note="S -> T (in Ref. 2; AAC43130)"
FT /evidence="ECO:0000305"
FT STRAND 27..39
FT /evidence="ECO:0007829|PDB:1AF6"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1AF6"
FT STRAND 64..78
FT /evidence="ECO:0007829|PDB:1AF6"
FT STRAND 81..93
FT /evidence="ECO:0007829|PDB:1AF6"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:1AF6"
FT STRAND 105..115
FT /evidence="ECO:0007829|PDB:1AF6"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:1MPQ"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:1AF6"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:1AF6"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:1AF6"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:1AF6"
FT STRAND 149..158
FT /evidence="ECO:0007829|PDB:1AF6"
FT STRAND 160..180
FT /evidence="ECO:0007829|PDB:1AF6"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:1AF6"
FT STRAND 190..207
FT /evidence="ECO:0007829|PDB:1AF6"
FT STRAND 210..221
FT /evidence="ECO:0007829|PDB:1AF6"
FT STRAND 236..248
FT /evidence="ECO:0007829|PDB:1AF6"
FT STRAND 251..261
FT /evidence="ECO:0007829|PDB:1AF6"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:1AF6"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:1AF6"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:1AF6"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:1AF6"
FT STRAND 292..305
FT /evidence="ECO:0007829|PDB:1AF6"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:1AF6"
FT STRAND 309..322
FT /evidence="ECO:0007829|PDB:1AF6"
FT STRAND 328..358
FT /evidence="ECO:0007829|PDB:1AF6"
FT TURN 359..361
FT /evidence="ECO:0007829|PDB:1AF6"
FT STRAND 364..381
FT /evidence="ECO:0007829|PDB:1AF6"
FT STRAND 387..403
FT /evidence="ECO:0007829|PDB:1AF6"
FT TURN 409..411
FT /evidence="ECO:0007829|PDB:1AF6"
FT TURN 413..416
FT /evidence="ECO:0007829|PDB:1AF6"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:1AF6"
FT HELIX 423..425
FT /evidence="ECO:0007829|PDB:1AF6"
FT STRAND 432..446
FT /evidence="ECO:0007829|PDB:1AF6"
SQ SEQUENCE 446 AA; 49912 MW; B2D4E4F120DA494E CRC64;
MMITLRKLPL AVAVAAGVMS AQAMAVDFHG YARSGIGWTG SGGEQQCFQT TGAQSKYRLG
NECETYAELK LGQEVWKEGD KSFYFDTNVA YSVAQQNDWE ATDPAFREAN VQGKNLIEWL
PGSTIWAGKR FYQRHDVHMI DFYYWDISGP GAGLENIDVG FGKLSLAATR SSEAGGSSSF
ASNNIYDYTN ETANDVFDVR LAQMEINPGG TLELGVDYGR ANLRDNYRLV DGASKDGWLF
TAEHTQSVLK GFNKFVVQYA TDSMTSQGKG LSQGSGVAFD NEKFAYNINN NGHMLRILDH
GAISMGDNWD MMYVGMYQDI NWDNDNGTKW WTVGIRPMYK WTPIMSTVME IGYDNVESQR
TGDKNNQYKI TLAQQWQAGD SIWSRPAIRV FATYAKWDEK WGYDYTGNAD NNANFGKAVP
ADFNGGSFGR GDSDEWTFGA QMEIWW
