LAMB_SALTY
ID LAMB_SALTY Reviewed; 452 AA.
AC P26466;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Maltoporin;
DE AltName: Full=Maltose-inducible porin;
DE Flags: Precursor;
GN Name=lamB; Synonyms=malL {ECO:0000303|PubMed:1730061};
GN OrderedLocusNames=STM4231;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=1730061; DOI=10.1016/0167-4781(92)90492-i;
RA Schneider E., Francoz E., Dassa E.;
RT "Completion of the nucleotide sequence of the 'maltose B' region in
RT Salmonella typhimurium: the high conservation of the malM gene suggests a
RT selected physiological role for its product.";
RL Biochim. Biophys. Acta 1129:223-227(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=LT2;
RX PubMed=2092357; DOI=10.1016/0923-2508(90)90078-5;
RA Francoz E., Molla A., Dassa E., Saurin W., Hofnung M.;
RT "The maltoporin of Salmonella typhimurium: sequence and folding model.";
RL Res. Microbiol. 141:1039-1059(1990).
RN [3]
RP SEQUENCE REVISION TO 427.
RA Dassa E.;
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 26-452 WITH AND WITHOUT SUBSTRATE,
RP SUBUNIT, TOPOLOGY, AND DISULFIDE BOND.
RX PubMed=9102468; DOI=10.1006/jmbi.1996.0823;
RA Meyer J.E.W., Hofnung M., Schulz G.E.;
RT "Structure of maltoporin from Salmonella typhimurium ligated with a
RT nitrophenyl-maltotrioside.";
RL J. Mol. Biol. 266:761-775(1997).
CC -!- FUNCTION: Involved in the transport of maltose and maltodextrins. Does
CC not act as a receptor for phages. {ECO:0000305|PubMed:1730061}.
CC -!- SUBUNIT: Homotrimer formed of three 18-stranded antiparallel beta-
CC barrels, containing three independent channels.
CC {ECO:0000269|PubMed:9102468}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein.
CC -!- INDUCTION: By maltose. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the porin LamB (TC 1.B.3) family. {ECO:0000305}.
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DR EMBL; X54292; CAA38187.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL23055.1; -; Genomic_DNA.
DR PIR; A60177; A60177.
DR RefSeq; NP_463096.1; NC_003197.2.
DR RefSeq; WP_000973645.1; NC_003197.2.
DR PDB; 1MPR; X-ray; 2.80 A; A/B/C=26-452.
DR PDB; 2MPR; X-ray; 2.40 A; A/B/C=26-452.
DR PDBsum; 1MPR; -.
DR PDBsum; 2MPR; -.
DR AlphaFoldDB; P26466; -.
DR SMR; P26466; -.
DR STRING; 99287.STM4231; -.
DR DrugBank; DB02379; Beta-D-Glucose.
DR PaxDb; P26466; -.
DR EnsemblBacteria; AAL23055; AAL23055; STM4231.
DR GeneID; 1255757; -.
DR KEGG; stm:STM4231; -.
DR PATRIC; fig|99287.12.peg.4451; -.
DR HOGENOM; CLU_032473_4_1_6; -.
DR OMA; DYGRANA; -.
DR PhylomeDB; P26466; -.
DR BioCyc; SENT99287:STM4231-MON; -.
DR EvolutionaryTrace; P26466; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0045203; C:integral component of cell outer membrane; IBA:GO_Central.
DR GO; GO:0046930; C:pore complex; IBA:GO_Central.
DR GO; GO:0015144; F:carbohydrate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042958; F:maltodextrin transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015481; F:maltose transporting porin activity; IEA:InterPro.
DR GO; GO:0015288; F:porin activity; IBA:GO_Central.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
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; Disulfide bond; Ion transport; Membrane;
KW Porin; Reference proteome; Signal; Sugar transport; Transmembrane;
KW Transmembrane beta strand; Transport.
FT SIGNAL 1..25
FT CHAIN 26..452
FT /note="Maltoporin"
FT /id="PRO_0000025180"
FT TOPO_DOM 26
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:9102468"
FT TRANSMEM 27..35
FT /note="Beta stranded"
FT /evidence="ECO:0000305|PubMed:9102468"
FT TOPO_DOM 36..64
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:9102468"
FT TRANSMEM 65..78
FT /note="Beta stranded"
FT /evidence="ECO:0000305|PubMed:9102468"
FT TOPO_DOM 79..80
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:9102468"
FT TRANSMEM 81..93
FT /note="Beta stranded"
FT /evidence="ECO:0000305|PubMed:9102468"
FT TOPO_DOM 94..104
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:9102468"
FT TRANSMEM 105..115
FT /note="Beta stranded"
FT /evidence="ECO:0000305|PubMed:9102468"
FT TOPO_DOM 116..122
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:9102468"
FT TRANSMEM 123..130
FT /note="Beta stranded"
FT /evidence="ECO:0000305|PubMed:9102468"
FT TOPO_DOM 131..148
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:9102468"
FT TRANSMEM 149..159
FT /note="Beta stranded"
FT /evidence="ECO:0000305|PubMed:9102468"
FT TOPO_DOM 160..161
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:9102468"
FT TRANSMEM 162..173
FT /note="Beta stranded"
FT /evidence="ECO:0000305|PubMed:9102468"
FT TOPO_DOM 174..191
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:9102468"
FT TRANSMEM 192..205
FT /note="Beta stranded"
FT /evidence="ECO:0000305|PubMed:9102468"
FT TOPO_DOM 206..209
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:9102468"
FT TRANSMEM 210..222
FT /note="Beta stranded"
FT /evidence="ECO:0000305|PubMed:9102468"
FT TOPO_DOM 223..234
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:9102468"
FT TRANSMEM 235..248
FT /note="Beta stranded"
FT /evidence="ECO:0000305|PubMed:9102468"
FT TOPO_DOM 249..250
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:9102468"
FT TRANSMEM 251..263
FT /note="Beta stranded"
FT /evidence="ECO:0000305|PubMed:9102468"
FT TOPO_DOM 264..300
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:9102468"
FT TRANSMEM 301..315
FT /note="Beta stranded"
FT /evidence="ECO:0000305|PubMed:9102468"
FT TOPO_DOM 316..317
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:9102468"
FT TRANSMEM 318..333
FT /note="Beta stranded"
FT /evidence="ECO:0000305|PubMed:9102468"
FT TOPO_DOM 334..336
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:9102468"
FT TRANSMEM 337..351
FT /note="Beta stranded"
FT /evidence="ECO:0000305|PubMed:9102468"
FT TOPO_DOM 352..353
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:9102468"
FT TRANSMEM 354..369
FT /note="Beta stranded"
FT /evidence="ECO:0000305|PubMed:9102468"
FT TOPO_DOM 370..372
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:9102468"
FT TRANSMEM 373..388
FT /note="Beta stranded"
FT /evidence="ECO:0000305|PubMed:9102468"
FT TOPO_DOM 389..395
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:9102468"
FT TRANSMEM 396..410
FT /note="Beta stranded"
FT /evidence="ECO:0000305|PubMed:9102468"
FT TOPO_DOM 411..436
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:9102468"
FT TRANSMEM 437..451
FT /note="Beta stranded"
FT /evidence="ECO:0000305|PubMed:9102468"
FT TOPO_DOM 452
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:9102468"
FT BINDING 134..143
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:9102468"
FT SITE 31
FT /note="Greasy slide, important in sugar transport"
FT /evidence="ECO:0000269|PubMed:9102468"
FT SITE 66
FT /note="Greasy slide, important in sugar transport"
FT /evidence="ECO:0000269|PubMed:9102468"
FT SITE 99
FT /note="Greasy slide, important in sugar transport"
FT /evidence="ECO:0000269|PubMed:9102468"
FT SITE 143
FT /note="Important in sugar transport"
FT /evidence="ECO:0000269|PubMed:9102468"
FT SITE 252
FT /note="Greasy slide, important in sugar transport"
FT /evidence="ECO:0000269|PubMed:9102468"
FT SITE 393
FT /note="Greasy slide, important in sugar transport"
FT /evidence="ECO:0000269|PubMed:9102468"
FT SITE 451
FT /note="Greasy slide, important in sugar transport"
FT /evidence="ECO:0000269|PubMed:9102468"
FT DISULFID 47..63
FT /evidence="ECO:0000269|PubMed:9102468"
FT STRAND 27..39
FT /evidence="ECO:0007829|PDB:2MPR"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:2MPR"
FT STRAND 64..78
FT /evidence="ECO:0007829|PDB:2MPR"
FT STRAND 81..93
FT /evidence="ECO:0007829|PDB:2MPR"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:2MPR"
FT STRAND 105..115
FT /evidence="ECO:0007829|PDB:2MPR"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:2MPR"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:2MPR"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:2MPR"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:2MPR"
FT STRAND 149..158
FT /evidence="ECO:0007829|PDB:2MPR"
FT STRAND 160..182
FT /evidence="ECO:0007829|PDB:2MPR"
FT STRAND 185..207
FT /evidence="ECO:0007829|PDB:2MPR"
FT STRAND 210..222
FT /evidence="ECO:0007829|PDB:2MPR"
FT STRAND 236..248
FT /evidence="ECO:0007829|PDB:2MPR"
FT STRAND 251..261
FT /evidence="ECO:0007829|PDB:2MPR"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:2MPR"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:2MPR"
FT TURN 274..277
FT /evidence="ECO:0007829|PDB:2MPR"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:2MPR"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:2MPR"
FT STRAND 302..315
FT /evidence="ECO:0007829|PDB:2MPR"
FT TURN 316..318
FT /evidence="ECO:0007829|PDB:2MPR"
FT STRAND 319..332
FT /evidence="ECO:0007829|PDB:2MPR"
FT STRAND 338..352
FT /evidence="ECO:0007829|PDB:2MPR"
FT STRAND 355..368
FT /evidence="ECO:0007829|PDB:2MPR"
FT TURN 369..371
FT /evidence="ECO:0007829|PDB:2MPR"
FT STRAND 374..391
FT /evidence="ECO:0007829|PDB:2MPR"
FT STRAND 396..416
FT /evidence="ECO:0007829|PDB:2MPR"
FT STRAND 419..431
FT /evidence="ECO:0007829|PDB:2MPR"
FT STRAND 438..451
FT /evidence="ECO:0007829|PDB:2MPR"
SQ SEQUENCE 452 AA; 50549 MW; E5148050ECABF063 CRC64;
MMITLRKLPL AVAVAAGVMS AQAMAVDFHG YARSGIGWTG SGGEQQCFQA TGAQSKYRLG
NECETYAELK LGQEVWKEGD KSFYFDTNVA YSVNQQNDWE STDPAFREAN VQGKNLIEWL
PGSTIWAGKR FYQRHDVHMI DFYYWDISGP GAGIENIDLG FGKLSLAATR STEAGGSYTF
SSQNIYDEVK DTANDVFDVR LAGLQTNPDG VLELGVDYGR ANTTDGYKLA DGASKDGWMF
TAEHTQSMLK GYNKFVVQYA TDAMTTQGKG QARGSDGSSS FTEELSDGTK INYANKVINN
NGNMWRILDH GAISLGDKWD LMYVGMYQNI DWDNNLGTEW WTVGVRPMYK WTPIMSTLLE
VGYDNVKSQQ TGDRNNQYKI TLAQQWQAGD SIWSRPAIRI FATYAKWDEK WGYIKDGDNI
SRYAAATNSG ISTNSRGDSD EWTFGAQMEI WW
