LAMB_ECOL6
ID LAMB_ECOL6 Reviewed; 446 AA.
AC Q8CVI4;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Maltoporin {ECO:0000255|HAMAP-Rule:MF_01301};
DE AltName: Full=Maltose-inducible porin {ECO:0000255|HAMAP-Rule:MF_01301};
DE Flags: Precursor;
GN Name=lamB {ECO:0000255|HAMAP-Rule:MF_01301}; OrderedLocusNames=c5006;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: Involved in the transport of maltose and maltodextrins.
CC {ECO:0000255|HAMAP-Rule:MF_01301}.
CC -!- SUBUNIT: Homotrimer formed of three 18-stranded antiparallel beta-
CC barrels, containing three independent channels. {ECO:0000255|HAMAP-
CC Rule:MF_01301}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC Rule:MF_01301}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01301}.
CC -!- INDUCTION: By maltose. {ECO:0000255|HAMAP-Rule:MF_01301}.
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; AE014075; AAN83432.1; -; Genomic_DNA.
DR RefSeq; WP_000973666.1; NC_004431.1.
DR PDB; 2VDA; NMR; -; B=1-25.
DR PDBsum; 2VDA; -.
DR AlphaFoldDB; Q8CVI4; -.
DR SMR; Q8CVI4; -.
DR STRING; 199310.c5006; -.
DR EnsemblBacteria; AAN83432; AAN83432; c5006.
DR KEGG; ecc:c5006; -.
DR eggNOG; COG4580; Bacteria.
DR HOGENOM; CLU_032473_4_1_6; -.
DR OMA; DYGRANA; -.
DR BioCyc; ECOL199310:C5006-MON; -.
DR EvolutionaryTrace; Q8CVI4; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
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:0006811; P:ion transport; IEA:UniProtKB-KW.
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; Signal; Sugar transport; Transmembrane; Transmembrane beta strand;
KW Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01301"
FT CHAIN 26..446
FT /note="Maltoporin"
FT /id="PRO_0000025176"
FT TOPO_DOM 26
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 27..35
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TOPO_DOM 36..64
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 65..78
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TOPO_DOM 79..80
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 81..93
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TOPO_DOM 94..104
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 105..115
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TOPO_DOM 116..122
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 123..130
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TOPO_DOM 131..148
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 149..159
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TOPO_DOM 160..161
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 162..173
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TOPO_DOM 174..191
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 192..205
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TOPO_DOM 206..209
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 210..222
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TOPO_DOM 223..234
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 235..248
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TOPO_DOM 249..250
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 251..263
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TOPO_DOM 264..290
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 291..305
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TOPO_DOM 306..307
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 308..323
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TOPO_DOM 324..326
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 327..341
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TOPO_DOM 342..343
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 344..359
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TOPO_DOM 360..362
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 363..378
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TOPO_DOM 379..385
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 386..400
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TOPO_DOM 401..430
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 431..445
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TOPO_DOM 446
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT SITE 31
FT /note="Greasy slide, important in sugar transport"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01301"
FT SITE 66
FT /note="Greasy slide, important in sugar transport"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01301"
FT SITE 99
FT /note="Greasy slide, important in sugar transport"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01301"
FT SITE 143
FT /note="Important in sugar transport"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01301"
FT SITE 252
FT /note="Greasy slide, important in sugar transport"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01301"
FT SITE 383
FT /note="Greasy slide, important in sugar transport"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01301"
FT SITE 445
FT /note="Greasy slide, important in sugar transport"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01301"
FT DISULFID 47..63
FT /evidence="ECO:0000250"
FT HELIX 10..17
FT /evidence="ECO:0007829|PDB:2VDA"
SQ SEQUENCE 446 AA; 49941 MW; 66AD83740268B030 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 WGYDYTGSSS TNPYYGKAVS
ADFNGGSFGR GDSDEWTFGA QMEIWW
