LAMB_SALTI
ID LAMB_SALTI Reviewed; 452 AA.
AC Q8Z1T9;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 124.
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};
GN OrderedLocusNames=STY4427, t4137;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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; AL513382; CAD09215.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO71601.1; -; Genomic_DNA.
DR RefSeq; NP_458529.1; NC_003198.1.
DR RefSeq; WP_000973678.1; NZ_WSUR01000027.1.
DR AlphaFoldDB; Q8Z1T9; -.
DR SMR; Q8Z1T9; -.
DR STRING; 220341.16505219; -.
DR EnsemblBacteria; AAO71601; AAO71601; t4137.
DR KEGG; stt:t4137; -.
DR KEGG; sty:STY4427; -.
DR PATRIC; fig|220341.7.peg.4527; -.
DR eggNOG; COG4580; Bacteria.
DR HOGENOM; CLU_032473_4_1_6; -.
DR OMA; DYGRANA; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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 3: Inferred from homology;
KW Cell outer membrane; Disulfide bond; Ion transport; Membrane; Porin;
KW Signal; Sugar transport; Transmembrane; Transmembrane beta strand;
KW Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01301"
FT CHAIN 26..452
FT /note="Maltoporin"
FT /id="PRO_0000025179"
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..300
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 301..315
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TOPO_DOM 316..317
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 318..333
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TOPO_DOM 334..336
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 337..351
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TOPO_DOM 352..353
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 354..369
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TOPO_DOM 370..372
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 373..388
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TOPO_DOM 389..395
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 396..410
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TOPO_DOM 411..436
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 437..451
FT /note="Beta stranded"
FT /evidence="ECO:0000250"
FT TOPO_DOM 452
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 393
FT /note="Greasy slide, important in sugar transport"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01301"
FT SITE 451
FT /note="Greasy slide, important in sugar transport"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01301"
FT DISULFID 47..63
FT /evidence="ECO:0000250"
SQ SEQUENCE 452 AA; 50588 MW; C4BFB8CA1218C2C2 CRC64;
MMITLRKLPL AVAVAAGVMS AQAMAVDFHG YARSGIGWTG SGGEQQCFQV TGAQSKYRLG
NECETYAELK LGQEVWKEGD KSFYFDTNVA YSVNQQNDWE STDPAFREAN VQGKNLIEWL
PGSTIWAGKR FYQRHDVHMI DFYYWDISGP GAGIENIDLG FGKLSLAATR STEAGGSYTF
SSQNIYDEVK DTANDVFDVR LAGLQTNPDG VLELGVDYGR ANTTDGYKLA DGASKDGWMF
TAEHTQSMLK GYNKFVVQYA TDAMTTQGKG QARGSDGSSS FTEELPDGTK INYANKVINN
NGDMWRILDH GAISLGDKWD LMYVGMYQNI DWDNNLGTEW WTVGVRPMYK WTPIMSTLLE
VGYDNVKSQQ TGDRNNQYKI TLAQQWQAGD SIWSRPAIRI FATYAKWDEK WGYIKDGDNI
SRYAAATNSG ISTNSRGDSD EWTFGAQMEI WW
