ID   LAMB_SALPK              Reviewed;         452 AA.
AC   B5BJV4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 71.
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=SSPA3757;
OS   Salmonella paratyphi A (strain AKU_12601).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=554290;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AKU_12601;
RX   PubMed=19159446; DOI=10.1186/1471-2164-10-36;
RA   Holt K.E., Thomson N.R., Wain J., Langridge G.C., Hasan R., Bhutta Z.A.,
RA   Quail M.A., Norbertczak H., Walker D., Simmonds M., White B., Bason N.,
RA   Mungall K., Dougan G., Parkhill J.;
RT   "Pseudogene accumulation in the evolutionary histories of Salmonella
RT   enterica serovars Paratyphi A and Typhi.";
RL   BMC Genomics 10:36-36(2009).
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; FM200053; CAR62041.1; -; Genomic_DNA.
DR   RefSeq; WP_000973684.1; NC_011147.1.
DR   AlphaFoldDB; B5BJV4; -.
DR   SMR; B5BJV4; -.
DR   KEGG; sek:SSPA3757; -.
DR   HOGENOM; CLU_032473_4_1_6; -.
DR   OMA; DYGRANA; -.
DR   Proteomes; UP000001869; 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; Ion transport; Membrane; Porin; Signal;
KW   Sugar transport; Transmembrane; Transmembrane beta strand; Transport.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01301"
FT   CHAIN           26..452
FT                   /note="Maltoporin"
FT                   /id="PRO_1000140493"
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"
SQ   SEQUENCE   452 AA;  50558 MW;  462B60F8ACDC387B CRC64;
     MMITLRKLPL AVAVAAGVMS AQAMAVDFHG YARSGIGWTG SGGEQQCFQV TGAQSKYRLG
     NECETYAELK LGQEVWKEGD KSFYFDTNVA YSVNQQNDWE STDPAFREAN VQGKNLIEWL
     PGSTIWAGKR FYQRHDVHMI DFYYWDISGP GAGIENIDLG FGKLSLAATR STEAGGSYTF
     SSQNIYDEVK DTANDVFDVR LAGLQTNPDG VLELGVDYGR ANTTDGYKLV DGASKDGWMF
     TAEHTQSMLK GYNKFVVQYA TDAMTTQGKG QARGSDGSSS FTEELPDGTK INYANKVINN
     NGDMWRILDH GAISLGDKWG LMYVGMYQNI DWDNNLGTEW WTVGVRPMYK WTPIMSTLLE
     VGYDNVKSQQ TGDRNNQYKI TLAQQWQAGD SIWSRPAIRI FATYAKWDEK WGYIKDGDNI
     SRYAAATNSG ISTNSRGDSD EWTFGAQMEI WW