LAMB_VIBC3
ID LAMB_VIBC3 Reviewed; 416 AA.
AC A5F137; C3M6W8;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 84.
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}; Synonyms=ompS;
GN OrderedLocusNames=VC0395_0213, VC395_A1051;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
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; CP000626; ABQ19267.1; -; Genomic_DNA.
DR EMBL; CP001236; ACP11881.1; -; Genomic_DNA.
DR RefSeq; WP_001882819.1; NZ_CP045718.1.
DR AlphaFoldDB; A5F137; -.
DR SMR; A5F137; -.
DR STRING; 345073.VC395_A1051; -.
DR EnsemblBacteria; ABQ19267; ABQ19267; VC0395_0213.
DR KEGG; vco:VC0395_0213; -.
DR KEGG; vcr:VC395_A1051; -.
DR PATRIC; fig|345073.21.peg.3774; -.
DR eggNOG; COG4580; Bacteria.
DR HOGENOM; CLU_032473_4_1_6; -.
DR OMA; DYGRANA; -.
DR Proteomes; UP000000249; Chromosome 1.
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..26
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01301"
FT CHAIN 27..416
FT /note="Maltoporin"
FT /id="PRO_0000322015"
FT SITE 32
FT /note="Greasy slide, important in sugar transport"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01301"
FT SITE 64
FT /note="Greasy slide, important in sugar transport"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01301"
FT SITE 96
FT /note="Greasy slide, important in sugar transport"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01301"
FT SITE 140
FT /note="Important in sugar transport"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01301"
FT SITE 231
FT /note="Greasy slide, important in sugar transport"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01301"
FT SITE 378
FT /note="Greasy slide, important in sugar transport"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01301"
FT SITE 415
FT /note="Greasy slide, important in sugar transport"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01301"
SQ SEQUENCE 416 AA; 45011 MW; 168B2BA308E5B26D CRC64;
MELTMKKVSV IAAAVAATLA AGSAFAVDFN GYFRAGTGIS GNGNADQAVN KAGTGRLGNE
NDNYYEFGFA EELKTGEQTW KVESMIAQGN SGANGWEDGD FNVAQFNVQA KGLLASDQEA
VMWAGKRYYQ RKDIHITDFY FLNTSGTGGG IENLSVGNQK LSVALVQDGD NTNSSGYIFD
ARLANIGLWE NASLELAMAY NFATEKDSKN EVADDGVLVS AILHQGLSNG FNQTVFQYGT
AGYGAQAANF WGAGSYYARG TEAFNDASGF RLLNWGVINL GENWEMGHQL AYLAGSDIGG
QFGGDGANKN TYTGKSFDID QYSVVVRPMY KWNDTMRTVF EAGYNAGEKI SNGGLATEDF
GNAKFTVAQA WAMGDSFWAR PELRVYGTYL LDTENDKAFG DDDTEFVVGI QVEAWW