LAMB1_AERS4
ID LAMB1_AERS4 Reviewed; 428 AA.
AC A4SNG2;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Maltoporin 1 {ECO:0000255|HAMAP-Rule:MF_01301};
DE AltName: Full=Maltose-inducible porin 1 {ECO:0000255|HAMAP-Rule:MF_01301};
DE Flags: Precursor;
GN Name=lamB1 {ECO:0000255|HAMAP-Rule:MF_01301}; OrderedLocusNames=ASA_2388;
OS Aeromonas salmonicida (strain A449).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=382245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A449;
RX PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J.,
RA Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C.,
RA Brown L.L.;
RT "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into
RT the evolution of a fish pathogen.";
RL BMC Genomics 9:427-427(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; CP000644; ABO90434.1; -; Genomic_DNA.
DR AlphaFoldDB; A4SNG2; -.
DR SMR; A4SNG2; -.
DR STRING; 382245.ASA_2388; -.
DR EnsemblBacteria; ABO90434; ABO90434; ASA_2388.
DR KEGG; asa:ASA_2388; -.
DR eggNOG; COG4580; Bacteria.
DR HOGENOM; CLU_032473_4_1_6; -.
DR OMA; YYTYASW; -.
DR Proteomes; UP000000225; 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..428
FT /note="Maltoporin 1"
FT /id="PRO_0000322009"
FT SITE 31
FT /note="Greasy slide, important in sugar transport"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01301"
FT SITE 62
FT /note="Greasy slide, important in sugar transport"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01301"
FT SITE 427
FT /note="Greasy slide, important in sugar transport"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01301"
SQ SEQUENCE 428 AA; 46921 MW; 8DC0653F3150FAFC CRC64;
MTMKVKLLTT SVALALSMTA FSSNAVDFSG YFRSGVGVSQ DGDMQTGNQS LVGRLGNESD
TYTEIGIGQE VYNKDGKVFY VDSMFSMQSN GSNDYESTAT VCDFDKKQCS EDATFALRQF
NVKAKGLISA APDAVVWAGK RFYQRHDLHI IDTKYWNISG AGAGIENLKA GPGAFSLAWI
RSDGNDIDNS IVDNDLNVNF LDLRYAGWAP WEGAWTEAGV SYAMPNPTDE QKATGGKYDP
ENGVMLTAEM SQYFAGSGIN EKLVLQYANK GLAQNMISQG GGWYDVWQLT DDAKGYRVIL
TGDIPLGDKF SVNHVFTYGK GEKLQEWHDN TELFSAVARG GYAWTDIMKT LVEAGTYEST
KTWTSGAEDK SSGQKYTLAQ AWSAGPSMFA RPEIRVFASY LKDGEGESFN GGEDDSTWNF
GVQAEAWW
