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LAMB_ECO57
ID   LAMB_ECO57              Reviewed;         446 AA.
AC   Q8X5W7;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 127.
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=malB;
GN   OrderedLocusNames=Z5634, ECs5019;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Involved in the transport of maltose and maltodextrins,
CC       indispensable for translocation of dextrins containing more than three
CC       glucosyl moieties. A hydrophobic path ('greasy slide') of aromatic
CC       residues serves to guide and select the sugars for transport through
CC       the channel (By similarity). {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; AE005174; AAG59235.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB38442.1; -; Genomic_DNA.
DR   PIR; C91256; C91256.
DR   PIR; G86096; G86096.
DR   RefSeq; NP_313046.1; NC_002695.1.
DR   RefSeq; WP_000973673.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; Q8X5W7; -.
DR   SMR; Q8X5W7; -.
DR   STRING; 155864.EDL933_5373; -.
DR   EnsemblBacteria; AAG59235; AAG59235; Z5634.
DR   EnsemblBacteria; BAB38442; BAB38442; ECs_5019.
DR   GeneID; 914315; -.
DR   KEGG; ece:Z5634; -.
DR   KEGG; ecs:ECs_5019; -.
DR   PATRIC; fig|386585.9.peg.5242; -.
DR   eggNOG; COG4580; Bacteria.
DR   HOGENOM; CLU_032473_4_1_6; -.
DR   OMA; DYGRANA; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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   Reference proteome; Signal; Sugar transport; Transmembrane;
KW   Transmembrane beta strand; Transport.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01301"
FT   CHAIN           26..446
FT                   /note="Maltoporin"
FT                   /id="PRO_0000025177"
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"
SQ   SEQUENCE   446 AA;  49968 MW;  BAC6EC4264D9068B CRC64;
     MMITLRKLPL AVAVAAGVMS AQAMAVDFHG YARSGIGWTG SGGEQQCFQT TGAQSKYRLG
     NECETYAELK LGQEVWKEGD KSFYFDTNVA YSVAQQNDWE ATDPAFREAN VQGKNLIEWL
     PGSTIWAGKR FYQRHDVHMI DFYYWDISGP GAGLENIDVG FGKLSLAATR SSEAGGSSSF
     ASNNIYDYTN ETANDVFDVR LAQMEVNPGG TLELGVDYGR ANLRDNYRLV DGASKDGWLF
     TAEHTQSVLK GFNKFVVQYA TDSMTSQGKG LSQGSGVAFD NEKFAYNINN NGHMLRILDH
     GAISMGDNWD MMYVGMYQDI NWDNDNGTKW WTVGIRPMYK WTPIMSTVME IGYDNVESQR
     TGDKNNQYKI TLAQQWQAGD SIWSRPAIRV FATYAKWDEK WGYDYNGDSK VNPNYGKAVP
     ADFNGGSFGR GDSDEWTFGA QMEIWW
 
 
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