ID G8PQB1_PSEUV Unreviewed; 389 AA.
AC G8PQB1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Maltodextrin-binding protein {ECO:0000256|ARBA:ARBA00030303, ECO:0000256|RuleBase:RU365005};
GN Name=malE {ECO:0000313|EMBL:AEV38425.1};
GN OrderedLocusNames=PSE_3921 {ECO:0000313|EMBL:AEV38425.1};
OS Pseudovibrio sp. (strain FO-BEG1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Stappiaceae; Pseudovibrio.
OX NCBI_TaxID=911045 {ECO:0000313|EMBL:AEV38425.1, ECO:0000313|Proteomes:UP000005634};
RN [1] {ECO:0000313|Proteomes:UP000005634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FO-BEG1 {ECO:0000313|Proteomes:UP000005634};
RA Bondarev V., Richter M., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT "The genus Pseudovibrio contains metabolically versatile and symbiotically
RT interacting bacteria.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEV38425.1, ECO:0000313|Proteomes:UP000005634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FO-BEG1 {ECO:0000313|EMBL:AEV38425.1,
RC ECO:0000313|Proteomes:UP000005634};
RX PubMed=23601235; DOI=10.1111/1462-2920.12123;
RA Bondarev V., Richter M., Romano S., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT "The genus Pseudovibrio contains metabolically versatile bacteria adapted
RT for symbiosis.";
RL Environ. Microbiol. 15:2095-2113(2013).
CC -!- FUNCTION: Part of the ABC transporter complex MalEFGK involved in
CC maltose/maltodextrin import. Binds maltose and higher maltodextrins.
CC {ECO:0000256|RuleBase:RU365005}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418,
CC ECO:0000256|RuleBase:RU365005}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 1 family.
CC {ECO:0000256|ARBA:ARBA00008520, ECO:0000256|RuleBase:RU365005}.
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DR EMBL; CP003147; AEV38425.1; -; Genomic_DNA.
DR RefSeq; WP_014286330.1; NC_016642.1.
DR AlphaFoldDB; G8PQB1; -.
DR STRING; 911045.PSE_3921; -.
DR KEGG; psf:PSE_3921; -.
DR eggNOG; COG2182; Bacteria.
DR HOGENOM; CLU_031285_17_0_5; -.
DR Proteomes; UP000005634; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0015144; F:carbohydrate transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR006060; Maltose/Cyclodextrin-bd.
DR InterPro; IPR006059; SBP.
DR InterPro; IPR006061; SBP_1_CS.
DR PANTHER; PTHR30061; MALTOSE-BINDING PERIPLASMIC PROTEIN; 1.
DR PANTHER; PTHR30061:SF50; MALTOSE_MALTODEXTRIN-BINDING PERIPLASMIC PROTEIN; 1.
DR Pfam; PF13416; SBP_bac_8; 1.
DR PRINTS; PR00181; MALTOSEBP.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS01037; SBP_BACTERIAL_1; 1.
PE 3: Inferred from homology;
KW Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|RuleBase:RU365005};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU365005};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597,
KW ECO:0000256|RuleBase:RU365005};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365005}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|RuleBase:RU365005"
FT CHAIN 23..389
FT /note="Maltodextrin-binding protein"
FT /evidence="ECO:0000256|RuleBase:RU365005"
FT /id="PRO_5013428101"
SQ SEQUENCE 389 AA; 41457 MW; A58E366563D41B26 CRC64;
MKILRTTLVA AMLATTSTAA MAAVEGELLI WIGADKDIKQ LQAVAARFTE ELGVPTKVEL
VDPELPDKFQ RAASTGDGPD LVMWAHDRFG EWAASGLLQP VEPTSEFKAG VLPTAWDAVS
FNGKVWGYPI AIEAIGLVYN KDLISEPPKD FSEFAHLELP EGVKPILWDY TNTYFTMPML
MANGGYSFKK VDGVYNGKET GVNNQGAIEG AEVLAKLFAD GIIPDGVDYG VMDAAMARGE
VAMVINGPWS WKAYEEAGLN IGVAPIPQVN GNVSPPFIGV YSVALNSASP NADLASEFIE
NYMLTDEGLA VWNKNRALGA LADISASEAL HSDKISATLK NASTGVPMPS NPEMGAFWAA
MAPALSNITT GKQTPEEALK DAASRILGE
//
