MALE_PYRAB
ID MALE_PYRAB Reviewed; 453 AA.
AC Q9V297; G8ZG12;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Maltotriose-binding protein;
DE AltName: Full=MMBP;
DE AltName: Full=Maltodextrin-binding protein;
DE Flags: Precursor;
GN Name=malE; OrderedLocusNames=PYRAB01770; ORFNames=PAB0119;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
CC -!- FUNCTION: Involved in an abc transport system for maltotriose.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 1 family.
CC {ECO:0000305}.
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DR EMBL; AJ248283; CAB49101.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE69553.1; -; Genomic_DNA.
DR PIR; F75206; F75206.
DR RefSeq; WP_010867301.1; NC_000868.1.
DR AlphaFoldDB; Q9V297; -.
DR SMR; Q9V297; -.
DR STRING; 272844.PAB0119; -.
DR EnsemblBacteria; CAB49101; CAB49101; PAB0119.
DR GeneID; 1495064; -.
DR KEGG; pab:PAB0119; -.
DR PATRIC; fig|272844.11.peg.191; -.
DR eggNOG; arCOG00154; Archaea.
DR HOGENOM; CLU_031285_17_1_2; -.
DR OMA; WAHDWIG; -.
DR OrthoDB; 74127at2157; -.
DR PhylomeDB; Q9V297; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; Chromosome.
DR GO; GO:0015144; F:carbohydrate transmembrane transporter activity; IEA:InterPro.
DR InterPro; IPR006060; Maltose/Cyclodextrin-bd.
DR InterPro; IPR006059; SBP.
DR InterPro; IPR006061; SBP_1_CS.
DR Pfam; PF01547; SBP_bac_1; 1.
DR PRINTS; PR00181; MALTOSEBP.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS01037; SBP_BACTERIAL_1; 1.
PE 3: Inferred from homology;
KW Signal; Sugar transport; Transport.
FT SIGNAL 1..29
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 30..453
FT /note="Maltotriose-binding protein"
FT /id="PRO_0000031700"
FT REGION 27..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 453 AA; 50597 MW; FA6211EA75D6AC87 CRC64;
MKRGIYAVLL VGVLIFSVVA SGCIGGTQTQ TETQTPEKTQ TPTTTQPSPT TTTSPTQTTS
QTPTETETHT QEAECGSGKV VIWHNMQPNE LQVFQSLAEE YMAMCPDVEI VFEQKPDLEN
ALKVAIPAGQ GPDLFIWAHD WIGKFAEAGL LEPIDEYITD DLLQKFAPMA REAIEYKGHY
YALPFAAETV AMIYNKKIVS EPPKTFDELK EVMEKYYDPN NEKYGIAWPI NAYFISAIAQ
AFGGYYFDDK TEQPGLDKPE TIEGFKFFFE NIWPYMAPTA DYNTQQSIFL EGRAPIMVNG
PWSIGSVKDA GIDFGVAPLP PIIKDGKEYW PRPYGGVKLI YFAAGTHNKD AAWKFVKWFT
TNPEVIKQLA LDLGYIPVLS EVLNDPEIKN DPVIYGFGQA VQHAYLMPKS PKMGAVWGGV
QGAIDEILKD PKHADIEAIL KKYQEEILKN MQG