MALK_KLEAE
ID MALK_KLEAE Reviewed; 294 AA.
AC P18813;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Maltose/maltodextrin import ATP-binding protein MalK {ECO:0000255|HAMAP-Rule:MF_01709};
DE EC=7.5.2.1 {ECO:0000255|HAMAP-Rule:MF_01709};
DE Flags: Fragment;
GN Name=malK {ECO:0000255|HAMAP-Rule:MF_01709};
OS Klebsiella aerogenes (Enterobacter aerogenes).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=548;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2674653; DOI=10.1007/bf00331269;
RA Dahl M.K., Francoz E., Saurin W., Boos W., Manson M.D., Hofnung M.;
RT "Comparison of sequences from the malB regions of Salmonella typhimurium
RT and Enterobacter aerogenes with Escherichia coli K12: a potential new
RT regulatory site in the interoperonic region.";
RL Mol. Gen. Genet. 218:199-207(1989).
CC -!- FUNCTION: Part of the ABC transporter complex MalEFGK involved in
CC maltose/maltodextrin import. Responsible for energy coupling to the
CC transport system. {ECO:0000255|HAMAP-Rule:MF_01709}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-maltose(out) + H2O = ADP + D-maltose(in) + H(+) +
CC phosphate; Xref=Rhea:RHEA:22132, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17306, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.5.2.1;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01709};
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (MalK),
CC two transmembrane proteins (MalG and MalK) and a solute-binding protein
CC (MalE). {ECO:0000255|HAMAP-Rule:MF_01709}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01709}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01709}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily.
CC Maltooligosaccharide importer (TC 3.A.1.1.1) family.
CC {ECO:0000255|HAMAP-Rule:MF_01709}.
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DR PIR; S05328; S05328.
DR AlphaFoldDB; P18813; -.
DR SMR; P18813; -.
DR STRING; 548.EAG7_03818; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IEA:UniProt.
DR GO; GO:0015423; F:ABC-type maltose transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR CDD; cd03301; ABC_MalK_N; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR015855; ABC_transpr_MalK-like.
DR InterPro; IPR008995; Mo/tungstate-bd_C_term_dom.
DR InterPro; IPR040582; OB_MalK.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF17912; OB_MalK; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF50331; SSF50331; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Sugar transport; Translocase; Transport.
FT CHAIN 1..>294
FT /note="Maltose/maltodextrin import ATP-binding protein
FT MalK"
FT /id="PRO_0000092478"
FT DOMAIN 4..233
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01709"
FT BINDING 36..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01709"
FT NON_TER 294
SQ SEQUENCE 294 AA; 32247 MW; 7A4D6C96280F9C13 CRC64;
MASVQLRNVT KAWGDVVVSK DINLEIQDGE FVVFVGPSGC GKSTLLRMIA GLETVTSGDL
FIGDTRMNDV PPAERGIGMV FQSYALYPHL SVAENMSFGL KLAGAKKEVI NQRVTQVAEV
LQLAHLLERN RKALSGGQRP GVAIRTLVAE PRVFLLDEPL SNLDAALRVQ MRIEISRLHK
RLGRTMIYVT HDQVEAMTLA DKIVVLDAGR VAQVGKPLEL YHYPADRFVA GFIGSPKMNF
LPVKVTATAI EQVQVELPNR QQVWLPVDSA HVQVGANMSL GIRPEHLLPS DIAD
