MALK_SALTY
ID MALK_SALTY Reviewed; 369 AA.
AC P19566; O06952;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 3.
DT 03-AUG-2022, entry version 158.
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};
GN Name=malK {ECO:0000255|HAMAP-Rule:MF_01709}; OrderedLocusNames=STM4230;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=1730061; DOI=10.1016/0167-4781(92)90492-i;
RA Schneider E., Francoz E., Dassa E.;
RT "Completion of the nucleotide sequence of the 'maltose B' region in
RT Salmonella typhimurium: the high conservation of the malM gene suggests a
RT selected physiological role for its product.";
RL Biochim. Biophys. Acta 1129:223-227(1992).
RN [3]
RP SEQUENCE REVISION TO 99-102.
RA Schneider E.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [5]
RP FUNCTION.
RX PubMed=9765559; DOI=10.1128/jb.180.20.5299-5305.1998;
RA Schmees G., Schneider E.;
RT "Domain structure of the ATP-binding-cassette protein MalK of salmonella
RT typhimurium as assessed by coexpressed half molecules and LacK'-'MalK
RT chimeras.";
RL J. Bacteriol. 180:5299-5305(1998).
RN [6]
RP MUTAGENESIS OF LEU-86; PRO-160; ASP-165 AND GLU-306.
RX PubMed=10671470; DOI=10.1128/jb.182.5.1432-1436.2000;
RA Hunke S., Landmesser H., Schneider E.;
RT "Novel missense mutations that affect the transport function of MalK, the
RT ATP-binding-cassette subunit of the Salmonella enterica serovar typhimurium
RT maltose transport system.";
RL J. Bacteriol. 182:1432-1436(2000).
RN [7]
RP INTERACTION WITH MALT AND PTS ENZYME IIA.
RX PubMed=12180984; DOI=10.1046/j.1432-1033.2002.03099.x;
RA Stein A., Seifert M., Volkmer-Engert R., Siepelmeyer J., Jahreis K.,
RA Schneider E.;
RT "Functional characterization of the maltose ATP-binding-cassette
RT transporter of Salmonella typhimurium by means of monoclonal antibodies
RT directed against the MalK subunit.";
RL Eur. J. Biochem. 269:4074-4085(2002).
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 ECO:0000269|PubMed:9765559}.
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; Peripheral membrane protein.
CC -!- MISCELLANEOUS: Target for inducer exclusion, mediated by the
CC unphosphorylated enzyme III of the phosphotransferase system for
CC glucose and resulting in the inhibition of maltose transport.
CC -!- MISCELLANEOUS: Acts as a repressor of mal genes. In absence of maltose,
CC the C-terminus of MalK interacts with MalT, then MalT becomes inactive
CC and the mal genes are not activated. In presence of maltose, MalK is
CC tightly associated with the MalFG complex and has no affinity for MalT.
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 EMBL; X54292; CAA38188.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL23054.1; -; Genomic_DNA.
DR PIR; S05329; S05329.
DR RefSeq; NP_463095.1; NC_003197.2.
DR RefSeq; WP_000179176.1; NC_003197.2.
DR AlphaFoldDB; P19566; -.
DR SMR; P19566; -.
DR IntAct; P19566; 1.
DR STRING; 99287.STM4230; -.
DR PaxDb; P19566; -.
DR EnsemblBacteria; AAL23054; AAL23054; STM4230.
DR GeneID; 1255756; -.
DR KEGG; stm:STM4230; -.
DR PATRIC; fig|99287.12.peg.4450; -.
DR HOGENOM; CLU_000604_1_1_6; -.
DR OMA; SPKAFLM; -.
DR PhylomeDB; P19566; -.
DR BioCyc; SENT99287:STM4230-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IBA:GO_Central.
DR GO; GO:1990060; C:maltose transport complex; IBA:GO_Central.
DR GO; GO:0015423; F:ABC-type maltose transporter activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR CDD; cd03301; ABC_MalK_N; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR015855; ABC_transpr_MalK-like.
DR InterPro; IPR008995; Mo/tungstate-bd_C_term_dom.
DR InterPro; IPR012340; NA-bd_OB-fold.
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; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS51245; MALK; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Reference proteome; Sugar transport; Translocase;
KW Transport.
FT CHAIN 1..369
FT /note="Maltose/maltodextrin import ATP-binding protein
FT MalK"
FT /id="PRO_0000092482"
FT DOMAIN 4..234
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 MUTAGEN 86
FT /note="L->F: Loss of transport. No effect on ATP-binding
FT activity but decrease in ATP hydrolysis. Retains repressor
FT activity."
FT /evidence="ECO:0000269|PubMed:10671470"
FT MUTAGEN 160
FT /note="P->L: Loss of transport. No effect on ATP-binding
FT activity but decrease in ATP hydrolysis. Retains repressor
FT activity."
FT /evidence="ECO:0000269|PubMed:10671470"
FT MUTAGEN 165
FT /note="D->N: Loss of transport. No effect on ATP-binding
FT activity but decrease in ATP hydrolysis. Retains repressor
FT activity."
FT /evidence="ECO:0000269|PubMed:10671470"
FT MUTAGEN 306
FT /note="E->K: Loss of transport. No effect on ATP-binding
FT and ATP hydrolysis. Retains repressor activity."
FT /evidence="ECO:0000269|PubMed:10671470"
FT CONFLICT 141
FT /note="R -> A (in Ref. 1; CAA38188 and 2; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 369 AA; 40799 MW; 98CA374498C88FCF CRC64;
MASVQLRNVT KAWGDVVVSK DINLDIHDGE FVVFVGPSGC GKSTLLRMIA GLETITSGDL
FIGETRMNDI PPAERGVGMV FQSYALYPHL SVAENMSFGL KLAGAKKEVM NQRVNQVAEV
LQLAHLLERK PKALSGGQRQ RVAIGRTLVA EPRVFLLDEP LSNLDAALRV QMRIEISRLH
KRLGRTMIYV THDQVEAMTL ADKIVVLDAG RVAQVGKPLE LYHYPADRFV AGFIGSPKMN
FLPVKVTATA IEQVQVELPN RQQIWLPVES RGVQVGANMS LGIRPEHLLP SDIADVTLEG
EVQVVEQLGH ETQIHIQIPA IRQNLVYRQN DVVLVEEGAT FAIGLPPERC HLFREDGSAC
RRLHQEPGV
