MALK_SALCH
ID MALK_SALCH Reviewed; 369 AA.
AC Q57GZ7;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=SCH_4109;
OS Salmonella choleraesuis (strain SC-B67).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=321314;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC-B67;
RX PubMed=15781495; DOI=10.1093/nar/gki297;
RA Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA Lee Y.-S.;
RT "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT invasive and resistant zoonotic pathogen.";
RL Nucleic Acids Res. 33:1690-1698(2005).
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 EMBL; AE017220; AAX68015.1; -; Genomic_DNA.
DR RefSeq; WP_000179176.1; NC_006905.1.
DR AlphaFoldDB; Q57GZ7; -.
DR SMR; Q57GZ7; -.
DR EnsemblBacteria; AAX68015; AAX68015; SCH_4109.
DR KEGG; sec:SCH_4109; -.
DR HOGENOM; CLU_000604_1_1_6; -.
DR OMA; SPKAFLM; -.
DR Proteomes; UP000000538; Chromosome.
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; 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 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Sugar transport; Translocase; Transport.
FT CHAIN 1..369
FT /note="Maltose/maltodextrin import ATP-binding protein
FT MalK"
FT /id="PRO_0000273997"
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"
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