MALK_THELN
ID MALK_THELN Reviewed; 372 AA.
AC Q9YGA6; Q9V306; S5ZTR0;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Trehalose/maltose import ATP-binding protein MalK;
DE EC=7.5.2.1;
GN Name=malK; ORFNames=OCC_13985;
OS Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=523849;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ATPASE ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RC STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C;
RX PubMed=10400644; DOI=10.1074/jbc.274.29.20259;
RA Greller G., Horlacher R., DiRuggiero J., Boos W.;
RT "Molecular and biochemical analysis of MalK, the ATP-hydrolyzing subunit of
RT the trehalose/maltose transport system of the hyperthermophilic archaeon
RT Thermococcus litoralis.";
RL J. Biol. Chem. 274:20259-20264(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C;
RX PubMed=11115105; DOI=10.1046/j.1365-2958.2000.02161.x;
RA Diruggiero J., Dunn D., Maeder D.L., Holley-Shanks R., Chatard J.,
RA Horlacher R., Robb F.T., Boos W., Weiss R.B.;
RT "Evidence of recent lateral gene transfer among hyperthermophilic
RT archaea.";
RL Mol. Microbiol. 38:684-693(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C;
RX PubMed=15158466; DOI=10.1016/j.bbrc.2004.04.174;
RA Imamura H., Jeon B.S., Wakagi T.;
RT "Molecular evolution of the ATPase subunit of three archaeal sugar ABC
RT transporters.";
RL Biochem. Biophys. Res. Commun. 319:230-234(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C;
RX PubMed=22493191; DOI=10.1128/jb.00123-12;
RA Gardner A.F., Kumar S., Perler F.B.;
RT "Genome sequence of the model hyperthermophilic archaeon Thermococcus
RT litoralis NS-C.";
RL J. Bacteriol. 194:2375-2376(2012).
RN [5]
RP FUNCTION.
RC STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C;
RX PubMed=8759837; DOI=10.1128/jb.178.16.4773-4777.1996;
RA Xavier K.B., Martins L.O., Peist R., Kossmann M., Boos W., Santos H.;
RT "High-affinity maltose/trehalose transport system in the hyperthermophilic
RT archaeon Thermococcus litoralis.";
RL J. Bacteriol. 178:4773-4777(1996).
RN [6]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=11453995; DOI=10.1046/j.1432-1327.2001.02313.x;
RA Greller G., Riek R., Boos W.;
RT "Purification and characterization of the heterologously expressed
RT trehalose/maltose ABC transporter complex of the hyperthermophilic archaeon
RT Thermococcus litoralis.";
RL Eur. J. Biochem. 268:4011-4018(2001).
RN [7]
RP CRYSTALLIZATION, AND SUBUNIT.
RX PubMed=12454482; DOI=10.1107/s090744490201572x;
RA Schiefner A., Diederichs K., Hashimoto K., Boos W., Welte W.;
RT "Crystallization and preliminary X-ray analysis of the trehalose/maltose
RT ABC transporter MalFGK2 from Thermococcus litoralis.";
RL Acta Crystallogr. D 58:2147-2149(2002).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), SUBUNIT, AND DOMAIN.
RX PubMed=11080142; DOI=10.1093/emboj/19.22.5951;
RA Diederichs K., Diez J., Greller G., Muller C., Breed J., Schnell C.,
RA Vonrhein C., Boos W., Welte W.;
RT "Crystal structure of MalK, the ATPase subunit of the trehalose/maltose ABC
RT transporter of the archaeon Thermococcus litoralis.";
RL EMBO J. 19:5951-5961(2000).
CC -!- FUNCTION: Part of the ABC transporter complex MalEFGK involved in
CC trehalose/maltose import. Responsible for energy coupling to the
CC transport system. {ECO:0000269|PubMed:10400644,
CC ECO:0000269|PubMed:11453995, ECO:0000269|PubMed:8759837}.
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 -!- ACTIVITY REGULATION: Inhibited by N-ethylmaleimide but not by vanadate.
CC {ECO:0000269|PubMed:10400644}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=155 uM for ATP {ECO:0000269|PubMed:10400644};
CC KM=430 uM for GTP {ECO:0000269|PubMed:10400644};
CC KM=870 uM for CTP {ECO:0000269|PubMed:10400644};
CC Vmax=0.55 umol/min/mg enzyme with ATP as substrate
CC {ECO:0000269|PubMed:10400644};
CC Vmax=0.45 umol/min/mg enzyme with GTP as substrate
CC {ECO:0000269|PubMed:10400644};
CC Vmax=0.32 umol/min/mg enzyme with CTP as substrate
CC {ECO:0000269|PubMed:10400644};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:10400644};
CC Temperature dependence:
CC Optimum temperature is 80 degrees Celsius.
CC {ECO:0000269|PubMed:10400644};
CC -!- SUBUNIT: Homodimer. The complex is composed of two ATP-binding proteins
CC (MalK), two transmembrane proteins (MalG and MalF) and a solute-binding
CC protein (MalE). {ECO:0000269|PubMed:11080142,
CC ECO:0000269|PubMed:11453995, ECO:0000269|PubMed:12454482}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11453995};
CC Peripheral membrane protein {ECO:0000269|PubMed:11453995}.
CC -!- INDUCTION: Induced by maltose and trehalose.
CC {ECO:0000269|PubMed:10400644}.
CC -!- DOMAIN: Contains an N-terminal ATPase domain and a C-terminal
CC regulatory domain. {ECO:0000269|PubMed:11080142}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily.
CC Maltose/trehalose importer (TC 3.A.1.1.7) family. {ECO:0000305}.
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DR EMBL; AF121946; AAD23570.1; -; Genomic_DNA.
DR EMBL; AF126010; AAD24578.1; -; Genomic_DNA.
DR EMBL; AF307053; AAG45393.1; -; Genomic_DNA.
DR EMBL; AB054186; BAC10984.1; -; Genomic_DNA.
DR EMBL; CP006670; AGT34279.1; -; Genomic_DNA.
DR PDB; 1G29; X-ray; 1.90 A; 1/2=1-372.
DR PDBsum; 1G29; -.
DR AlphaFoldDB; Q9YGA6; -.
DR SMR; Q9YGA6; -.
DR STRING; 523849.OCC_13985; -.
DR PRIDE; Q9YGA6; -.
DR EnsemblBacteria; AGT34279; AGT34279; OCC_13985.
DR KEGG; tlt:OCC_13985; -.
DR HOGENOM; CLU_000604_1_1_2; -.
DR SABIO-RK; Q9YGA6; -.
DR EvolutionaryTrace; Q9YGA6; -.
DR Proteomes; UP000015502; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015423; F:ABC-type maltose transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion 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.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Sugar transport; Translocase; Transport.
FT CHAIN 1..372
FT /note="Trehalose/maltose import ATP-binding protein MalK"
FT /id="PRO_0000421285"
FT DOMAIN 4..240
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 36..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CONFLICT 22
FT /note="M -> L (in Ref. 1; AAD24578 and 2; AAG45393)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="K -> R (in Ref. 1; AAD24578 and 2; AAG45393)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="Q -> R (in Ref. 1; AAD24578 and 2; AAG45393)"
FT /evidence="ECO:0000305"
FT CONFLICT 338
FT /note="S -> A (in Ref. 1; AAD24578 and 2; AAG45393)"
FT /evidence="ECO:0000305"
FT STRAND 2..13
FT /evidence="ECO:0007829|PDB:1G29"
FT STRAND 16..27
FT /evidence="ECO:0007829|PDB:1G29"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:1G29"
FT HELIX 42..50
FT /evidence="ECO:0007829|PDB:1G29"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:1G29"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:1G29"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:1G29"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:1G29"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:1G29"
FT HELIX 98..108
FT /evidence="ECO:0007829|PDB:1G29"
FT HELIX 113..126
FT /evidence="ECO:0007829|PDB:1G29"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:1G29"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:1G29"
FT HELIX 142..155
FT /evidence="ECO:0007829|PDB:1G29"
FT STRAND 159..164
FT /evidence="ECO:0007829|PDB:1G29"
FT TURN 166..169
FT /evidence="ECO:0007829|PDB:1G29"
FT HELIX 172..189
FT /evidence="ECO:0007829|PDB:1G29"
FT STRAND 192..198
FT /evidence="ECO:0007829|PDB:1G29"
FT HELIX 200..206
FT /evidence="ECO:0007829|PDB:1G29"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:1G29"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:1G29"
FT HELIX 224..229
FT /evidence="ECO:0007829|PDB:1G29"
FT HELIX 234..239
FT /evidence="ECO:0007829|PDB:1G29"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:1G29"
FT STRAND 246..252
FT /evidence="ECO:0007829|PDB:1G29"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:1G29"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:1G29"
FT HELIX 269..277
FT /evidence="ECO:0007829|PDB:1G29"
FT STRAND 283..289
FT /evidence="ECO:0007829|PDB:1G29"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:1G29"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:1G29"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:1G29"
FT TURN 305..307
FT /evidence="ECO:0007829|PDB:1G29"
FT STRAND 308..319
FT /evidence="ECO:0007829|PDB:1G29"
FT STRAND 324..330
FT /evidence="ECO:0007829|PDB:1G29"
FT STRAND 333..339
FT /evidence="ECO:0007829|PDB:1G29"
FT STRAND 350..355
FT /evidence="ECO:0007829|PDB:1G29"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:1G29"
FT STRAND 361..364
FT /evidence="ECO:0007829|PDB:1G29"
FT TURN 365..367
FT /evidence="ECO:0007829|PDB:1G29"
SQ SEQUENCE 372 AA; 41786 MW; 31261E66048BC76F CRC64;
MAGVRLVDVW KVFGEVTAVR EMSLEVKDGE FMILLGPSGC GKTTTLRMIA GLEEPSRGQI
YIGDKLVADP EKGIFVPPKD RDIAMVFQSY ALYPHMTVYD NIAFPLKLRK VPRQEIDQRV
REVAELLGLT ELLNRKPREL SGGQRQRVAL GRAIVRKPQV FLMDEPLSNL DAKLRVRMRA
ELKKLQRQLG VTTIYVTHDQ VEAMTMGDRI AVMNRGVLQQ VGSPDEVYDK PANTFVAGFI
GSPPMNFLDA IVTEDGFVDF GEFRLKLLPD QFEVLGELGY VGREVIFGIR PEDLYDAMFA
QVRVPGENLV RAVVEIVENL GSERIVHLRV GGVTFVGSFR SESRVREGVE VDVVFDMKKI
HIFDKTTGKA IF
