MSMX_BACSU
ID MSMX_BACSU Reviewed; 365 AA.
AC P94360;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Oligosaccharides import ATP-binding protein MsmX {ECO:0000305};
DE EC=7.5.2.- {ECO:0000305|PubMed:16707683, ECO:0000305|PubMed:20693325, ECO:0000305|PubMed:27501980, ECO:0000305|PubMed:29240795, ECO:0000305|PubMed:31138628};
DE AltName: Full=Maltodextrin import ATP-binding protein MsmX {ECO:0000305};
DE AltName: Full=Melibiose/raffinose/stachyose import ATP-binding protein MsmX {ECO:0000305};
GN Name=msmX; Synonyms=yxkG; OrderedLocusNames=BSU38810;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / BGSC1A1;
RX PubMed=8969509; DOI=10.1099/13500872-142-11-3113;
RA Yoshida K., Shindo K., Sano H., Seki S., Fujimura M., Yanai N., Miwa Y.,
RA Fujita Y.;
RT "Sequencing of a 65 kb region of the Bacillus subtilis genome containing
RT the lic and cel loci, and creation of a 177 kb contig covering the gnt-
RT sacXY region.";
RL Microbiology 142:3113-3123(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION IN MALTODEXTRIN IMPORT, AND SUBUNIT.
RC STRAIN=168;
RX PubMed=16707683; DOI=10.1128/jb.00213-06;
RA Schoenert S., Seitz S., Krafft H., Feuerbaum E.-A., Andernach I., Witz G.,
RA Dahl M.K.;
RT "Maltose and maltodextrin utilization by Bacillus subtilis.";
RL J. Bacteriol. 188:3911-3922(2006).
RN [4]
RP FUNCTION IN ARABINOOLIGOSACCHARIDES IMPORT, SUBUNIT, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=20693325; DOI=10.1128/jb.00832-10;
RA Ferreira M.J., Sa-Nogueira I.D.;
RT "A multitask ATPase serving different ABC-type sugar importers in Bacillus
RT subtilis.";
RL J. Bacteriol. 192:5312-5318(2010).
RN [5]
RP FUNCTION IN GALACTOOLIGOSACCHARIDES IMPORT, AND SUBUNIT.
RX PubMed=27501980; DOI=10.1128/jb.00468-16;
RA Watzlawick H., Morabbi Heravi K., Altenbuchner J.;
RT "Role of the ganSPQAB operon in degradation of galactan by Bacillus
RT subtilis.";
RL J. Bacteriol. 198:2887-2896(2016).
RN [6]
RP FUNCTION, SUBUNIT, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29240795; DOI=10.1371/journal.pone.0189483;
RA Ferreira M.J., Mendes A.L., de Sa-Nogueira I.;
RT "The MsmX ATPase plays a crucial role in pectin mobilization by Bacillus
RT subtilis.";
RL PLoS ONE 12:e0189483-e0189483(2017).
RN [7]
RP FUNCTION IN MELIBIOSE; RAFFINOSE AND STACHYOSE IMPORT, SUBUNIT, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=168 / KM0;
RX PubMed=31138628; DOI=10.1128/jb.00109-19;
RA Morabbi Heravi K., Watzlawick H., Altenbuchner J.;
RT "The melREDCA operon encodes a utilization system for the raffinose family
RT of oligosaccharides in Bacillus subtilis.";
RL J. Bacteriol. 201:E00109-E00109(2019).
CC -!- FUNCTION: Required to energize different ABC-type saccharide
CC transporters (PubMed:20693325, PubMed:29240795). Part of the MdxEFG-
CC MsmX ABC transporter complex involved in maltodextrin import, of the
CC AraNPQ-MsmX complex involved in arabinooligosaccharides import, of the
CC GanPQS-MsmX complex involved in galactooligosaccharides import, and of
CC the MelEDC-MsmX complex involved in melibiose, raffinose and stachyose
CC import (PubMed:16707683, PubMed:20693325, PubMed:27501980,
CC PubMed:29240795, PubMed:31138628). Is probably also part of the ABC
CC transporter complex YtcQP-YteP-MsmX involved in polygalacturonan and
CC rhamnogalacturonan type I import during pectin degradation
CC (PubMed:29240795). Responsible for energy coupling to the transport
CC system (Probable). {ECO:0000269|PubMed:16707683,
CC ECO:0000269|PubMed:20693325, ECO:0000269|PubMed:27501980,
CC ECO:0000269|PubMed:29240795, ECO:0000269|PubMed:31138628, ECO:0000305}.
CC -!- SUBUNIT: The complex involved in maltodextrin import is composed of two
CC ATP-binding proteins (MsmX), two transmembrane proteins (MdxF and MdxG)
CC and a solute-binding protein (MdxE) (PubMed:16707683). The complex
CC involved in arabinooligosaccharides uptake is composed of two ATP-
CC binding proteins (MsmX), two transmembrane proteins (AraP and AraQ) and
CC a solute-binding protein (AraN) (PubMed:20693325). The complex involved
CC in galactooligosaccharides uptake is composed of two ATP-binding
CC proteins (MsmX), two transmembrane proteins (GanP and GanQ) and a
CC solute-binding protein (GanS) (PubMed:27501980, PubMed:29240795). The
CC complex involved in melibiose, raffinose and stachyose import is
CC composed of two ATP-binding proteins (MsmX), two transmembrane proteins
CC (MelC and MelD) and a solute-binding protein (MelE) (PubMed:31138628).
CC The complex involved in polygalacturonan and rhamnogalacturonan type I
CC uptake is probably composed of two ATP-binding proteins (MsmX), two
CC transmembrane proteins (YtcP and YteP) and a solute-binding protein
CC (YtcQ) (PubMed:29240795). {ECO:0000269|PubMed:16707683,
CC ECO:0000269|PubMed:20693325, ECO:0000269|PubMed:27501980,
CC ECO:0000269|PubMed:29240795, ECO:0000269|PubMed:31138628}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Expressed in the presence of either arabinose or
CC arabinotriose. Repressed by glucose. {ECO:0000269|PubMed:29240795}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene abolishes induction of the
CC melREDCA operon the presence of melibiose and raffinose
CC (PubMed:31138628). It does not affect growth in the presence of glucose
CC and arabinose, but it has a negative effect on the ability of the
CC mutant to grow on the alpha-1,5-arabinose oligomers alpha-1,5-
CC arabinobiose, alpha-1,5-arabinotriose and alpha-1,5-arabinotetraose
CC (PubMed:20693325). Deletion mutant cannot utilize pectin and galactan,
CC and shows a slower but steady growth rate in the presence of type I
CC rhamnogalacturonan or polygalacturonan (PubMed:29240795).
CC {ECO:0000269|PubMed:20693325, ECO:0000269|PubMed:29240795,
CC ECO:0000269|PubMed:31138628}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; D83026; BAA11723.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15907.1; -; Genomic_DNA.
DR PIR; B69661; B69661.
DR RefSeq; NP_391760.1; NC_000964.3.
DR RefSeq; WP_003242648.1; NZ_JNCM01000034.1.
DR PDB; 6YIR; X-ray; 1.68 A; A=1-365.
DR PDBsum; 6YIR; -.
DR AlphaFoldDB; P94360; -.
DR SMR; P94360; -.
DR STRING; 224308.BSU38810; -.
DR TCDB; 3.A.1.1.26; the atp-binding cassette (abc) superfamily.
DR TCDB; 3.A.1.1.34; the atp-binding cassette (abc) superfamily.
DR jPOST; P94360; -.
DR PaxDb; P94360; -.
DR PRIDE; P94360; -.
DR EnsemblBacteria; CAB15907; CAB15907; BSU_38810.
DR GeneID; 937422; -.
DR KEGG; bsu:BSU38810; -.
DR PATRIC; fig|224308.179.peg.4200; -.
DR eggNOG; COG3842; Bacteria.
DR InParanoid; P94360; -.
DR OMA; APPMNLM; -.
DR PhylomeDB; P94360; -.
DR BioCyc; BSUB:BSU38810-MON; -.
DR SABIO-RK; P94360; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IBA:GO_Central.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0015774; P:polysaccharide transport; 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 InterPro; IPR005116; Transp-assoc_OB_typ1.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF17912; OB_MalK; 1.
DR Pfam; PF03459; TOBE; 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; Hydrolase; Membrane;
KW Nucleotide-binding; Polysaccharide transport; Reference proteome;
KW Sugar transport; Translocase; Transport.
FT CHAIN 1..365
FT /note="Oligosaccharides import ATP-binding protein MsmX"
FT /id="PRO_0000092613"
FT DOMAIN 4..235
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 37..44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:6YIR"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:6YIR"
FT STRAND 19..27
FT /evidence="ECO:0007829|PDB:6YIR"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:6YIR"
FT HELIX 43..50
FT /evidence="ECO:0007829|PDB:6YIR"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:6YIR"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:6YIR"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:6YIR"
FT TURN 81..84
FT /evidence="ECO:0007829|PDB:6YIR"
FT HELIX 93..103
FT /evidence="ECO:0007829|PDB:6YIR"
FT HELIX 108..121
FT /evidence="ECO:0007829|PDB:6YIR"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:6YIR"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:6YIR"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:6YIR"
FT HELIX 143..150
FT /evidence="ECO:0007829|PDB:6YIR"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:6YIR"
FT TURN 161..164
FT /evidence="ECO:0007829|PDB:6YIR"
FT HELIX 167..184
FT /evidence="ECO:0007829|PDB:6YIR"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:6YIR"
FT HELIX 195..201
FT /evidence="ECO:0007829|PDB:6YIR"
FT STRAND 203..209
FT /evidence="ECO:0007829|PDB:6YIR"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:6YIR"
FT HELIX 219..224
FT /evidence="ECO:0007829|PDB:6YIR"
FT HELIX 229..234
FT /evidence="ECO:0007829|PDB:6YIR"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:6YIR"
FT STRAND 241..247
FT /evidence="ECO:0007829|PDB:6YIR"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:6YIR"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:6YIR"
FT HELIX 263..271
FT /evidence="ECO:0007829|PDB:6YIR"
FT STRAND 277..283
FT /evidence="ECO:0007829|PDB:6YIR"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:6YIR"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:6YIR"
FT TURN 291..293
FT /evidence="ECO:0007829|PDB:6YIR"
FT STRAND 302..306
FT /evidence="ECO:0007829|PDB:6YIR"
FT STRAND 308..313
FT /evidence="ECO:0007829|PDB:6YIR"
FT STRAND 316..323
FT /evidence="ECO:0007829|PDB:6YIR"
FT STRAND 326..333
FT /evidence="ECO:0007829|PDB:6YIR"
FT STRAND 342..348
FT /evidence="ECO:0007829|PDB:6YIR"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:6YIR"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:6YIR"
FT TURN 358..360
FT /evidence="ECO:0007829|PDB:6YIR"
SQ SEQUENCE 365 AA; 41366 MW; C50689EE0E060D32 CRC64;
MAELRMEHIY KFYDQKEPAV DDFNLHIADK EFIVFVGPSG CGKSTTLRMV AGLEEISKGD
FYIEGKRVND VAPKDRDIAM VFQNYALYPH MTVYDNIAFG LKLRKMPKPE IKKRVEEAAK
ILGLEEYLHR KPKALSGGQR QRVALGRAIV RDAKVFLMDE PLSNLDAKLR VQMRAEIIKL
HQRLQTTTIY VTHDQTEALT MATRIVVMKD GKIQQIGTPK DVYEFPENVF VGGFIGSPAM
NFFKGKLTDG LIKIGSAALT VPEGKMKVLR EKGYIGKEVI FGIRPEDIHD ELIVVESYKN
SSIKAKINVA ELLGSEIMIY SQIDNQDFIA RIDARLDIQS GDELTVAFDM NKGHFFDSET
EVRIR
