MELE_BACSU
ID MELE_BACSU Reviewed; 426 AA.
AC O34335; Q795Q9;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Melibiose/raffinose/stachyose-binding protein MelE {ECO:0000305};
DE Flags: Precursor;
GN Name=melE {ECO:0000303|PubMed:31138628}; Synonyms=msmE;
GN OrderedLocusNames=BSU30270;
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;
RX PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT 200 kb rrnB-dnaB region.";
RL Microbiology 143:3431-3441(1997).
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, SUBUNIT, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION
RP 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).
RN [4] {ECO:0007744|PDB:4R6H}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 22-426.
RA Patskovsky Y., Toro R., Bhosle R., Al obaidi N., Chamala S.,
RA Scott glenn A., Attonito J.D., Chowdhury S., Lafleur J., Siedel R.D.,
RA Hillerich B., Love J., Whalen K.L., Gerlt J.A., Almo S.C.;
RT "Crystal structure of transporter MsmE from Bacillus subtilis, target Efi-
RT 510764.";
RL Submitted (AUG-2014) to the PDB data bank.
CC -!- FUNCTION: Part of the ABC transporter complex MelEDC-MsmX involved in
CC melibiose, raffinose and stachyose import. Binds melibiose, raffinose
CC and stachyose. {ECO:0000269|PubMed:31138628}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (MsmX),
CC two transmembrane proteins (MelC and MelD) and a solute-binding protein
CC (MelE). {ECO:0000269|PubMed:31138628}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:31138628};
CC Lipid-anchor {ECO:0000305}.
CC -!- INDUCTION: Repressed by the transcriptional regulator MelR. Induced by
CC melibiose and raffinose. {ECO:0000269|PubMed:31138628}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene abolishes induction in the
CC presence of melibiose and raffinose. {ECO:0000269|PubMed:31138628}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 1 family.
CC {ECO:0000305}.
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DR EMBL; AF008220; AAC00386.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15005.1; -; Genomic_DNA.
DR PIR; H69660; H69660.
DR RefSeq; NP_390905.1; NC_000964.3.
DR RefSeq; WP_004398680.1; NZ_JNCM01000036.1.
DR PDB; 4R6H; X-ray; 1.50 A; A=22-426.
DR PDBsum; 4R6H; -.
DR AlphaFoldDB; O34335; -.
DR SMR; O34335; -.
DR STRING; 224308.BSU30270; -.
DR PaxDb; O34335; -.
DR DNASU; 936693; -.
DR EnsemblBacteria; CAB15005; CAB15005; BSU_30270.
DR GeneID; 936693; -.
DR KEGG; bsu:BSU30270; -.
DR PATRIC; fig|224308.179.peg.3283; -.
DR eggNOG; COG1653; Bacteria.
DR OMA; QNKIAFT; -.
DR PhylomeDB; O34335; -.
DR BioCyc; BSUB:BSU30270-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015774; P:polysaccharide transport; IEA:UniProtKB-KW.
DR InterPro; IPR006059; SBP.
DR Pfam; PF01547; SBP_bac_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Lipoprotein; Membrane; Palmitate;
KW Polysaccharide transport; Reference proteome; Signal; Sugar transport;
KW Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..426
FT /note="Melibiose/raffinose/stachyose-binding protein MelE"
FT /id="PRO_0000387963"
FT LIPID 19
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT LIPID 19
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:4R6H"
FT HELIX 42..58
FT /evidence="ECO:0007829|PDB:4R6H"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:4R6H"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:4R6H"
FT HELIX 73..82
FT /evidence="ECO:0007829|PDB:4R6H"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:4R6H"
FT HELIX 96..100
FT /evidence="ECO:0007829|PDB:4R6H"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:4R6H"
FT HELIX 111..115
FT /evidence="ECO:0007829|PDB:4R6H"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:4R6H"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:4R6H"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:4R6H"
FT STRAND 139..146
FT /evidence="ECO:0007829|PDB:4R6H"
FT HELIX 147..153
FT /evidence="ECO:0007829|PDB:4R6H"
FT HELIX 161..175
FT /evidence="ECO:0007829|PDB:4R6H"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:4R6H"
FT HELIX 190..204
FT /evidence="ECO:0007829|PDB:4R6H"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:4R6H"
FT HELIX 213..217
FT /evidence="ECO:0007829|PDB:4R6H"
FT HELIX 223..226
FT /evidence="ECO:0007829|PDB:4R6H"
FT HELIX 227..238
FT /evidence="ECO:0007829|PDB:4R6H"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:4R6H"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:4R6H"
FT HELIX 254..259
FT /evidence="ECO:0007829|PDB:4R6H"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:4R6H"
FT HELIX 272..279
FT /evidence="ECO:0007829|PDB:4R6H"
FT STRAND 285..290
FT /evidence="ECO:0007829|PDB:4R6H"
FT STRAND 300..304
FT /evidence="ECO:0007829|PDB:4R6H"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:4R6H"
FT HELIX 318..329
FT /evidence="ECO:0007829|PDB:4R6H"
FT HELIX 331..340
FT /evidence="ECO:0007829|PDB:4R6H"
FT HELIX 357..362
FT /evidence="ECO:0007829|PDB:4R6H"
FT TURN 363..365
FT /evidence="ECO:0007829|PDB:4R6H"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:4R6H"
FT HELIX 372..376
FT /evidence="ECO:0007829|PDB:4R6H"
FT HELIX 381..393
FT /evidence="ECO:0007829|PDB:4R6H"
FT HELIX 399..418
FT /evidence="ECO:0007829|PDB:4R6H"
SQ SEQUENCE 426 AA; 48238 MW; 6BBA821525E18901 CRC64;
MKHTFVLFLS LILLVLPGCS AEKSSADTAK KTLTIYSTMS TDSERDTFRK LAAAFEKEHS
DIHVSLHFPG NDYENMMRVR MAANDLPDLF DTHGWGKIRY GEYTADLRDM KWTQDLDPNL
NSILKNKSGK VYAYPINQAK DGLAYNRNIL DRYGIAPPET MDDFIKALRT IKEKSKGSIV
PFWFAGYDKS SFAQYYDQFA TPLLITDPAH NEKKQLINGT FQWSKFTYLS EILKQMQKEK
LINIDAVTAK KSQLIELMAQ NKIAFTMQGG TLGQDVAQIN PNVKVGIIPT PAIHPGDDPI
WIGGERYTLA AWKDSPQLKE AKDFIAFMAR PANAKQMAEA TSLPSGLTNV KADIFYANDY
EYYQDVKVEP YFDRLYLPNG MWDVLGTVGQ ELAADILAPQ DISQKLGREY KRLREQSETQ
GAENNE
