EXUT_BACSU
ID EXUT_BACSU Reviewed; 422 AA.
AC O34456;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Hexuronate transporter {ECO:0000303|PubMed:9882655};
DE AltName: Full=Aldohexuronate transport system {ECO:0000305};
GN Name=exuT {ECO:0000303|PubMed:9579062}; Synonyms=yjmG;
GN OrderedLocusNames=BSU12360;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROBABLE OPERON STRUCTURE.
RC STRAIN=168;
RX PubMed=9579062; DOI=10.1099/00221287-144-4-877;
RA Rivolta C., Soldo B., Lazarevic V., Joris B., Mauel C., Karamata D.;
RT "A 35.7 kb DNA fragment from the Bacillus subtilis chromosome containing a
RT putative 12.3 kb operon involved in hexuronate catabolism and a perfectly
RT symmetrical hypothetical catabolite-responsive element.";
RL Microbiology 144:877-884(1998).
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 PROBABLE OPERON STRUCTURE, AND INDUCTION.
RC STRAIN=168 / MB24;
RX PubMed=9882655; DOI=10.1128/jb.181.2.426-433.1999;
RA Mekjian K.R., Bryan E.M., Beall B.W., Moran C.P. Jr.;
RT "Regulation of hexuronate utilization in Bacillus subtilis.";
RL J. Bacteriol. 181:426-433(1999).
CC -!- FUNCTION: Transport of aldohexuronates such as D-glucuronate and D-
CC galacturonate. {ECO:0000305|PubMed:9882655}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=aldehydo-D-glucuronate(in) + H(+)(in) = aldehydo-D-
CC glucuronate(out) + H(+)(out); Xref=Rhea:RHEA:28955,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:142686;
CC Evidence={ECO:0000305|PubMed:9882655};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=aldehydo-D-galacturonate(out) + H(+)(out) = aldehydo-D-
CC galacturonate(in) + H(+)(in); Xref=Rhea:RHEA:29295,
CC ChEBI:CHEBI:12952, ChEBI:CHEBI:15378;
CC Evidence={ECO:0000305|PubMed:9882655};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Induced by galacturonate, repressed by glucose.
CC {ECO:0000305|PubMed:9882655}.
CC -!- MISCELLANEOUS: Member of the exu locus which is required for
CC galacturonate utilization.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Phthalate
CC permease family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF015825; AAC46332.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13093.1; -; Genomic_DNA.
DR PIR; A69853; A69853.
DR RefSeq; NP_389118.1; NC_000964.3.
DR RefSeq; WP_003245531.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O34456; -.
DR SMR; O34456; -.
DR STRING; 224308.BSU12360; -.
DR PaxDb; O34456; -.
DR EnsemblBacteria; CAB13093; CAB13093; BSU_12360.
DR GeneID; 939405; -.
DR KEGG; bsu:BSU12360; -.
DR PATRIC; fig|224308.179.peg.1337; -.
DR eggNOG; COG2271; Bacteria.
DR InParanoid; O34456; -.
DR OMA; LDRFCSK; -.
DR PhylomeDB; O34456; -.
DR BioCyc; BSUB:BSU12360-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR000849; Sugar_P_transporter.
DR Pfam; PF07690; MFS_1; 1.
DR PIRSF; PIRSF002808; Hexose_phosphate_transp; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..422
FT /note="Hexuronate transporter"
FT /id="PRO_0000121381"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 422 AA; 45314 MW; C2E291AF347F7EDD CRC64;
MFSKDKLPVI LFLFLAGVIN YLDRSALSIA APFIQDDLTL SATQMGLIFS SFSIGYAIFN
FLGGVASDRY GAKLTLFVAM VVWSLFSGAV ALAFGFVSLL IIRILFGMGE GPLSATINKM
VNNWFPPTQR ASVIGVTNSG TPLGGAISGP IVGMIAVAFS WKVSFVLIMI IGLIWAVLWF
KFVKEKPQET IKEAPAIKAE TSPGEKIPLT FYLKQKTVLF TAFAFFAYNY ILFFFLTWFP
SYLVDERGLS VESMSVITVI PWILGFIGLA AGGFVSDYVY KKTARKGVLF SRKVVLVTCL
FSSAVLIGFA GLVATTAGAV TLVALSVFFL YLTGAIYWAV IQDVVDQNNV GSVGGFMHFL
ANTAGIIGPA LTGFIVDQTG TFSGAFLLAG GLAVFASLAV IRFVRPIIGK PAGTEAENPV
SY
