PTEA_BACSU
ID PTEA_BACSU Reviewed; 110 AA.
AC O05506; Q797E1;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=PTS system oligo-beta-mannoside-specific EIIA component {ECO:0000303|PubMed:18177310};
DE AltName: Full=Glucomannan utilization protein A {ECO:0000303|PubMed:18177310};
DE AltName: Full=Oligo-beta-mannoside-specific phosphotransferase enzyme IIA component {ECO:0000303|PubMed:18177310};
GN Name=gmuA {ECO:0000303|PubMed:18177310}; Synonyms=ydhN;
GN OrderedLocusNames=BSU05820;
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 / JH642;
RX PubMed=9202461; DOI=10.1099/00221287-143-6-1861;
RA Sadaie Y., Yata K., Fujita M., Sagai H., Itaya M., Kasahara Y.,
RA Ogasawara N.;
RT "Nucleotide sequence and analysis of the phoB-rrnE-groESL region of the
RT Bacillus subtilis chromosome.";
RL Microbiology 143:1861-1866(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 SEQUENCE REVISION TO 11.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP FUNCTION IN GLUCOMANNAN UTILIZATION, CATALYTIC ACTIVITY, AND INDUCTION.
RC STRAIN=168;
RX PubMed=18177310; DOI=10.1111/j.1574-6968.2007.01018.x;
RA Sadaie Y., Nakadate H., Fukui R., Yee L.M., Asai K.;
RT "Glucomannan utilization operon of Bacillus subtilis.";
RL FEMS Microbiol. Lett. 279:103-109(2008).
CC -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC system (sugar PTS), a major carbohydrate active transport system,
CC catalyzes the phosphorylation of incoming sugar substrates
CC concomitantly with their translocation across the cell membrane. The
CC enzyme II GmuABC PTS system is involved in the transport of oligo-
CC glucomannans such as cellobiose or mannobiose.
CC {ECO:0000305|PubMed:18177310}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Up-regulated by konjac glucomannan and by cellobiose and
CC mannobiose, the possible degradation products of glucomannan. Repressed
CC by glucose via the carbon catabolite repression system. Also repressed
CC by GmuR. {ECO:0000269|PubMed:18177310}.
CC -!- DOMAIN: The PTS EIIA type-3 domain is phosphorylated by phospho-HPr on
CC a histidyl residue. Then, it transfers the phosphoryl group to the PTS
CC EIIB type-3 domain. {ECO:0000255|PROSITE-ProRule:PRU00418}.
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DR EMBL; D88802; BAA19706.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12401.2; -; Genomic_DNA.
DR PIR; B69785; B69785.
DR RefSeq; NP_388463.2; NC_000964.3.
DR RefSeq; WP_003243550.1; NZ_JNCM01000031.1.
DR AlphaFoldDB; O05506; -.
DR SMR; O05506; -.
DR STRING; 224308.BSU05820; -.
DR TCDB; 4.A.3.2.10; the pts lactose-n,n'-diacetylchitobiose-Beta-glucoside (lac) family.
DR PaxDb; O05506; -.
DR PRIDE; O05506; -.
DR EnsemblBacteria; CAB12401; CAB12401; BSU_05820.
DR GeneID; 938039; -.
DR KEGG; bsu:BSU05820; -.
DR PATRIC; fig|224308.179.peg.626; -.
DR eggNOG; COG1447; Bacteria.
DR OMA; EVFETRA; -.
DR PhylomeDB; O05506; -.
DR BioCyc; BSUB:BSU05820-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0015774; P:polysaccharide transport; IEA:UniProtKB-KW.
DR CDD; cd00215; PTS_IIA_lac; 1.
DR InterPro; IPR003188; PTS_IIA_lac/cel.
DR InterPro; IPR036542; PTS_IIA_lac/cel_sf.
DR PANTHER; PTHR34382; PTHR34382; 1.
DR Pfam; PF02255; PTS_IIA; 1.
DR PIRSF; PIRSF000699; PTS_IILac_III; 1.
DR SUPFAM; SSF46973; SSF46973; 1.
DR PROSITE; PS51095; PTS_EIIA_TYPE_3; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Kinase; Phosphoprotein; Phosphotransferase system;
KW Polysaccharide transport; Reference proteome; Sugar transport; Transferase;
KW Transport.
FT CHAIN 1..110
FT /note="PTS system oligo-beta-mannoside-specific EIIA
FT component"
FT /id="PRO_0000372433"
FT DOMAIN 9..107
FT /note="PTS EIIA type-3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00418"
FT ACT_SITE 83
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000305"
FT MOD_RES 83
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00418"
FT CONFLICT 11
FT /note="D -> G (in Ref. 1; BAA19706)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 110 AA; 12408 MW; AF4EB855B901833A CRC64;
MEQMKITNLT DEQISFQLIL HSGNARSCII QSLRAYKEGK KDEADALIAK AEQDLSAAHD
IHFQMIQKES GGEATAFSLL LMHAEDHLMS TLSMKELVKE MLDLFKTKNI
