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 01-MAY-2013, entry version 74.
DE RecName: Full=Oligo-beta-mannoside-specific phosphotransferase enzyme IIA component;
DE EC=2.7.1.-;
DE AltName: Full=Glucomannan utilization protein A;
DE AltName: Full=PTS system oligo-beta-mannoside-specific EIIA component;
GN Name=gmuA; Synonyms=ydhN; 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
RT the 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.,
RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA 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.,
RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA 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.,
RA Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus
RT subtilis 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP INDUCTION, AND FUNCTION IN GLUCOMANNAN UTILIZATION.
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
CC phosphotransferase system (sugar PTS), a major carbohydrate active
CC -transport system, catalyzes the phosphorylation of incoming sugar
CC substrates concomitantly with their translocation across the cell
CC membrane. This system is involved in the transport of oligo-
CC glucomannans such as cellobiose or mannobiose (Probable).
CC -!- CATALYTIC ACTIVITY: Protein EIIA N(pi)-phospho-L-histidine +
CC protein EIIB = protein EIIA + protein EIIB N(pi)-phospho-L-
CC histidine/cysteine.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC -!- INDUCTION: Up-regulated by konjac glucomannan and by cellobiose
CC and mannobiose, the possible degradation products of glucomannan.
CC Repressed by glucose via the carbon catabolite repression system.
CC Also repressed by GmuR.
CC -!- DOMAIN: The EIIA domain is phosphorylated by phospho-HPr on a
CC histidyl residue. Then, it transfers the phosphoryl group to the
CC EIIB domain.
CC -!- SIMILARITY: Contains 1 PTS EIIA type-3 domain.
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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 HSSP; P69791; 1WCR.
DR ProteinModelPortal; O05506; -.
DR SMR; O05506; 8-109.
DR STRING; 224308.BSU05820; -.
DR PaxDb; O05506; -.
DR EnsemblBacteria; CAB12401; CAB12401; BSU05820.
DR GeneID; 938039; -.
DR KEGG; bsu:BSU05820; -.
DR PATRIC; 18972780; VBIBacSub10457_0611.
DR GenoList; BSU05820; -.
DR eggNOG; COG1447; -.
DR HOGENOM; HOG000224338; -.
DR KO; K02759; -.
DR ProtClustDB; CLSK873753; -.
DR BioCyc; BSUB:BSU05820-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0005351; F:sugar:hydrogen symporter activity; IEA:InterPro.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR GO; GO:0015774; P:polysaccharide transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.58.80; -; 1.
DR InterPro; IPR003188; PTS_IIA_lac.
DR Pfam; PF02255; PTS_IIA; 1.
DR PIRSF; PIRSF000699; PTS_IILac_III; 1.
DR SUPFAM; SSF46973; Ptrans_IIA; 1.
DR PROSITE; PS51095; PTS_EIIA_TYPE_3; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Cytoplasm; Kinase; Phosphotransferase system;
KW Polysaccharide transport; Reference proteome; Sugar transport;
KW Transferase; Transport.
FT CHAIN 1 110 Oligo-beta-mannoside-specific
FT phosphotransferase enzyme IIA component.
FT /FTId=PRO_0000372433.
FT DOMAIN 9 107 PTS EIIA type-3.
FT ACT_SITE 83 83 Tele-phosphohistidine intermediate; by
FT HPr (By similarity).
FT CONFLICT 11 11 D -> G (in Ref. 1; BAA19706).
SQ SEQUENCE 110 AA; 12408 MW; AF4EB855B901833A CRC64;
MEQMKITNLT DEQISFQLIL HSGNARSCII QSLRAYKEGK KDEADALIAK AEQDLSAAHD
IHFQMIQKES GGEATAFSLL LMHAEDHLMS TLSMKELVKE MLDLFKTKNI
//
