(data stored in SCRATCH zone)

SWISSPROT: PTMCB_BACSU

ID   PTMCB_BACSU             Reviewed;         478 AA.
AC   P42956; P94435;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 4.
DT   11-DEC-2019, entry version 149.
DE   RecName: Full=PTS system mannitol-specific EIICB component {ECO:0000303|PubMed:8574415};
DE   AltName: Full=EIICB-Mtl {ECO:0000250|UniProtKB:P28008};
DE            Short=EII-Mtl {ECO:0000250|UniProtKB:P28008};
DE   Includes:
DE     RecName: Full=Mannitol permease IIC component {ECO:0000250|UniProtKB:P28008};
DE     AltName: Full=PTS system mannitol-specific EIIC component {ECO:0000250|UniProtKB:P28008};
DE   Includes:
DE     RecName: Full=Mannitol-specific phosphotransferase enzyme IIB component {ECO:0000250|UniProtKB:P28008};
DE              EC=2.7.1.197 {ECO:0000250|UniProtKB:P00550, ECO:0000250|UniProtKB:P28008};
DE     AltName: Full=PTS system mannitol-specific EIIB component {ECO:0000250|UniProtKB:P28008};
GN   Name=mtlA {ECO:0000303|PubMed:8574415}; OrderedLocusNames=BSU03981;
GN   ORFNames=BSU03980;
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=8574415; DOI=10.1099/13500872-141-12-3241;
RA   Akagawa E., Kurita K., Sugawara T., Nakamura K., Kasahara Y., Ogasawara N.,
RA   Yamane K.;
RT   "Determination of a 17,484 bp nucleotide sequence around the 39 degrees
RT   region of the Bacillus subtilis chromosome and similarity analysis of the
RT   products of putative ORFs.";
RL   Microbiology 141:3241-3245(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969502; DOI=10.1099/13500872-142-11-3047;
RA   Yamane K., Kumano M., Kurita K.;
RT   "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT   determination of the sequence of a 146 kb segment and identification of 113
RT   genes.";
RL   Microbiology 142:3047-3056(1996).
RN   [3]
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   [4]
RP   SEQUENCE REVISION TO 133; 187; 234; 274-290; 380-415 AND C-TERMINUS.
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).
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 CmtAB PTS system is involved in D-mannitol transport.
CC       {ECO:0000250|UniProtKB:P28008}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-mannitol(out) + N(pros)-phospho-L-histidyl-[protein] = D-
CC         mannitol 1-phosphate(in) + L-histidyl-[protein];
CC         Xref=Rhea:RHEA:33363, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746,
CC         ChEBI:CHEBI:16899, ChEBI:CHEBI:29979, ChEBI:CHEBI:61381,
CC         ChEBI:CHEBI:64837; EC=2.7.1.197;
CC         Evidence={ECO:0000250|UniProtKB:P00550,
CC         ECO:0000250|UniProtKB:P28008};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P28008}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00427}; Multi-pass membrane protein {ECO:0000255|PROSITE-
CC       ProRule:PRU00427}.
CC   -!- DOMAIN: The EIIC type-2 domain forms the PTS system translocation
CC       channel and contains the specific substrate-binding site.
CC       {ECO:0000255|PROSITE-ProRule:PRU00427}.
CC   -!- DOMAIN: The PTS EIIB type-2 domain is phosphorylated by phospho-EIIA on
CC       a cysteinyl residue. Then, it transfers the phosphoryl group to the
CC       sugar substrate concomitantly with the sugar uptake processed by the
CC       PTS EIIC type-2 domain. {ECO:0000255|PROSITE-ProRule:PRU00422}.
CC   -!- CAUTION: Was originally thought to be a longer ORF that encodes what is
CC       now known to be mtlA and mtlF. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA07350.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAA09029.1; Type=Frameshift; Evidence={ECO:0000305};
DR   EMBL; D38161; BAA07350.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; D50453; BAA09029.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AL009126; CAB12206.2; -; Genomic_DNA.
DR   PIR; E69661; E69661.
DR   RefSeq; NP_388280.2; NC_000964.3.
DR   RefSeq; WP_010886406.1; NZ_JNCM01000031.1.
DR   SMR; P42956; -.
DR   STRING; 224308.BSU03981; -.
DR   TCDB; 4.A.2.1.5; the pts fructose-mannitol (fru) family.
DR   PaxDb; P42956; -.
DR   PRIDE; P42956; -.
DR   EnsemblBacteria; CAB12206; CAB12206; BSU03981.
DR   GeneID; 938263; -.
DR   KEGG; bsu:BSU03981; -.
DR   PATRIC; fig|224308.179.peg.421; -.
DR   eggNOG; COG2213; LUCA.
DR   HOGENOM; HOG000252814; -.
DR   InParanoid; P42956; -.
DR   KO; K02799; -.
DR   KO; K02800; -.
DR   OMA; SIIHFFG; -.
DR   PhylomeDB; P42956; -.
DR   BioCyc; BSUB:BSU03981-MONOMER; -.
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:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0022872; F:protein-N(PI)-phosphohistidine-mannitol phosphotransferase system transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   CDD; cd05567; PTS_IIB_mannitol; 1.
DR   InterPro; IPR036095; PTS_EIIB-like_sf.
DR   InterPro; IPR013011; PTS_EIIB_2.
DR   InterPro; IPR003501; PTS_EIIB_2/3.
DR   InterPro; IPR029503; PTS_EIIB_mannitol.
DR   InterPro; IPR003352; PTS_EIIC.
DR   InterPro; IPR013014; PTS_EIIC_2.
DR   InterPro; IPR004718; PTS_IIC_mtl.
DR   Pfam; PF02378; PTS_EIIC; 1.
DR   Pfam; PF02302; PTS_IIB; 1.
DR   SUPFAM; SSF52794; SSF52794; 1.
DR   TIGRFAMs; TIGR00851; mtlA; 1.
DR   PROSITE; PS51099; PTS_EIIB_TYPE_2; 1.
DR   PROSITE; PS51104; PTS_EIIC_TYPE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; P42956.
DR   SWISS-2DPAGE; P42956.
KW   Cell membrane; Kinase; Membrane; Phosphoprotein; Phosphotransferase system;
KW   Reference proteome; Sugar transport; Transferase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..478
FT                   /note="PTS system mannitol-specific EIICB component"
FT                   /id="PRO_0000186610"
FT   TOPO_DOM        1..29
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P00550"
FT   TRANSMEM        30..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00550"
FT   TOPO_DOM        52..55
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P00550"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00550"
FT   TOPO_DOM        77..139
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P00550"
FT   TRANSMEM        140..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00550"
FT   TOPO_DOM        162..170
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P00550"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00550"
FT   TOPO_DOM        192..278
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P00550"
FT   TRANSMEM        279..298
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00550"
FT   TOPO_DOM        299..318
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P00550"
FT   TRANSMEM        319..340
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00550"
FT   TOPO_DOM        341..478
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P00550"
FT   DOMAIN          18..347
FT                   /note="PTS EIIC type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   DOMAIN          390..478
FT                   /note="PTS EIIB type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT   ACT_SITE        396
FT                   /note="Phosphocysteine intermediate; for EIIB activity"
FT                   /evidence="ECO:0000250|UniProtKB:P00550,
FT                   ECO:0000250|UniProtKB:P28008"
FT   MOD_RES         396
FT                   /note="Phosphocysteine; by EIIA"
FT                   /evidence="ECO:0000250|UniProtKB:P00550,
FT                   ECO:0000250|UniProtKB:P28008, ECO:0000255|PROSITE-
FT                   ProRule:PRU00422"
FT   CONFLICT        133..135
FT                   /note="EML -> GIR (in Ref. 1; BAA07350)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        133
FT                   /note="E -> G (in Ref. 2; BAA09029)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        187
FT                   /note="V -> L (in Ref. 1; BAA07350 and 2; BAA09029)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        234
FT                   /note="L -> F (in Ref. 1; BAA07350 and 2; BAA09029)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        274..290
FT                   /note="ALILAAIAGGASGLLTF -> GPDSRSHCRRSKRTLNI (in Ref. 1;
FT                   BAA07350 and 2; BAA09029)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        380..415
FT                   /note="EASELSPESVNKIIFACDAGMGSSAMGASILRNKVK -> KRLSCLLKARTK
FT                   LSFRVIRDGIKCHGGIHLKKQSE (in Ref. 1; BAA07350 and 2;
FT                   BAA09029)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   478 AA;  50185 MW;  368BF52A316CC235 CRC64;
     MQQQEQQQGG MKVKVQRFGS YLSGMIMPNI GAFIAWGIIT ALFIPAGWFP NEQLNTLVSP
     MITYLLPLLI AYTGGKMIYD HRGGVVGATA AIGVIVGSDI PMFLGAMIMG PLGGYLIKQT
     DKLFKDKVKQ GFEMLINNFT AGIVGAALTI LAFYAIGPVV LTLNKLLAAG VEVIVHANLL
     PVASVFVEPA KVLFLNNAIN HGILSPIGIE QASQTGKSIL FLVEANPGPG LGILLAYMFF
     GKGSSKSTAP GAAIIHFFGG IHEIYFPYIL MKPALILAAI AGGASGLLTF TIFNAGLVAA
     ASPGSIIALM AMTPRGGYFG VLAGVLVAAA VSFIVSAVIL KSSKASEEDL AAATEKMQSM
     KGKKSQAAAA LEAEQAKAEE ASELSPESVN KIIFACDAGM GSSAMGASIL RNKVKKAELD
     ISVTNTAINN LPSDADIVIT HKDLTDRAKA KLPNATHISV DNFLNSPKYD ELIEKLKK
//

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