MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
Description | RecName: Full=PTS system glucitol/sorbitol-specific EIIB component {ECO:0000250|UniProtKB:P56580}; EC=2.7.1.198 {ECO:0000250|UniProtKB:P56580}; AltName: Full=EII-Gut {ECO:0000250|UniProtKB:P56580}; AltName: Full=Enzyme II-Gut {ECO:0000250|UniProtKB:P56580}; AltName: Full=Glucitol/sorbitol-specific phosphotransferase enzyme IIB component {ECO:0000250|UniProtKB:P56580}; |
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MyHits synonyms | PTHB_CLOB8 , O32333 , A6LQ95 , D766D0501EA10694 |
![]() Legends: 1, ACT_SITE Phosphocysteine intermediate; for EIIB activity. {ECO:0000305}; 2, Phosphocysteine; by EIIA. {ECO:0000255|PROSITE-ProRule:PRU00425}; 3, TRANSMEM Helical. {ECO:0000255}.
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ID PTHB_CLOB8 Reviewed; 336 AA. AC O32333; A6LQ95; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 02-NOV-2016, entry version 103. DE RecName: Full=PTS system glucitol/sorbitol-specific EIIB component {ECO:0000250|UniProtKB:P56580}; DE EC=2.7.1.198 {ECO:0000250|UniProtKB:P56580}; DE AltName: Full=EII-Gut {ECO:0000250|UniProtKB:P56580}; DE AltName: Full=Enzyme II-Gut {ECO:0000250|UniProtKB:P56580}; DE AltName: Full=Glucitol/sorbitol-specific phosphotransferase enzyme IIB component {ECO:0000250|UniProtKB:P56580}; GN Name=srlE; Synonyms=gutA2; OrderedLocusNames=Cbei_0337; OS Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium OS acetobutylicum). OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=290402; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION. RC STRAIN=ATCC 51743 / NCIMB 8052; RX PubMed=9572925; RA Tangney M., Brehm J.K., Minton N.P., Mitchell W.J.; RT "A gene system for glucitol transport and metabolism in Clostridium RT beijerinckii NCIMB 8052."; RL Appl. Environ. Microbiol. 64:1612-1619(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51743 / NCIMB 8052; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., RA Pitluck S., Sims D., Brettin T., Bruce D., Tapia R., Brainard J., RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Bennet G., Cann I., Chen J.-S., Contreras A.L., RA Jones D., Kashket E., Mitchell W., Stoddard S., Schwarz W., RA Qureshi N., Young M., Shi Z., Ezeji T., White B., Blaschek H., RA Richardson P.; RT "Complete sequence of Clostridium beijerinckii NCIMB 8052."; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. 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. The enzyme II complex composed of SrlA, SrlB and SrlE is CC involved in glucitol/sorbitol transport. CC {ECO:0000305|PubMed:9572925}. CC -!- CATALYTIC ACTIVITY: [Protein]-N(pi)-phospho-L-histidine + D- CC sorbitol(Side 1) = [protein]-L-histidine + D-sorbitol 6- CC phosphate(Side 2). {ECO:0000250|UniProtKB:P56580}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000255}. CC -!- INDUCTION: Activated by sorbitol and repressed by glucose. CC {ECO:0000269|PubMed:9572925}. CC -!- DOMAIN: The EIIB domain is phosphorylated by phospho-EIIA on a CC cysteinyl or histidyl residue, depending on the transported sugar. CC Then, it transfers the phosphoryl group to the sugar substrate CC concomitantly with the sugar uptake processed by the EIIC domain. CC {ECO:0000255|PROSITE-ProRule:PRU00425}. CC -!- SIMILARITY: Contains 1 PTS EIIB type-5 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00425}. DR EMBL; AJ002527; CAA05514.1; -; Genomic_DNA. DR EMBL; CP000721; ABR32525.1; -; Genomic_DNA. DR RefSeq; WP_011967686.1; NC_009617.1. DR STRING; 290402.Cbei_0337; -. DR TCDB; 4.A.4.1.2; the pts glucitol (gut) family. DR EnsemblBacteria; ABR32525; ABR32525; Cbei_0337. DR KEGG; cbe:Cbei_0337; -. DR PATRIC; 19344528; VBICloBei69853_0347. DR eggNOG; ENOG4105DZY; Bacteria. DR eggNOG; COG3732; LUCA. DR HOGENOM; HOG000242653; -. DR KO; K02782; -. DR KO; K02783; -. DR OMA; ALAIVDC; -. DR OrthoDB; POG091H0RIL; -. DR Proteomes; UP000000565; 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:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro. DR GO; GO:0090563; F:protein-phosphocysteine-sugar phosphotransferase activity; ISS:UniProtKB. DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; ISS:UniProtKB. DR InterPro; IPR011638; PTS_EIIBC_GUT_C. DR InterPro; IPR011618; PTS_EIIBC_GUT_N. DR InterPro; IPR004702; PTS_sorb_EIIBC. DR Pfam; PF07663; EIIBC-GUT_C; 1. DR Pfam; PF03612; EIIBC-GUT_N; 1. DR TIGRFAMs; TIGR00825; EIIBC-GUT; 1. DR PROSITE; PS51102; PTS_EIIB_TYPE_5; 1. PE 2: Evidence at transcript level; KW Cell membrane; Complete proteome; Kinase; Membrane; Phosphoprotein; KW Phosphotransferase system; Reference proteome; Sugar transport; KW Transferase; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 336 PTS system glucitol/sorbitol-specific FT EIIB component. FT /FTId=PRO_0000186564. FT TRANSMEM 194 214 Helical. {ECO:0000255}. FT TRANSMEM 228 248 Helical. {ECO:0000255}. FT TRANSMEM 250 270 Helical. {ECO:0000255}. FT TRANSMEM 278 298 Helical. {ECO:0000255}. FT TRANSMEM 312 332 Helical. {ECO:0000255}. FT DOMAIN 3 195 PTS EIIB type-5. {ECO:0000255|PROSITE- FT ProRule:PRU00425}. FT ACT_SITE 75 75 Phosphocysteine intermediate; for EIIB FT activity. {ECO:0000305}. FT MOD_RES 75 75 Phosphocysteine; by EIIA. FT {ECO:0000255|PROSITE-ProRule:PRU00425}. CC -------------------------------------------------------------------------- CC The following FT lines are automated annotations from the MyHits database. CC -------------------------------------------------------------------------- FT MYHIT 3 195 iprf:PTS_EIIB_TYPE_5 [T] FT MYHIT 6 188 ipfam:EIIBC-GUT_N [T] FT MYHIT 243 335 ipfam:EIIBC-GUT_C [T] SQ SEQUENCE 336 AA; 35174 MW; D766D0501EA10694 CRC64; MEKYNAIKIV KGSGGFGGPL TVKPEEGKDT LLYITGGGAE PEIVEKIVNL TGCKAVNGFK TSVPEEQIFL VIIDCGGTLR CGIYPQKRIP TINVMPVGKS GPLAKFITED IYVSAVGLNQ ISLADSSAEP IKSTKVPEEG KREFKYSADK KVSQSLAENS KSSIVQKIGM GAGKVVNTLY QAGRDAVQSM ITTILPFMAF VAMLIGIIQG SGFGNWFAKI LVPLAGNGIG LMILGFICSI PLLSALLGPG AVIAQIVGTL IGVEIGKGTI PPSLALPALF AINTQCACDF IPVGLGLAEA EPETVEVGVP SVLYSRFMIG VPRVAVAWVA SIGLYQ // |