PTUCB_LEPBD
ID PTUCB_LEPBD Reviewed; 529 AA.
AC C7NB69;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=PTS system alpha-glucoside-specific EIICB component;
DE Includes:
DE RecName: Full=Alpha-glucoside permease IIC component;
DE AltName: Full=PTS system alpha-glucoside-specific EIIC component;
DE Includes:
DE RecName: Full=Alpha-glucoside-specific phosphotransferase enzyme IIB component;
DE EC=2.7.1.-;
DE AltName: Full=PTS system alpha-glucoside-specific EIIB component;
GN OrderedLocusNames=Lebu_1527;
OS Leptotrichia buccalis (strain ATCC 14201 / DSM 1135 / JCM 12969 / NCTC
OS 10249 / C-1013-b).
OC Bacteria; Fusobacteria; Fusobacteriales; Leptotrichiaceae; Leptotrichia.
OX NCBI_TaxID=523794;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14201 / DSM 1135 / JCM 12969 / NCTC 10249 / C-1013-b;
RX PubMed=21304648; DOI=10.4056/sigs.1854;
RA Ivanova N., Gronow S., Lapidus A., Copeland A., Glavina Del Rio T.,
RA Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E., Bruce D.,
RA Goodwin L., Brettin T., Detter J.C., Han C., Pitluck S., Mikhailova N.,
RA Pati A., Mavrommatis K., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Chain P., Rohde C., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Leptotrichia buccalis type strain (C-1013-
RT b).";
RL Stand. Genomic Sci. 1:126-132(2009).
RN [2]
RP FUNCTION.
RC STRAIN=ATCC 14201 / DSM 1135 / JCM 12969 / NCTC 10249 / C-1013-b;
RX PubMed=22230464; DOI=10.1111/j.2041-1014.2011.00627.x;
RA Thompson J., Pikis A.;
RT "Metabolism of sugars by genetically diverse species of oral
RT Leptotrichia.";
RL Mol. Oral. Microbiol. 27:34-44(2012).
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. This
CC system is probably involved in transport of the alpha-glucosides
CC trehalulose, turanose, maltulose and palatinose.
CC {ECO:0000269|PubMed:22230464}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00426}; Multi-pass membrane protein {ECO:0000255|PROSITE-
CC ProRule:PRU00426}.
CC -!- DOMAIN: The EIIC domain forms the PTS system translocation channel and
CC contains the specific substrate-binding site.
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.
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DR EMBL; CP001685; ACV39400.1; -; Genomic_DNA.
DR RefSeq; WP_015769741.1; NC_013192.1.
DR AlphaFoldDB; C7NB69; -.
DR SMR; C7NB69; -.
DR STRING; 523794.Lebu_1527; -.
DR TCDB; 4.A.1.1.16; the pts glucose-glucoside (glc) family.
DR PRIDE; C7NB69; -.
DR EnsemblBacteria; ACV39400; ACV39400; Lebu_1527.
DR KEGG; lba:Lebu_1527; -.
DR eggNOG; COG1263; Bacteria.
DR eggNOG; COG1264; Bacteria.
DR HOGENOM; CLU_012312_1_0_0; -.
DR OMA; WIPMFHN; -.
DR OrthoDB; 2035550at2; -.
DR Proteomes; UP000001910; 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:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00212; PTS_IIB_glc; 1.
DR Gene3D; 3.30.1360.60; -; 1.
DR InterPro; IPR036878; Glu_permease_IIB.
DR InterPro; IPR018113; PTrfase_EIIB_Cys.
DR InterPro; IPR003352; PTS_EIIC.
DR InterPro; IPR013013; PTS_EIIC_1.
DR InterPro; IPR001996; PTS_IIB_1.
DR InterPro; IPR010975; PTS_IIBC_a_glc.
DR Pfam; PF00367; PTS_EIIB; 1.
DR Pfam; PF02378; PTS_EIIC; 1.
DR SUPFAM; SSF55604; SSF55604; 1.
DR TIGRFAMs; TIGR00826; EIIB_glc; 1.
DR TIGRFAMs; TIGR02005; PTS-IIBC-alpha; 1.
DR PROSITE; PS51098; PTS_EIIB_TYPE_1; 1.
DR PROSITE; PS01035; PTS_EIIB_TYPE_1_CYS; 1.
DR PROSITE; PS51103; PTS_EIIC_TYPE_1; 1.
PE 3: Inferred from homology;
KW Cell membrane; Kinase; Membrane; Phosphotransferase system;
KW Reference proteome; Sugar transport; Transferase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..529
FT /note="PTS system alpha-glucoside-specific EIICB component"
FT /id="PRO_5000507514"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 380..400
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN 1..416
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN 450..529
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT ACT_SITE 472
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
SQ SEQUENCE 529 AA; 57788 MW; FDC92750A3AAAC2A CRC64;
MMKKVQRFGG AMMAPVLLFA FTGIVVGLSS VFTNTEVMGK IAEEGTVWYN FWYVISEGGW
TVFRQMPILF AIGLPISLAT KTNARACMET FALYTTFNYF VAAILKVFYG IDAAKQVADK
VTGYSAIGGV PTLDTNLFGG ILIAALVVYL HNKYFDKKLP DFLGVFQGSV FVYIVGFVVM
IPCAFLTVLI WPKFQMGISA LQGFMKASGI FGVWIYTFLE RILIPTGLHH FVYTPFVFGP
AAVPDGIQVY WVQHIKEFAQ STQSLKSLFP QGGFALHGNS KIFGAPGIAL AMYATAKSDK
KKAVAALLIP IIFTAVISGI TEPLEFTFLF IAPVLFAVHA CLAATMAATM YAFGVVGNMG
GGLLDFFFLN WIPMFKNHSG TVIAQIVIGL IFTAIYFVVF RFLILKMDLK TPGREDEDEE
MKLYSKADYR AKHGEGDAKG GVSSAEDEYA QKGAIILEAL GGKENIEELN NCATRLRVSV
KDASKLLPDA AFKAAGAHGV VRKGTAIQVI IGLSVPQVRE RIEEMMKKG
