PTSBC_KLEPN
ID PTSBC_KLEPN Reviewed; 456 AA.
AC P27219;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=PTS system sucrose-specific EIIBC component;
DE AltName: Full=EIIBC-Scr;
DE Short=EII-Scr;
DE Includes:
DE RecName: Full=Sucrose-specific phosphotransferase enzyme IIB component;
DE EC=2.7.1.-;
DE AltName: Full=PTS system sucrose-specific EIIB component;
DE Includes:
DE RecName: Full=Sucrose permease IIC component;
DE AltName: Full=PTS system sucrose-specific EIIC component;
GN Name=scrA;
OS Klebsiella pneumoniae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1033-5P14 / KAY2026;
RX PubMed=8628219; DOI=10.1007/bf02174179;
RA Titgemeyer F., Jahreis K., Ebner R., Lengeler J.W.;
RT "Molecular analysis of the scrA and scrB genes from Klebsiella pneumoniae
RT and plasmid pUR400, which encode the sucrose transport protein Enzyme II
RT Scr of the phosphotransferase system and a sucrose-6-phosphate invertase.";
RL Mol. Gen. Genet. 250:197-206(1996).
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 involved in sucrose transport.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
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 -!- DOMAIN: The EIIC domain forms the PTS system translocation channel and
CC contains the specific substrate-binding site.
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DR EMBL; X57401; CAA40658.1; -; Genomic_DNA.
DR PIR; S62331; S62331.
DR RefSeq; WP_002892640.1; NZ_WYAM01000013.1.
DR AlphaFoldDB; P27219; -.
DR SMR; P27219; -.
DR OMA; LITHAGW; -.
DR OrthoDB; 196185at2; -.
DR BioCyc; MetaCyc:MON-12625; -.
DR BRENDA; 2.7.1.211; 2814.
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; IPR010973; PTS_IIBC_sucr.
DR InterPro; IPR004719; PTS_maltose/Glc_sub_IIC.
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; TIGR00852; pts-Glc; 1.
DR TIGRFAMs; TIGR01996; PTS-II-BC-sucr; 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 4: Predicted;
KW Cell inner membrane; Cell membrane; Kinase; Membrane;
KW Phosphotransferase system; Sugar transport; Transferase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..456
FT /note="PTS system sucrose-specific EIIBC component"
FT /id="PRO_0000186668"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 144..164
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 428..448
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN 1..87
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT DOMAIN 107..456
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT ACT_SITE 26
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
SQ SEQUENCE 456 AA; 48022 MW; 4AFDF5405CAEFC66 CRC64;
MDFEQISRSL LPLLGGKENI ASAAHCATRL RLVLVDDALA DQQAIGKIDG VKGCFRNAGQ
MQIIFGTGVV NKVYAAFIQA AGISESSKSE AADLAAKKLN PFQRIARLLS NIFVPIIPAI
VASGLLMGLL GMVKTYGWVD PSNALYIMLD MCSSAAFIIL PILIGFTAAR EFGGNPYLGA
TLGGILTHPA LTNAWGVAAG FHTMNFFGIE VAMIGYQGTV FPVLLAVWFM SMVEKRLRRV
IPDALDLILT PFLTVIISGF IALLLIGPAG RALGDGISFI LSTLISHAGW LAGLLFGGLY
SVIVITGIHH SFHAIEAGLL GNPSIGVNFL LPIWAMANVA QGGACFAVWF KTKDAKIKAI
TLPSAFSAML GITEAAIFGI NLRFVKPFIA ALVGGAAGGA WVVSMHVYMT AVGLTAIPGM
AIVQASSLLN YIIGMAIAFA VAFALSLTLK YKTDAE
