PTIBC_ECOLI
ID PTIBC_ECOLI Reviewed; 485 AA.
AC P24241; Q2MAB4; Q46880; Q6BF64;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 3.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=PTS system arbutin-, cellobiose-, and salicin-specific EIIBC component;
DE AltName: Full=EIIBC-Asc;
DE Short=EII-Asc;
DE Includes:
DE RecName: Full=Arbutin-, cellobiose-, and salicin-specific phosphotransferase enzyme IIB component;
DE EC=2.7.1.-;
DE AltName: Full=PTS system arbutin-, cellobiose-, and salicin-specific EIIB component;
DE Includes:
DE RecName: Full=Arbutin, cellobiose, and salicin permease IIC component;
DE AltName: Full=PTS system arbutin-, cellobiose-, and salicin-specific EIIC component;
GN Name=ascF; OrderedLocusNames=b2715, JW5435;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630307; DOI=10.1093/oxfordjournals.molbev.a040753;
RA Hall B.G., Xu L.;
RT "Nucleotide sequence, function, activation, and evolution of the cryptic
RT asc operon of Escherichia coli K12.";
RL Mol. Biol. Evol. 9:688-706(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP SEQUENCE REVISION TO 167-170.
RX PubMed=16397293; DOI=10.1093/nar/gkj405;
RA Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R.,
RA Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T.,
RA Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H.,
RA Thomson N.R., Wishart D., Wanner B.L.;
RT "Escherichia coli K-12: a cooperatively developed annotation snapshot
RT -- 2005.";
RL Nucleic Acids Res. 34:1-9(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
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 arbutin, cellobiose, and salicin transport.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00426, ECO:0000269|PubMed:15919996}; Multi-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00426,
CC ECO:0000269|PubMed:15919996}.
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; M73326; AAA16429.1; -; Unassigned_DNA.
DR EMBL; U29579; AAA69225.1; -; Genomic_DNA.
DR EMBL; U00096; AAT48150.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76792.1; -; Genomic_DNA.
DR PIR; G65051; G65051.
DR RefSeq; WP_001107828.1; NZ_LN832404.1.
DR RefSeq; YP_026182.1; NC_000913.3.
DR AlphaFoldDB; P24241; -.
DR SMR; P24241; -.
DR BioGRID; 4261308; 9.
DR STRING; 511145.b2715; -.
DR TCDB; 4.A.1.2.3; the pts glucose-glucoside (glc) family.
DR PaxDb; P24241; -.
DR PRIDE; P24241; -.
DR EnsemblBacteria; AAT48150; AAT48150; b2715.
DR EnsemblBacteria; BAE76792; BAE76792; BAE76792.
DR GeneID; 947154; -.
DR KEGG; ecj:JW5435; -.
DR KEGG; eco:b2715; -.
DR PATRIC; fig|1411691.4.peg.4026; -.
DR EchoBASE; EB0084; -.
DR eggNOG; COG1263; Bacteria.
DR eggNOG; COG1264; Bacteria.
DR HOGENOM; CLU_012312_2_0_6; -.
DR OMA; VRNDNQC; -.
DR PhylomeDB; P24241; -.
DR BioCyc; EcoCyc:ASCF-MON; -.
DR BioCyc; MetaCyc:ASCF-MON; -.
DR PRO; PR:P24241; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
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; IBA:GO_Central.
DR GO; GO:0090589; F:protein-phosphocysteine-trehalose phosphotransferase system transporter activity; IBA:GO_Central.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0015771; P:trehalose transport; IBA:GO_Central.
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; 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; TIGR00852; pts-Glc; 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 inner membrane; Cell membrane; Kinase; Membrane;
KW Phosphotransferase system; Reference proteome; Sugar transport;
KW Transferase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..485
FT /note="PTS system arbutin-, cellobiose-, and salicin-
FT specific EIIBC component"
FT /id="PRO_0000186498"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 433..453
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN 1..88
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT DOMAIN 108..470
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT ACT_SITE 28
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT CONFLICT 167..170
FT /note="ASAA -> HLPR (in Ref. 2; AAA69225)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="A -> Q (in Ref. 1; AAA16429)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="R -> H (in Ref. 1; AAA16429)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 485 AA; 51026 MW; E53627EB31B9523C CRC64;
MAKNYAALAR SVIAALGGVD NISAVTHCMT RLRFVIKDDA LIDSPTLKTI PGVLGVVRSD
NQCQVIIGNT VSQAFQEVVS LLPGDMQPAQ PVGKPKLTLR RIGAGILDAL IGTMSPLIPA
IIGGSMVKLL AMILEMSGVL TKGSPTLTIL NVIGDGAFFF LPLMVAASAA IKFKTNMSLA
IAIAGVLVHP SFIELMAKAA QGEHVEFALI PVTAVKYTYT VIPALVMTWC LSYIERWVDS
ITPAVTKNFL KPMLIVLIAA PLAILLIGPI GIWIGSAISA LVYTIHGYLG WLSVAIMGAL
WPLLVMTGMH RVFTPTIIQT IAETGKEGMV MPSEIGANLS LGGSSLAVAW KTKNPELRQT
ALAAAASAIM AGISEPALYG VAIRLKRPLI ASLISGFICG AVAGMAGLAS HSMAAPGLFT
SVQFFDPANP MSIVWVFAVM ALAVVLSFIL TLLLGFEDIP VEEAAAQARK YQSVQPTVAK
EVSLN
