ID Q97J79_CLOAB Unreviewed; 628 AA.
AC Q97J79;
DT 01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 141.
DE SubName: Full=PTS system, beta-glucosides-specific IIABC component {ECO:0000313|EMBL:AAK79375.1};
GN OrderedLocusNames=CA_C1407 {ECO:0000313|EMBL:AAK79375.1};
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562 {ECO:0000313|EMBL:AAK79375.1, ECO:0000313|Proteomes:UP000000814};
RN [1] {ECO:0000313|EMBL:AAK79375.1, ECO:0000313|Proteomes:UP000000814}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787
RC {ECO:0000313|Proteomes:UP000000814};
RX PubMed=11466286; DOI=10.1128/JB.183.16.4823-4838.2001;
RA Nolling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; AE001437; AAK79375.1; -; Genomic_DNA.
DR PIR; D97073; D97073.
DR RefSeq; NP_348035.1; NC_003030.1.
DR RefSeq; WP_010964716.1; NC_003030.1.
DR AlphaFoldDB; Q97J79; -.
DR STRING; 272562.CA_C1407; -.
DR GeneID; 44997913; -.
DR KEGG; cac:CA_C1407; -.
DR PATRIC; fig|272562.8.peg.1613; -.
DR eggNOG; COG1263; Bacteria.
DR eggNOG; COG1264; Bacteria.
DR eggNOG; COG2190; Bacteria.
DR HOGENOM; CLU_012312_2_1_9; -.
DR OrthoDB; 92465at2; -.
DR Proteomes; UP000000814; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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; 2.70.70.10; Glucose Permease (Domain IIA); 1.
DR Gene3D; 3.30.1360.60; Glucose permease domain IIB; 1.
DR InterPro; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR036878; Glu_permease_IIB.
DR InterPro; IPR018113; PTrfase_EIIB_Cys.
DR InterPro; IPR001127; PTS_EIIA_1_perm.
DR InterPro; IPR003352; PTS_EIIC.
DR InterPro; IPR013013; PTS_EIIC_1.
DR InterPro; IPR011297; PTS_IIABC_b_glu.
DR InterPro; IPR001996; PTS_IIB_1.
DR NCBIfam; TIGR00830; PTBA; 1.
DR NCBIfam; TIGR01995; PTS-II-ABC-beta; 1.
DR PANTHER; PTHR30175; PHOSPHOTRANSFERASE SYSTEM TRANSPORT PROTEIN; 1.
DR PANTHER; PTHR30175:SF1; PTS SYSTEM ARBUTIN-, CELLOBIOSE-, AND SALICIN-SPECIFIC EIIBC COMPONENT-RELATED; 1.
DR Pfam; PF00358; PTS_EIIA_1; 1.
DR Pfam; PF00367; PTS_EIIB; 1.
DR Pfam; PF02378; PTS_EIIC; 1.
DR SUPFAM; SSF51261; Duplicated hybrid motif; 1.
DR SUPFAM; SSF55604; Glucose permease domain IIB; 1.
DR PROSITE; PS51093; PTS_EIIA_TYPE_1; 1.
DR PROSITE; PS00371; PTS_EIIA_TYPE_1_HIS; 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 membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphotransferase system {ECO:0000256|ARBA:ARBA00022683};
KW Reference proteome {ECO:0000313|Proteomes:UP000000814};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 172..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 210..234
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 254..276
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 296..322
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 366..384
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 391..408
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 414..430
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 437..460
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 4..86
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000259|PROSITE:PS51098"
FT DOMAIN 102..474
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000259|PROSITE:PS51103"
FT DOMAIN 498..602
FT /note="PTS EIIA type-1"
FT /evidence="ECO:0000259|PROSITE:PS51093"
FT ACT_SITE 26
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00421"
SQ SEQUENCE 628 AA; 67461 MW; 7F715A1D2B9DE19A CRC64;
MKYEKLAKDI IENVGGKENV NSLTHCITRL RFKLKDESKA NTDVLKNMDG VVTVIKSGGQ
YQVVIGNHVP DVYADVVAIG GFSSSSEEGT KEKTNLFNAF IDTISGVFTP TLGVLAATGM
IKGFNAMFIA FGWLTKTSGT YNILNAVGDC LFYFFPIFLG YSAAKKFKGN HFIGMAIGAS
LVYPTLSTLM TGKPLYTLFQ GTIFASPVYV TFLGIPVILM SYSSTVIPII LASYVGVKVE
KAFAKIIPDV VKTFLVPFCT LLVMVPLSLI VIGPISTWAG KLLGAGTLAI YNLSPILAGL
FIGAFWQVFV IFGLHWGLVP IAMNNLSVLH YDPILAGTLG ASFAQTGVVL AILIKTKNVK
LKGIALPAFI SGIFGVTEPA IYGVTLPRKK PFIISCIGAA IGGGITGFMG TKLWMMGGLG
IFAIPSYIGA KGMDRGFYGA VMSVVISFVV GFLIMFFAGF KDEEVKQETT KKKNELVKQE
TLVSPLKGKI KTLSEVKDEA FSTGSLGKGI AIEPEEGKLV SPVDGVLATL FPTGHAVGII
SDKGTEILIH VGMDTVQLEG KYFKTILKQG DHVKAGDTIL EFDIPKIKKA GYTLTTPVVV
TNSESYLDVI ETDKIKVERK DQLLTVML
//
