GLCT_BACSU
ID GLCT_BACSU Reviewed; 281 AA.
AC O31691; O06710;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 3.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=PtsGHI operon antiterminator;
DE AltName: Full=RNA-binding antitermination protein GlcT;
GN Name=glcT; Synonyms=ykwA; OrderedLocusNames=BSU13880;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS AN ANTITERMINATOR, AND
RP REGULATION BY EII-GLC.
RC STRAIN=168;
RX PubMed=11902727; DOI=10.1046/j.1365-2958.1997.4351797.x;
RA Stuelke J., Martin-Verstraete I., Zagorec M., Rose M., Klier A.,
RA Rapoport G.;
RT "Induction of the Bacillus subtilis ptsGHI operon by glucose is controlled
RT by a novel antiterminator, GlcT.";
RL Mol. Microbiol. 25:65-78(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SEQUENCE REVISION TO C-TERMINUS.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP FUNCTION AS AN ANTITERMINATOR, PHOSPHORYLATION AT HIS-104, REGULATION BY
RP HPR AND EII-GLC, AND MUTAGENESIS OF THR-102; ASP-103; HIS-104; ILE-109 AND
RP THR-245.
RX PubMed=9765562; DOI=10.1128/jb.180.20.5319-5326.1998;
RA Bachem S., Stuelke J.;
RT "Regulation of the Bacillus subtilis GlcT antiterminator protein by
RT components of the phosphotransferase system.";
RL J. Bacteriol. 180:5319-5326(1998).
RN [5]
RP INTERACTION WITH THE RNA ANTITERMINATOR (RAT) SEQUENCE, AND MUTAGENESIS OF
RP PHE-5; LYS-9; VAL-10; LEU-11; ASN-12; SER-19; HIS-20; ILE-29; LYS-38;
RP MET-51 AND PHE-52.
RX PubMed=10543968; DOI=10.1006/jmbi.1999.3176;
RA Langbein I., Bachem S., Stuelke J.;
RT "Specific interaction of the RNA-binding domain of the Bacillus subtilis
RT transcriptional antiterminator GlcT with its RNA target, RAT.";
RL J. Mol. Biol. 293:795-805(1999).
RN [6]
RP PHOSPHORYLATION AT HIS-104; HIS-163 AND HIS-211 BY HPR AND EII-GLC, AND
RP MUTAGENESIS OF HIS-104; HIS-163 AND HIS-211.
RX PubMed=14527945; DOI=10.1074/jbc.m309972200;
RA Schmalisch M.H., Bachem S., Stuelke J.;
RT "Control of the Bacillus subtilis antiterminator protein GlcT by
RT phosphorylation. Elucidation of the phosphorylation chain leading to
RT inactivation of GlcT.";
RL J. Biol. Chem. 278:51108-51115(2003).
RN [7]
RP INTERACTION WITH THE RNA ANTITERMINATOR (RAT) SEQUENCE.
RX PubMed=15155854; DOI=10.1093/nar/gkh611;
RA Schilling O., Langbein I., Mueller M., Schmalisch M.H., Stuelke J.;
RT "A protein-dependent riboswitch controlling ptsGHI operon expression in
RT Bacillus subtilis: RNA structure rather than sequence provides interaction
RT specificity.";
RL Nucleic Acids Res. 32:2853-2864(2004).
RN [8]
RP INTERACTION WITH THE RNA ANTITERMINATOR (RAT) SEQUENCE.
RX PubMed=17074746; DOI=10.1093/nar/gkl733;
RA Schilling O., Herzberg C., Hertrich T., Voersmann H., Jessen D.,
RA Huebner S., Titgemeyer F., Stuelke J.;
RT "Keeping signals straight in transcription regulation: specificity
RT determinants for the interaction of a family of conserved bacterial RNA-
RT protein couples.";
RL Nucleic Acids Res. 34:6102-6115(2006).
CC -!- FUNCTION: Mediates the positive regulation of the glucose PTS operon
CC (ptsGHI) by functioning as an antiterminator factor of transcription
CC via its interaction with the RNA-antiterminator (RAT) sequence located
CC upstream of the ptsG gene. The RNA-binding domain of GlcT directly
CC binds to the RNA antiterminator (RAT) sequence and prevents
CC transcriptional termination. GlcT binding requires two identical and
CC nearly symmetrical triple base pairings in the RAT sequence.
CC {ECO:0000269|PubMed:11902727, ECO:0000269|PubMed:9765562}.
CC -!- SUBUNIT: Homodimer (By similarity). The monomeric form probably also
CC exists but it would be inactive in RNA binding and antitermination.
CC {ECO:0000250}.
CC -!- DOMAIN: Composed of 3 domains: an N-terminal RNA-binding domain that
CC prevents transcriptional termination, and two PTS regulation domains,
CC PRD 1 and PRD 2. PRD 1 is the target of negative control exerted by
CC EII-Glc and PRD 2 is the target of HPr.
CC -!- PTM: Phosphorylated by HPr (PtsH) and EII-Glc (PtsG). HPr
CC phosphorylates the PRD 2 domain which has a slight stimulatory effect
CC on GlcT activity, while EII-Glc phosphorylates the PRD 1 domain which
CC inactivates GlcT. The phosphorylation is dependent on the presence or
CC absence of glucose which acts as an inducer of the ptsGHI operon
CC expression. In the presence of glucose the phosphoryl group is
CC transferred from phosphorylated HPr to the sugar via EII-Glc. Under
CC these conditions GlcT is not phosphorylated and binds to the RAT
CC sequence, thus allowing transcription of the ptsGHI operon. In the
CC absence of glucose, phosphorylated EII-Glc accumulates in the cell and
CC phosphorylates the PRD 1 domain of GlcT, leading to its inactivation;
CC this phosphorylation may prevent dimerization of GlcT.
CC {ECO:0000269|PubMed:14527945, ECO:0000269|PubMed:9765562}.
CC -!- SIMILARITY: Belongs to the transcriptional antiterminator BglG family.
CC GlcT subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB13261.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; Y11193; CAA72077.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13261.2; ALT_INIT; Genomic_DNA.
DR PIR; D69632; D69632.
DR RefSeq; NP_389271.2; NC_000964.3.
DR PDB; 3GWH; X-ray; 1.95 A; A/B=171-273.
DR PDB; 3RIO; X-ray; 1.99 A; A=2-170.
DR PDB; 3UFE; X-ray; 1.50 A; A/B=171-273.
DR PDBsum; 3GWH; -.
DR PDBsum; 3RIO; -.
DR PDBsum; 3UFE; -.
DR AlphaFoldDB; O31691; -.
DR BMRB; O31691; -.
DR SMR; O31691; -.
DR STRING; 224308.BSU13880; -.
DR iPTMnet; O31691; -.
DR PaxDb; O31691; -.
DR PRIDE; O31691; -.
DR EnsemblBacteria; CAB13261; CAB13261; BSU_13880.
DR GeneID; 939254; -.
DR KEGG; bsu:BSU13880; -.
DR PATRIC; fig|224308.43.peg.1471; -.
DR eggNOG; COG3711; Bacteria.
DR BioCyc; BSUB:BSU13880-MON; -.
DR EvolutionaryTrace; O31691; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 2.30.24.10; -; 1.
DR InterPro; IPR004341; CAT_RNA-bd_dom.
DR InterPro; IPR036650; CAT_RNA-bd_dom_sf.
DR InterPro; IPR011608; PRD.
DR InterPro; IPR036634; PRD_sf.
DR InterPro; IPR001550; Transcrpt_antitermin_CS.
DR Pfam; PF03123; CAT_RBD; 1.
DR Pfam; PF00874; PRD; 2.
DR SMART; SM01061; CAT_RBD; 1.
DR SUPFAM; SSF50151; SSF50151; 1.
DR SUPFAM; SSF63520; SSF63520; 2.
DR PROSITE; PS00654; PRD_1; 1.
DR PROSITE; PS51372; PRD_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Transcription; Transcription regulation.
FT CHAIN 1..281
FT /note="PtsGHI operon antiterminator"
FT /id="PRO_0000388967"
FT DOMAIN 69..174
FT /note="PRD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00704"
FT DOMAIN 175..278
FT /note="PRD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00704"
FT REGION 1..60
FT /note="RNA binding"
FT MOD_RES 104
FT /note="Phosphohistidine; by EII-Glc"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00704,
FT ECO:0000269|PubMed:9765562, ECO:0000305|PubMed:14527945"
FT MOD_RES 163
FT /note="Phosphohistidine; by EII-Glc"
FT /evidence="ECO:0000305|PubMed:14527945"
FT MOD_RES 211
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000305|PubMed:14527945"
FT MUTAGEN 5
FT /note="F->L: Loss of antiterminator activity; when
FT associated with P-19."
FT /evidence="ECO:0000269|PubMed:10543968"
FT MUTAGEN 5
FT /note="F->S: Loss of antiterminator activity; when
FT associated with T-29."
FT /evidence="ECO:0000269|PubMed:10543968"
FT MUTAGEN 9
FT /note="K->R: Drastically reduced antiterminator activity;
FT when associated with N-38."
FT /evidence="ECO:0000269|PubMed:10543968"
FT MUTAGEN 10
FT /note="V->G: Loss of antiterminator activity."
FT /evidence="ECO:0000269|PubMed:10543968"
FT MUTAGEN 11
FT /note="L->P: Drastically reduced antiterminator activity."
FT /evidence="ECO:0000269|PubMed:10543968"
FT MUTAGEN 12
FT /note="N->D: Loss of antiterminator activity."
FT /evidence="ECO:0000269|PubMed:10543968"
FT MUTAGEN 19
FT /note="S->P: Loss of antiterminator activity; when
FT associated with L-5."
FT /evidence="ECO:0000269|PubMed:10543968"
FT MUTAGEN 20
FT /note="H->R: Drastically reduced antiterminator activity."
FT /evidence="ECO:0000269|PubMed:10543968"
FT MUTAGEN 29
FT /note="I->T: Loss of antiterminator activity; when
FT associated with S-5."
FT /evidence="ECO:0000269|PubMed:10543968"
FT MUTAGEN 38
FT /note="K->N: Drastically reduced antiterminator activity;
FT when associated with R-9."
FT /evidence="ECO:0000269|PubMed:10543968"
FT MUTAGEN 51
FT /note="M->T: Drastically reduced antiterminator activity."
FT /evidence="ECO:0000269|PubMed:10543968"
FT MUTAGEN 52
FT /note="F->V: Loss of antiterminator activity."
FT /evidence="ECO:0000269|PubMed:10543968"
FT MUTAGEN 102
FT /note="T->S: Affects negative regulation of the
FT antiterminator activity; when associated with T-103."
FT /evidence="ECO:0000269|PubMed:9765562"
FT MUTAGEN 103
FT /note="D->T: Affects negative regulation of the
FT antiterminator activity; when associated with S-102."
FT /evidence="ECO:0000269|PubMed:9765562"
FT MUTAGEN 104
FT /note="H->A: Affects negative regulation of the
FT antiterminator activity. No effect on phosphorylation by
FT HPr. Abolishes phosphorylation by both HPr and EII-Glc;
FT when associated with D-211."
FT /evidence="ECO:0000269|PubMed:14527945,
FT ECO:0000269|PubMed:9765562"
FT MUTAGEN 104
FT /note="H->D: Affects negative regulation of the
FT antitermination activity."
FT /evidence="ECO:0000269|PubMed:14527945,
FT ECO:0000269|PubMed:9765562"
FT MUTAGEN 109
FT /note="I->Q: No effect on negative regulation of the
FT antiterminator activity."
FT /evidence="ECO:0000269|PubMed:9765562"
FT MUTAGEN 163
FT /note="H->D: Affects negative regulation of the
FT antiterminator activity. No effect on phosphorylation by
FT HPr. Abolishes phosphorylation by both HPr and EII-Glc;
FT when associated with D-211."
FT /evidence="ECO:0000269|PubMed:14527945"
FT MUTAGEN 211
FT /note="H->D: Strongly reduced phosphorylation by HPr.
FT Abolishes phosphorylation by both HPr and EII-Glc; when
FT associated with A-104 or D-163."
FT /evidence="ECO:0000269|PubMed:14527945"
FT MUTAGEN 245
FT /note="T->P: Loss of ptsG expression."
FT /evidence="ECO:0000269|PubMed:9765562"
FT STRAND 4..12
FT /evidence="ECO:0007829|PDB:3RIO"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:3RIO"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:3RIO"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:3RIO"
FT TURN 31..36
FT /evidence="ECO:0007829|PDB:3RIO"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:3RIO"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:3RIO"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:3RIO"
FT HELIX 57..66
FT /evidence="ECO:0007829|PDB:3RIO"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:3RIO"
FT HELIX 72..89
FT /evidence="ECO:0007829|PDB:3RIO"
FT HELIX 97..113
FT /evidence="ECO:0007829|PDB:3RIO"
FT HELIX 123..129
FT /evidence="ECO:0007829|PDB:3RIO"
FT HELIX 131..148
FT /evidence="ECO:0007829|PDB:3RIO"
FT HELIX 156..169
FT /evidence="ECO:0007829|PDB:3RIO"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:3UFE"
FT HELIX 180..194
FT /evidence="ECO:0007829|PDB:3UFE"
FT HELIX 203..221
FT /evidence="ECO:0007829|PDB:3UFE"
FT HELIX 229..238
FT /evidence="ECO:0007829|PDB:3UFE"
FT HELIX 240..257
FT /evidence="ECO:0007829|PDB:3UFE"
FT HELIX 264..273
FT /evidence="ECO:0007829|PDB:3UFE"
SQ SEQUENCE 281 AA; 32755 MW; ED76E0D547760BDA CRC64;
MNGSFTVKKV LNNNVLIASH HKYSEVVLIG KGIGFGKKQD DVIEDKGYDK MFILKDEKEQ
KQFKKLLDYV DEKLVDISND VIYHISNRTN HSLNEHIHIA LTDHIAFAIK RQQQGFDMKN
PFLMETQSLY PEEYQIAKEV IDMINEKAGL CLPEGEIGFI ALHIHSALTN RPLSEVNQHS
QLMAQLVEVI EDSFQMKVNK ESVNYLRLIR HIRFTIERIK KEEPTKEPEK LMLLLKNEYP
LCYNTAWKLI KILQQTLKKP VHEAEAVYLT LHLYRLTNKI S
