LEVR_BACSU
ID LEVR_BACSU Reviewed; 935 AA.
AC P23914;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Transcriptional regulatory protein LevR;
DE Includes:
DE RecName: Full=Putative phosphotransferase EIIA component;
DE EC=2.7.1.-;
DE AltName: Full=Putative PTS system EIIA component;
GN Name=levR; OrderedLocusNames=BSU27080;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1900939; DOI=10.1073/pnas.88.6.2212;
RA Debarbouille M., Martin-Verstraete I., Klier A., Rapoport G.;
RT "The transcriptional regulator LevR of Bacillus subtilis has domains
RT homologous to both sigma 54- and phosphotransferase system-dependent
RT regulators.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:2212-2216(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9141695; DOI=10.1099/00221287-143-4-1321;
RA Parro V., San Roman M., Galindo I., Purnelle B., Bolotin A., Sorokin A.,
RA Mellado R.P.;
RT "A 23911 bp region of the Bacillus subtilis genome comprising genes located
RT upstream and downstream of the lev operon.";
RL Microbiology 143:1321-1326(1997).
RN [3]
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 [4]
RP SEQUENCE REVISION TO 883.
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).
CC -!- FUNCTION: Involved in positive regulation of the levanase operon which
CC comprises the levDEFG genes for a fructose PTS system, and sacA for
CC levanase.
CC -!- DOMAIN: The PTS EIIA type-4 domain may serve a regulatory function,
CC through its phosphorylation activity. {ECO:0000250}.
CC -!- PTM: Possibly phosphorylated and inactivated by the PTS system.
CC -!- SIMILARITY: Belongs to the transcriptional antiterminator BglG family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA22572.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA63460.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M60105; AAA22572.1; ALT_INIT; Genomic_DNA.
DR EMBL; X92868; CAA63460.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB14650.2; -; Genomic_DNA.
DR PIR; A39160; A39160.
DR RefSeq; NP_390586.2; NC_000964.3.
DR RefSeq; WP_003229830.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P23914; -.
DR SMR; P23914; -.
DR STRING; 224308.BSU27080; -.
DR PaxDb; P23914; -.
DR PRIDE; P23914; -.
DR EnsemblBacteria; CAB14650; CAB14650; BSU_27080.
DR GeneID; 937594; -.
DR KEGG; bsu:BSU27080; -.
DR PATRIC; fig|224308.179.peg.2941; -.
DR eggNOG; COG1221; Bacteria.
DR eggNOG; COG3933; Bacteria.
DR OMA; ELNCADY; -.
DR PhylomeDB; P23914; -.
DR BioCyc; BSUB:BSU27080-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00006; PTS_IIA_man; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.510; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011608; PRD.
DR InterPro; IPR036634; PRD_sf.
DR InterPro; IPR004701; PTS_EIIA_man-typ.
DR InterPro; IPR036662; PTS_EIIA_man-typ_sf.
DR InterPro; IPR033887; PTS_IIA_man.
DR InterPro; IPR002078; Sigma_54_int.
DR InterPro; IPR025943; Sigma_54_int_dom_ATP-bd_2.
DR InterPro; IPR001550; Transcrpt_antitermin_CS.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF03610; EIIA-man; 1.
DR Pfam; PF00874; PRD; 2.
DR Pfam; PF00158; Sigma54_activat; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF53062; SSF53062; 1.
DR SUPFAM; SSF63520; SSF63520; 2.
DR PROSITE; PS00654; PRD_1; 1.
DR PROSITE; PS51372; PRD_2; 2.
DR PROSITE; PS51096; PTS_EIIA_TYPE_4; 1.
DR PROSITE; PS00676; SIGMA54_INTERACT_2; 1.
DR PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE 3: Inferred from homology;
KW Activator; ATP-binding; DNA-binding; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..935
FT /note="Transcriptional regulatory protein LevR"
FT /id="PRO_0000204250"
FT DOMAIN 117..348
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT DOMAIN 468..573
FT /note="PRD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00704"
FT DOMAIN 574..711
FT /note="PTS EIIA type-4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00419"
FT DOMAIN 831..935
FT /note="PRD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00704"
FT BINDING 145..152
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT BINDING 215..224
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT MOD_RES 503
FT /note="Phosphohistidine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00704"
FT MOD_RES 582
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00704"
FT MOD_RES 866
FT /note="Phosphohistidine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00704"
FT CONFLICT 883
FT /note="S -> L (in Ref. 1; AAA22572 and 2; CAA63460)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 935 AA; 105833 MW; 9E8C0BD28B2435C8 CRC64;
MRRIDKIYHQ LKHNFHDSTL DHLLKIQGNS AKEIAEQLKM ERSNVSFELN NLVRSKKVIK
IKTFPVRYIP VEIAEKLFNK KWDTEMMEVK DLQAFSGNSK QNHQHISTNP LELMIGAKGS
LKKAISQAKA AVFYPPNGLH MLLLGPTGSG KSLFANRIYQ FAIYSDILKA GAPFITFNCA
DYYNNPQLLL SQLFGHKKGS FTGAAEDKAG LVEQANGGIL FMDEIHRLPP EGQEMLFYFI
DSGSYNRLGE SEHKRTSNVL FICATTENPS SALLKTFLRR IPMTIHIPSL EERSLNERVD
LTTFLLGKEA ERIKKNLSVH IDVYNALIHS AKFGNVGQLK SNVQLVCAHG FLHNLDRNEV
IELTVRDLPD EIKQEWMSSS KNMQRSKAIS EYVNITTIIS PIVEDETTKI DEDLSFNLYH
LIEEKVKTLM KEGLSKKDIN QYILTDVHLH VRSFFHHQAF QKDNLLTFVE DDVIQMTKQL
KEIAEHELDC TFDRKFIYFL SMHIDAFLKR GKQIDVLNTQ ETDEIRDTHV KEYRVAMIFK
DKIQEYFKVA IPEIEVIYLT MLIHSIKSLK ENKRVGIIVA AHGNSTASSM VEVATELLGS
TPIAAVDMPL TVSPSDILEC VAEKMKQVDE GEGVLMLVDM GSLAMLESRL EEKTGISIKT
ISNVTTSMVL DAVRKVNYLN LNLHAIYQSV TKDFIELWER QPAASGKKKA LVSICTTGSG
TAKKLEDILT TIVNKASDTP IHILTVSSIK LANSIKEIEK EYEILATVGT KDPKINAPHV
SLEVLIEGEG EKLIQQAITK GSISLSNGLN EANIIVRELC EDSLKKYLVF LNPHHVIDML
LEWLQTVQDE LGVIFNNAVL IKVIMHTAFA FERVIKQNPI AFSEEEEIND QLKEMVYVTE
RTLAPYEEKL GLRISDDEKL FIAAIFAEEV HGQLF
