MANR_BACSU
ID MANR_BACSU Reviewed; 648 AA.
AC O31644;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Transcriptional regulator ManR;
DE AltName: Full=Mannose operon transcriptional activator;
DE Includes:
DE RecName: Full=Putative phosphotransferase enzyme IIB component;
DE EC=2.7.1.191;
DE AltName: Full=Putative PTS system EIIB component;
DE Includes:
DE RecName: Full=Putative phosphotransferase enzyme IIA component;
DE AltName: Full=Putative PTS system EIIA component;
GN Name=manR; OrderedLocusNames=BSU12000;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
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 [2]
RP SEQUENCE REVISION TO 106.
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 [3]
RP FUNCTION AS A TRANSCRIPTIONAL ACTIVATOR, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=20139185; DOI=10.1128/jb.01673-09;
RA Sun T., Altenbuchner J.;
RT "Characterization of a mannose utilization system in Bacillus subtilis.";
RL J. Bacteriol. 192:2128-2139(2010).
RN [4]
RP FUNCTION, REGULATION, DNA-BINDING, PHOSPHORYLATION AT HIS-334; HIS-393;
RP CYS-415 AND HIS-570, AND MUTAGENESIS OF HIS-222; HIS-281; HIS-334; HIS-393;
RP CYS-415 AND HIS-570.
RX PubMed=23551403; DOI=10.1111/mmi.12209;
RA Wenzel M., Altenbuchner J.;
RT "The Bacillus subtilis mannose regulator, ManR, a DNA-binding protein
RT regulated by HPr and its cognate PTS transporter ManP.";
RL Mol. Microbiol. 88:562-576(2013).
CC -!- FUNCTION: Positively regulates the expression of the mannose operon
CC that consists of three genes, manP, manA, and yjdF, which are
CC responsible for the transport and utilization of mannose. Also
CC activates its own expression. {ECO:0000269|PubMed:20139185,
CC ECO:0000269|PubMed:23551403}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-mannose(out) + N(pros)-phospho-L-histidyl-[protein] = D-
CC mannose 6-phosphate(in) + L-histidyl-[protein]; Xref=Rhea:RHEA:49232,
CC Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746, ChEBI:CHEBI:4208,
CC ChEBI:CHEBI:29979, ChEBI:CHEBI:58735, ChEBI:CHEBI:64837;
CC EC=2.7.1.191;
CC -!- ACTIVITY REGULATION: The regulatory activity of ManR is modulated by
CC phosphorylation and dephosphorylation of the various ManR domains. It
CC becomes activated via phosphoryl group transfer from PEP, EI and HPr on
CC the two conserved histidine residues in the PRD 2 domain, whereas
CC phosphorylation of the EIIA-like domain on His-570 by the PTS EIIB-Man
CC domain of ManP inactivates ManR (PubMed:23551403).
CC {ECO:0000269|PubMed:23551403}.
CC -!- INDUCTION: Up-regulated by mannose. Is subject to carbon catabolite
CC repression (CCR) by glucose. {ECO:0000269|PubMed:20139185}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to grow with
CC mannose as the sole carbon source. {ECO:0000269|PubMed:20139185}.
CC -!- SIMILARITY: Belongs to the transcriptional antiterminator BglG family.
CC {ECO:0000305}.
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DR EMBL; AL009126; CAB13057.2; -; Genomic_DNA.
DR RefSeq; NP_389082.2; NC_000964.3.
DR RefSeq; WP_003245617.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; O31644; -.
DR SMR; O31644; -.
DR STRING; 224308.BSU12000; -.
DR iPTMnet; O31644; -.
DR jPOST; O31644; -.
DR PaxDb; O31644; -.
DR PRIDE; O31644; -.
DR EnsemblBacteria; CAB13057; CAB13057; BSU_12000.
DR GeneID; 939394; -.
DR KEGG; bsu:BSU12000; -.
DR PATRIC; fig|224308.179.peg.1295; -.
DR eggNOG; COG1762; Bacteria.
DR eggNOG; COG3711; Bacteria.
DR InParanoid; O31644; -.
DR OMA; HIVVSPL; -.
DR PhylomeDB; O31644; -.
DR BioCyc; BSUB:BSU12000-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0003677; F:DNA binding; 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:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00211; PTS_IIA_fru; 1.
DR Gene3D; 1.10.10.10; -; 2.
DR Gene3D; 3.40.930.10; -; 1.
DR InterPro; IPR013196; HTH_11.
DR InterPro; IPR007737; Mga_HTH.
DR InterPro; IPR011608; PRD.
DR InterPro; IPR036634; PRD_sf.
DR InterPro; IPR016152; PTrfase/Anion_transptr.
DR InterPro; IPR002178; PTS_EIIA_type-2_dom.
DR InterPro; IPR036095; PTS_EIIB-like_sf.
DR InterPro; IPR013011; PTS_EIIB_2.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF08279; HTH_11; 1.
DR Pfam; PF05043; Mga; 1.
DR Pfam; PF00874; PRD; 2.
DR Pfam; PF00359; PTS_EIIA_2; 1.
DR SUPFAM; SSF52794; SSF52794; 1.
DR SUPFAM; SSF55804; SSF55804; 1.
DR SUPFAM; SSF63520; SSF63520; 2.
DR PROSITE; PS51372; PRD_2; 2.
DR PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
DR PROSITE; PS00372; PTS_EIIA_TYPE_2_HIS; 1.
DR PROSITE; PS51099; PTS_EIIB_TYPE_2; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Kinase; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Transferase.
FT CHAIN 1..648
FT /note="Transcriptional regulator ManR"
FT /id="PRO_0000376080"
FT DOMAIN 187..292
FT /note="PRD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00704"
FT DOMAIN 297..404
FT /note="PRD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00704"
FT DOMAIN 409..500
FT /note="PTS EIIB type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT DOMAIN 510..648
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT MOD_RES 222
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00704"
FT MOD_RES 281
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00704"
FT MOD_RES 334
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000305|PubMed:23551403"
FT MOD_RES 393
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000305|PubMed:23551403"
FT MOD_RES 415
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000305|PubMed:23551403"
FT MOD_RES 570
FT /note="Phosphohistidine; by EIIB"
FT /evidence="ECO:0000305|PubMed:23551403"
FT MUTAGEN 222
FT /note="H->A: Reduced DNA binding."
FT /evidence="ECO:0000269|PubMed:23551403"
FT MUTAGEN 281
FT /note="H->A: Reduced DNA binding."
FT /evidence="ECO:0000269|PubMed:23551403"
FT MUTAGEN 334
FT /note="H->A: Loss of DNA binding."
FT /evidence="ECO:0000269|PubMed:23551403"
FT MUTAGEN 393
FT /note="H->A: Loss of DNA binding."
FT /evidence="ECO:0000269|PubMed:23551403"
FT MUTAGEN 415
FT /note="C->A: No effect on DNA binding. Results in a weak
FT constitutive ManR activity."
FT /evidence="ECO:0000269|PubMed:23551403"
FT MUTAGEN 570
FT /note="H->A: No reduction in DNA-binding activity can be
FT observed in the presence of EIIBA-Man. Leads to a nearly
FT constitutive ManR activity."
FT /evidence="ECO:0000269|PubMed:23551403"
SQ SEQUENCE 648 AA; 75351 MW; E987358049EBA550 CRC64;
MEYINTRQKE ILYLLLSEPD DYLVVQDFAD RVQCSEKTIR NDLKVIEDYL NEHSHAQLIR
KPGLGVYLHI EEQERTWLSQ QLHTEHFSSR QRSDKERMLH IAYDLLMNPK PVSAKDIAAR
HFVNRSSIKK DLYAVEEWLK RFDLTLVSRQ RLGLKVEGNE RNKRKALARI SDLIHNTAFT
SQFIKSKFLH YEVDFVTKEI KSLQKKHSLY FTDETFESLL LHTLLMVRRI KMKQPISLSP
KEMAAVKKKK EYQWTFACLQ RLEPVFAIRF PEEEAVYLTL HILGGKVRYP LQTEENLENA
VLPKVVGHLI NRVSELKMMD FHKDQDLING LNIHLNTVLQ RLSYDLSVAN PMLNDIKKMY
PYLFHLIIDV LEDINQTFDL HIPEEEAAYL TLHFQAAIER MQGSSETHKK AVIVCHMGIG
MSQLLRTKIE RKYHQIAVMA CIAKADLKDY IKKHEDIDLV ISTIALENIT VPHIVVSPLL
EPGEEKKLSA FIRQLGESHR QKQKTFQMLN NTTPFLVFLQ QEAEHRYKLI EQLATALFEK
GYVDKDYAVH AVMREKMSAT NIGSGIAIPH ANAKFIKQSA IAIATLKEPL EWGNEKVSLV
FMLAVKHEDQ TMTKQLFSEL SYLSEQPAFV QKLTKETNVM TFLSHLDY
