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Transcriptional regulator ManR (Mannose operon transcriptional activator) [Includes: Putative phosphotransferase enzyme IIB component (EC 2.7.1.191) (Putative PTS system EIIB component); Putative phosphotransferase enzyme IIA component (Putative PTS system EIIA component)]

 MANR_BACSU              Reviewed;         648 AA.
O31644;
26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
05-MAY-2009, sequence version 2.
05-DEC-2018, entry version 124.
RecName: Full=Transcriptional regulator ManR;
AltName: Full=Mannose operon transcriptional activator;
Includes:
RecName: Full=Putative phosphotransferase enzyme IIB component;
EC=2.7.1.191;
AltName: Full=Putative PTS system EIIB component;
Includes:
RecName: Full=Putative phosphotransferase enzyme IIA component;
AltName: Full=Putative PTS system EIIA component;
Name=manR; OrderedLocusNames=BSU12000;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
PubMed=9384377; DOI=10.1038/36786;
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus
subtilis.";
Nature 390:249-256(1997).
[2]
SEQUENCE REVISION TO 106.
PubMed=19383706; DOI=10.1099/mic.0.027839-0;
Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G.,
Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
"From a consortium sequence to a unified sequence: the Bacillus
subtilis 168 reference genome a decade later.";
Microbiology 155:1758-1775(2009).
[3]
FUNCTION AS A TRANSCRIPTIONAL ACTIVATOR, INDUCTION, AND DISRUPTION
PHENOTYPE.
PubMed=20139185; DOI=10.1128/JB.01673-09;
Sun T., Altenbuchner J.;
"Characterization of a mannose utilization system in Bacillus
subtilis.";
J. Bacteriol. 192:2128-2139(2010).
[4]
FUNCTION, REGULATION, DNA-BINDING, PHOSPHORYLATION AT HIS-334;
HIS-393; CYS-415 AND HIS-570, AND MUTAGENESIS OF HIS-222; HIS-281;
HIS-334; HIS-393; CYS-415 AND HIS-570.
PubMed=23551403; DOI=10.1111/mmi.12209;
Wenzel M., Altenbuchner J.;
"The Bacillus subtilis mannose regulator, ManR, a DNA-binding protein
regulated by HPr and its cognate PTS transporter ManP.";
Mol. Microbiol. 88:562-576(2013).
-!- FUNCTION: Positively regulates the expression of the mannose
operon that consists of three genes, manP, manA, and yjdF, which
are responsible for the transport and utilization of mannose. Also
activates its own expression. {ECO:0000269|PubMed:20139185,
ECO:0000269|PubMed:23551403}.
-!- CATALYTIC ACTIVITY:
Reaction=D-mannose(out) + N(pros)-phospho-L-histidyl-[protein] =
D-mannose 6-phosphate(in) + L-histidyl-[protein];
Xref=Rhea:RHEA:49232, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746,
ChEBI:CHEBI:4208, ChEBI:CHEBI:29979, ChEBI:CHEBI:58735,
ChEBI:CHEBI:64837; EC=2.7.1.191;
-!- ACTIVITY REGULATION: The regulatory activity of ManR is modulated
by phosphorylation and dephosphorylation of the various ManR
domains. It becomes activated via phosphoryl group transfer from
PEP, EI and HPr on the two conserved histidine residues in the PRD
2 domain, whereas phosphorylation of the EIIA-like domain on His-
570 by the PTS EIIB-Man domain of ManP inactivates ManR
(PubMed:23551403). {ECO:0000269|PubMed:23551403}.
-!- INDUCTION: Up-regulated by mannose. Is subject to carbon
catabolite repression (CCR) by glucose.
{ECO:0000269|PubMed:20139185}.
-!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to grow
with mannose as the sole carbon source.
{ECO:0000269|PubMed:20139185}.
-!- SIMILARITY: Belongs to the transcriptional antiterminator BglG
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AL009126; CAB13057.2; -; Genomic_DNA.
RefSeq; NP_389082.2; NC_000964.3.
RefSeq; WP_003245617.1; NZ_JNCM01000035.1.
ProteinModelPortal; O31644; -.
SMR; O31644; -.
STRING; 224308.Bsubs1_010100006636; -.
iPTMnet; O31644; -.
PaxDb; O31644; -.
PRIDE; O31644; -.
EnsemblBacteria; CAB13057; CAB13057; BSU12000.
GeneID; 939394; -.
KEGG; bsu:BSU12000; -.
PATRIC; fig|224308.179.peg.1295; -.
eggNOG; COG1762; LUCA.
eggNOG; COG3711; LUCA.
HOGENOM; HOG000099531; -.
InParanoid; O31644; -.
KO; K02538; -.
OMA; AAEIYEH; -.
PhylomeDB; O31644; -.
BioCyc; BSUB:BSU12000-MONOMER; -.
Proteomes; UP000001570; Chromosome.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
Gene3D; 1.10.10.10; -; 1.
Gene3D; 3.40.930.10; -; 1.
InterPro; IPR013196; HTH_11.
InterPro; IPR007737; Mga_HTH.
InterPro; IPR011608; PRD.
InterPro; IPR036634; PRD_sf.
InterPro; IPR016152; PTrfase/Anion_transptr.
InterPro; IPR002178; PTS_EIIA_type-2_dom.
InterPro; IPR036095; PTS_EIIB-like_sf.
InterPro; IPR013011; PTS_EIIB_2.
InterPro; IPR036388; WH-like_DNA-bd_sf.
Pfam; PF08279; HTH_11; 1.
Pfam; PF05043; Mga; 1.
Pfam; PF00874; PRD; 2.
Pfam; PF00359; PTS_EIIA_2; 1.
SUPFAM; SSF52794; SSF52794; 1.
SUPFAM; SSF55804; SSF55804; 1.
SUPFAM; SSF63520; SSF63520; 2.
PROSITE; PS51372; PRD_2; 2.
PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
PROSITE; PS00372; PTS_EIIA_TYPE_2_HIS; 1.
PROSITE; PS51099; PTS_EIIB_TYPE_2; 1.
1: Evidence at protein level;
Activator; Complete proteome; DNA-binding; Kinase; Phosphoprotein;
Reference proteome; Repeat; Transcription; Transcription regulation;
Transferase.
CHAIN 1 648 Transcriptional regulator ManR.
/FTId=PRO_0000376080.
DOMAIN 187 292 PRD 1. {ECO:0000255|PROSITE-
ProRule:PRU00704}.
DOMAIN 297 404 PRD 2. {ECO:0000255|PROSITE-
ProRule:PRU00704}.
DOMAIN 409 500 PTS EIIB type-2. {ECO:0000255|PROSITE-
ProRule:PRU00422}.
DOMAIN 510 648 PTS EIIA type-2. {ECO:0000255|PROSITE-
ProRule:PRU00417}.
MOD_RES 222 222 Phosphohistidine; by HPr.
{ECO:0000255|PROSITE-ProRule:PRU00704}.
MOD_RES 281 281 Phosphohistidine; by HPr.
{ECO:0000255|PROSITE-ProRule:PRU00704}.
MOD_RES 334 334 Phosphohistidine; by HPr.
{ECO:0000305|PubMed:23551403}.
MOD_RES 393 393 Phosphohistidine; by HPr.
{ECO:0000305|PubMed:23551403}.
MOD_RES 415 415 Phosphocysteine; by EIIA.
{ECO:0000305|PubMed:23551403}.
MOD_RES 570 570 Phosphohistidine; by EIIB.
{ECO:0000305|PubMed:23551403}.
MUTAGEN 222 222 H->A: Reduced DNA binding.
{ECO:0000269|PubMed:23551403}.
MUTAGEN 281 281 H->A: Reduced DNA binding.
{ECO:0000269|PubMed:23551403}.
MUTAGEN 334 334 H->A: Loss of DNA binding.
{ECO:0000269|PubMed:23551403}.
MUTAGEN 393 393 H->A: Loss of DNA binding.
{ECO:0000269|PubMed:23551403}.
MUTAGEN 415 415 C->A: No effect on DNA binding. Results
in a weak constitutive ManR activity.
{ECO:0000269|PubMed:23551403}.
MUTAGEN 570 570 H->A: No reduction in DNA-binding
activity can be observed in the presence
of EIIBA-Man. Leads to a nearly
constitutive ManR activity.
{ECO:0000269|PubMed:23551403}.
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


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