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PTS system mannose-specific EIIBCA component (EIIBCA-Man) (EII-Man) [Includes: Mannose-specific phosphotransferase enzyme IIB component (EC 2.7.1.191) (PTS system mannose-specific EIIB component); Mannose permease IIC component (PTS system mannose-specific EIIC component); Mannose-specific phosphotransferase enzyme IIA component (PTS system mannose-specific EIIA component)]

 PTN3B_BACSU             Reviewed;         650 AA.
O31645;
05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
05-MAY-2009, sequence version 2.
25-OCT-2017, entry version 118.
RecName: Full=PTS system mannose-specific EIIBCA component;
AltName: Full=EIIBCA-Man;
Short=EII-Man;
Includes:
RecName: Full=Mannose-specific phosphotransferase enzyme IIB component;
EC=2.7.1.191;
AltName: Full=PTS system mannose-specific EIIB component;
Includes:
RecName: Full=Mannose permease IIC component;
AltName: Full=PTS system mannose-specific EIIC component;
Includes:
RecName: Full=Mannose-specific phosphotransferase enzyme IIA component;
AltName: Full=PTS system mannose-specific EIIA component;
Name=manP; Synonyms=yjdD; OrderedLocusNames=BSU12010;
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 C-TERMINUS.
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]
GENE NAME.
STRAIN=168;
PubMed=10627040;
Reizer J., Bachem S., Reizer A., Arnaud M., Saier M.H. Jr.,
Stuelke J.;
"Novel phosphotransferase system genes revealed by genome analysis
- the complete complement of PTS proteins encoded within the genome of
Bacillus subtilis.";
Microbiology 145:3419-3429(1999).
[4]
DISRUPTION PHENOTYPE.
STRAIN=168;
PubMed=10960106; DOI=10.1128/JB.182.18.5202-5210.2000;
Turner M.S., Helmann J.D.;
"Mutations in multidrug efflux homologs, sugar isomerases, and
antimicrobial biosynthesis genes differentially elevate activity of
the sigma(X) and sigma(W) factors in Bacillus subtilis.";
J. Bacteriol. 182:5202-5210(2000).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, AND IDENTIFICATION
BY MASS SPECTROMETRY.
STRAIN=168;
PubMed=17218307; DOI=10.1074/mcp.M600464-MCP200;
Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
Mann M.;
"The serine/threonine/tyrosine phosphoproteome of the model bacterium
Bacillus subtilis.";
Mol. Cell. Proteomics 6:697-707(2007).
[6]
INDUCTION, DISRUPTION PHENOTYPE, DOMAIN, AND MUTAGENESIS OF CYS-9.
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).
[7]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-104.
Midwest center for structural genomics (MCSG);
"Crystal structure of the fructose specific IIb subunit of PTS system
from Bacillus subtilis subsp. subtilis str. 168.";
Submitted (SEP-2007) to the PDB data bank.
-!- FUNCTION: The phosphoenolpyruvate-dependent sugar
phosphotransferase system (sugar PTS), a major carbohydrate active
-transport system, catalyzes the phosphorylation of incoming sugar
substrates concomitantly with their translocation across the cell
membrane. This system is involved in mannose transport.
-!- CATALYTIC ACTIVITY: [Protein]-N(pi)-phospho-L-histidine + D-
mannose(Side 1) = [protein]-L-histidine + D-mannose 6-
phosphate(Side 2).
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
ProRule:PRU00427}; Multi-pass membrane protein
{ECO:0000255|PROSITE-ProRule:PRU00427}.
-!- INDUCTION: Up-regulated by mannose. Is under the control of ManR.
Is subject to carbon catabolite repression (CCR) by glucose. Forms
part of an operon with manA and yjdF.
{ECO:0000269|PubMed:20139185}.
-!- DOMAIN: The EIIB domain is phosphorylated by phospho-EIIA on a
cysteinyl or histidyl residue, depending on the transported sugar.
Then, it transfers the phosphoryl group to the sugar substrate
concomitantly with the sugar uptake processed by the EIIC domain.
The EIIB domain is also able to transfer its phosphoryl group to a
specific histidine residue in ManR, which leads to its
inactivation. {ECO:0000255|PROSITE-ProRule:PRU00422,
ECO:0000269|PubMed:20139185}.
-!- DOMAIN: The EIIC domain forms the PTS system translocation channel
and contains the specific substrate-binding site.
{ECO:0000255|PROSITE-ProRule:PRU00427,
ECO:0000269|PubMed:20139185}.
-!- DOMAIN: The EIIA domain is phosphorylated by phospho-HPr on a
histidyl residue. Then, it transfers the phosphoryl group to the
EIIB domain. {ECO:0000255|PROSITE-ProRule:PRU00417,
ECO:0000269|PubMed:20139185}.
-!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to grow
with mannose as the sole carbon source. Deletion of manP results
in constitutive expression from both the manP and manR promoters,
indicating that the phosphotransferase system (PTS) component EII-
Man has a negative effect on regulation of the mannose operon and
manR. {ECO:0000269|PubMed:10960106, ECO:0000269|PubMed:20139185}.
-----------------------------------------------------------------------
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EMBL; AL009126; CAB13058.2; -; Genomic_DNA.
PIR; G69848; G69848.
RefSeq; NP_389083.2; NC_000964.3.
RefSeq; WP_003245781.1; NZ_JNCM01000035.1.
PDB; 2R48; X-ray; 1.80 A; A=2-104.
PDBsum; 2R48; -.
ProteinModelPortal; O31645; -.
SMR; O31645; -.
STRING; 224308.Bsubs1_010100006641; -.
TCDB; 4.A.2.1.6; the pts fructose-mannitol (fru) family.
iPTMnet; O31645; -.
PaxDb; O31645; -.
EnsemblBacteria; CAB13058; CAB13058; BSU12010.
GeneID; 936437; -.
KEGG; bsu:BSU12010; -.
PATRIC; fig|224308.179.peg.1296; -.
eggNOG; ENOG4105DM4; Bacteria.
eggNOG; COG1299; LUCA.
eggNOG; COG1445; LUCA.
eggNOG; COG1762; LUCA.
HOGENOM; HOG000227677; -.
InParanoid; O31645; -.
KO; K02768; -.
KO; K02769; -.
KO; K02770; -.
OMA; QPIMPII; -.
PhylomeDB; O31645; -.
BioCyc; BSUB:BSU12010-MONOMER; -.
EvolutionaryTrace; O31645; -.
Proteomes; UP000001570; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
GO; GO:0022877; F:protein-N(PI)-phosphohistidine-fructose phosphotransferase system transporter activity; IEA:InterPro.
GO; GO:0090563; F:protein-phosphocysteine-sugar phosphotransferase activity; IBA:GO_Central.
GO; GO:0005351; F:sugar:proton symporter activity; IEA:InterPro.
GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IBA:GO_Central.
CDD; cd05569; PTS_IIB_fructose; 1.
Gene3D; 3.40.930.10; -; 1.
InterPro; IPR016152; PTrfase/Anion_transptr.
InterPro; IPR002178; PTS_EIIA_type-2_dom.
InterPro; IPR036095; PTS_EIIB-like_sf.
InterPro; IPR013011; PTS_EIIB_2.
InterPro; IPR003501; PTS_EIIB_2/3.
InterPro; IPR003352; PTS_EIIC.
InterPro; IPR013014; PTS_EIIC_2.
InterPro; IPR004715; PTS_IIA_fruc.
InterPro; IPR003353; PTS_IIB_fruc.
InterPro; IPR006327; PTS_IIC_fruc.
Pfam; PF00359; PTS_EIIA_2; 1.
Pfam; PF02378; PTS_EIIC; 1.
Pfam; PF02302; PTS_IIB; 1.
SUPFAM; SSF52794; SSF52794; 1.
SUPFAM; SSF55804; SSF55804; 1.
TIGRFAMs; TIGR00829; FRU; 1.
TIGRFAMs; TIGR00848; fruA; 1.
TIGRFAMs; TIGR01427; PTS_IIC_fructo; 1.
PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
PROSITE; PS00372; PTS_EIIA_TYPE_2_HIS; 1.
PROSITE; PS51099; PTS_EIIB_TYPE_2; 1.
PROSITE; PS51104; PTS_EIIC_TYPE_2; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Kinase; Membrane;
Phosphoprotein; Phosphotransferase system; Reference proteome;
Sugar transport; Transferase; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 650 PTS system mannose-specific EIIBCA
component.
/FTId=PRO_0000371313.
TRANSMEM 133 153 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00427}.
TRANSMEM 174 194 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00427}.
TRANSMEM 199 219 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00427}.
TRANSMEM 221 241 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00427}.
TRANSMEM 256 276 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00427}.
TRANSMEM 297 317 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00427}.
TRANSMEM 336 356 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00427}.
TRANSMEM 369 389 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00427}.
TRANSMEM 396 416 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00427}.
TRANSMEM 436 456 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00427}.
DOMAIN 1 98 PTS EIIB type-2. {ECO:0000255|PROSITE-
ProRule:PRU00422}.
DOMAIN 123 456 PTS EIIC type-2. {ECO:0000255|PROSITE-
ProRule:PRU00427}.
DOMAIN 504 649 PTS EIIA type-2. {ECO:0000255|PROSITE-
ProRule:PRU00417}.
ACT_SITE 9 9 Phosphocysteine intermediate; for EIIB
activity. {ECO:0000250}.
ACT_SITE 566 566 Tele-phosphohistidine intermediate; for
EIIA activity. {ECO:0000255|PROSITE-
ProRule:PRU00417}.
MOD_RES 365 365 Phosphoserine.
{ECO:0000269|PubMed:17218307}.
MUTAGEN 9 9 C->A: Appears to be unable to inactivate
ManR, since ManR does not show any
decrease in its DNA-binding activity in
the presence of this mutant.
{ECO:0000269|PubMed:20139185}.
STRAND 2 8 {ECO:0000244|PDB:2R48}.
HELIX 14 30 {ECO:0000244|PDB:2R48}.
STRAND 33 40 {ECO:0000244|PDB:2R48}.
STRAND 43 46 {ECO:0000244|PDB:2R48}.
HELIX 50 55 {ECO:0000244|PDB:2R48}.
STRAND 57 65 {ECO:0000244|PDB:2R48}.
HELIX 70 72 {ECO:0000244|PDB:2R48}.
STRAND 75 80 {ECO:0000244|PDB:2R48}.
HELIX 82 87 {ECO:0000244|PDB:2R48}.
HELIX 89 98 {ECO:0000244|PDB:2R48}.
SEQUENCE 650 AA; 69026 MW; BF92BA1E5E7EBE5F CRC64;
MKLLAITSCP NGIAHTYMAA ENLQKAADRL GVSIKVETQG GIGVENKLTE EEIREADAII
IAADRSVNKD RFIGKKLLSV GVQDGIRKPE ELIQKALNGD IPVYRSATKS ESGNHQEKKQ
NPIYRHLMNG VSFMVPFIVV GGLLIAVALT LGGEKTPKGL VIPDDSFWKT IEQIGSASFS
FMIPILAGYI AYSIADKPGL VPGMIGGYIA ATGSFYDSAS GAGFLGGIIA GFLAGYAALW
IKKLKVPKAI QPIMPIIIIP VFASLIVGLA FVFLIGAPVA QIFASLTVWL AGMKGSSSIL
LALILGAMIS FDMGGPVNKV AFLFGSAMIG EGNYEIMGPI AVAICIPPIG LGIATFLGKR
KFEASQREMG KAAFTMGLFG ITEGAIPFAA QDPLRVIPSI MAGSMTGSVI AMIGNVGDRV
AHGGPIVAVL GAVDHVLMFF IAVIAGSLVT ALFVNVLKKD ITASPVLSET APTSAPSEAA
AANEIKQPIQ SQKAEMSEFK KLTDIISPEL IEPNLSGETS DDIIDELIQK LSRRGALLSE
SGFKQAILNR EQQGTTAIGM NIAIPHGKSE AVREPSVAFG IKRSGVDWNS LDGSEAKLIF
MIAVPKESGG NQHLKILQML SRKLMDDNYR ERLLSVQTTE EAYKLLEEIE


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