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Entry: O31645
LinkDB: O31645
Original site: O31645 
ID   PTN3B_BACSU             Reviewed;         650 AA.
AC   O31645;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   16-APR-2014, entry version 94.
DE   RecName: Full=PTS system mannose-specific EIIBCA component;
DE   AltName: Full=EIIBCA-Man;
DE            Short=EII-Man;
DE   Includes:
DE     RecName: Full=Mannose-specific phosphotransferase enzyme IIB component;
DE              EC=2.7.1.69;
DE     AltName: Full=PTS system mannose-specific EIIB component;
DE   Includes:
DE     RecName: Full=Mannose permease IIC component;
DE     AltName: Full=PTS system mannose-specific EIIC component;
DE   Includes:
DE     RecName: Full=Mannose-specific phosphotransferase enzyme IIA component;
DE              EC=2.7.1.-;
DE     AltName: Full=PTS system mannose-specific EIIA component;
GN   Name=manP; Synonyms=yjdD; OrderedLocusNames=BSU12010;
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.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   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.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   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 C-TERMINUS.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G.,
RA   Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus
RT   subtilis 168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [3]
RP   GENE NAME.
RC   STRAIN=168;
RX   PubMed=10627040;
RA   Reizer J., Bachem S., Reizer A., Arnaud M., Saier M.H. Jr.,
RA   Stuelke J.;
RT   "Novel phosphotransferase system genes revealed by genome analysis -
RT   the complete complement of PTS proteins encoded within the genome of
RT   Bacillus subtilis.";
RL   Microbiology 145:3419-3429(1999).
RN   [4]
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=168;
RX   PubMed=10960106; DOI=10.1128/JB.182.18.5202-5210.2000;
RA   Turner M.S., Helmann J.D.;
RT   "Mutations in multidrug efflux homologs, sugar isomerases, and
RT   antimicrobial biosynthesis genes differentially elevate activity of
RT   the sigma(X) and sigma(W) factors in Bacillus subtilis.";
RL   J. Bacteriol. 182:5202-5210(2000).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY.
RC   STRAIN=168;
RX   PubMed=17218307; DOI=10.1074/mcp.M600464-MCP200;
RA   Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA   Mann M.;
RT   "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT   Bacillus subtilis.";
RL   Mol. Cell. Proteomics 6:697-707(2007).
RN   [6]
RP   INDUCTION, DISRUPTION PHENOTYPE, DOMAIN, AND MUTAGENESIS OF CYS-9.
RX   PubMed=20139185; DOI=10.1128/JB.01673-09;
RA   Sun T., Altenbuchner J.;
RT   "Characterization of a mannose utilization system in Bacillus
RT   subtilis.";
RL   J. Bacteriol. 192:2128-2139(2010).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-104.
RG   Midwest center for structural genomics (MCSG);
RT   "Crystal structure of the fructose specific IIb subunit of PTS system
RT   from Bacillus subtilis subsp. subtilis str. 168.";
RL   Submitted (SEP-2007) to the PDB data bank.
CC   -!- FUNCTION: The phosphoenolpyruvate-dependent sugar
CC       phosphotransferase system (sugar PTS), a major carbohydrate active
CC       -transport system, catalyzes the phosphorylation of incoming sugar
CC       substrates concomitantly with their translocation across the cell
CC       membrane. This system is involved in mannose transport.
CC   -!- CATALYTIC ACTIVITY: Protein EIIB N(pi)-phospho-L-
CC       histidine/cysteine + sugar = protein EIIB + sugar phosphate.
CC   -!- CATALYTIC ACTIVITY: Protein EIIA N(pi)-phospho-L-histidine +
CC       protein EIIB = protein EIIA + protein EIIB N(pi)-phospho-L-
CC       histidine/cysteine.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- INDUCTION: Up-regulated by mannose. Is under the control of ManR.
CC       Is subject to carbon catabolite repression (CCR) by glucose. Forms
CC       part of an operon with manA and yjdF.
CC   -!- DOMAIN: The EIIB domain is phosphorylated by phospho-EIIA on a
CC       cysteinyl or histidyl residue, depending on the transported sugar.
CC       Then, it transfers the phosphoryl group to the sugar substrate
CC       concomitantly with the sugar uptake processed by the EIIC domain.
CC       The EIIB domain is also able to transfer its phosphoryl group to a
CC       specific histidine residue in ManR, which leads to its
CC       inactivation.
CC   -!- DOMAIN: The EIIC domain forms the PTS system translocation channel
CC       and contains the specific substrate-binding site.
CC   -!- DOMAIN: The EIIA domain is phosphorylated by phospho-HPr on a
CC       histidyl residue. Then, it transfers the phosphoryl group to the
CC       EIIB domain.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to grow
CC       with mannose as the sole carbon source. Deletion of manP results
CC       in constitutive expression from both the manP and manR promoters,
CC       indicating that the phosphotransferase system (PTS) component EII-
CC       Man has a negative effect on regulation of the mannose operon and
CC       manR.
CC   -!- SIMILARITY: Contains 1 PTS EIIA type-2 domain.
CC   -!- SIMILARITY: Contains 1 PTS EIIB type-2 domain.
CC   -!- SIMILARITY: Contains 1 PTS EIIC type-2 domain.
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DR   EMBL; AL009126; CAB13058.2; -; Genomic_DNA.
DR   PIR; G69848; G69848.
DR   RefSeq; NP_389083.2; NC_000964.3.
DR   PDB; 2R48; X-ray; 1.80 A; A=2-104.
DR   PDBsum; 2R48; -.
DR   ProteinModelPortal; O31645; -.
DR   SMR; O31645; 2-104, 502-647.
DR   STRING; 224308.BSU12010; -.
DR   TCDB; 4.A.2.1.6; the pts fructose-mannitol (fru) family.
DR   PhosSite; P0802257; -.
DR   PaxDb; O31645; -.
DR   EnsemblBacteria; CAB13058; CAB13058; BSU12010.
DR   GeneID; 936437; -.
DR   KEGG; bsu:BSU12010; -.
DR   PATRIC; 18974131; VBIBacSub10457_1258.
DR   GenoList; BSU12010; -.
DR   eggNOG; COG1445; -.
DR   HOGENOM; HOG000227677; -.
DR   KO; K02768; -.
DR   KO; K02769; -.
DR   KO; K02770; -.
DR   OrthoDB; EOG6XDGX2; -.
DR   ProtClustDB; CLSK886127; -.
DR   BioCyc; BSUB:BSU12010-MONOMER; -.
DR   EvolutionaryTrace; O31645; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005351; F:sugar:hydrogen symporter activity; IEA:InterPro.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.930.10; -; 1.
DR   InterPro; IPR016152; PTrfase/Anion_transptr.
DR   InterPro; IPR002178; PTS_EIIA_type-2_dom.
DR   InterPro; IPR013011; PTS_EIIB_2.
DR   InterPro; IPR003501; PTS_EIIB_2/3.
DR   InterPro; IPR003352; PTS_EIIC.
DR   InterPro; IPR013014; PTS_EIIC_2.
DR   InterPro; IPR004715; PTS_IIA_fruc.
DR   InterPro; IPR003353; PTS_IIB_fruc.
DR   InterPro; IPR006327; PTS_IIC_fruc.
DR   Pfam; PF00359; PTS_EIIA_2; 1.
DR   Pfam; PF02378; PTS_EIIC; 1.
DR   Pfam; PF02302; PTS_IIB; 1.
DR   SUPFAM; SSF52794; SSF52794; 1.
DR   SUPFAM; SSF55804; SSF55804; 1.
DR   TIGRFAMs; TIGR00829; FRU; 1.
DR   TIGRFAMs; TIGR00848; fruA; 1.
DR   TIGRFAMs; TIGR01427; PTS_IIC_fructo; 1.
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.
DR   PROSITE; PS51104; PTS_EIIC_TYPE_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Complete proteome; Kinase; Membrane;
KW   Phosphoprotein; Phosphotransferase system; Reference proteome;
KW   Sugar transport; Transferase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN         1    650       PTS system mannose-specific EIIBCA
FT                                component.
FT                                /FTId=PRO_0000371313.
FT   TRANSMEM    133    153       Helical; (Potential).
FT   TRANSMEM    174    194       Helical; (Potential).
FT   TRANSMEM    199    219       Helical; (Potential).
FT   TRANSMEM    221    241       Helical; (Potential).
FT   TRANSMEM    256    276       Helical; (Potential).
FT   TRANSMEM    297    317       Helical; (Potential).
FT   TRANSMEM    336    356       Helical; (Potential).
FT   TRANSMEM    369    389       Helical; (Potential).
FT   TRANSMEM    396    416       Helical; (Potential).
FT   TRANSMEM    436    456       Helical; (Potential).
FT   DOMAIN        1     98       PTS EIIB type-2.
FT   DOMAIN      123    456       PTS EIIC type-2.
FT   DOMAIN      504    649       PTS EIIA type-2.
FT   ACT_SITE      9      9       Phosphocysteine intermediate; for EIIB
FT                                activity (By similarity).
FT   ACT_SITE    566    566       Tele-phosphohistidine intermediate; for
FT                                EIIA activity (By similarity).
FT   MOD_RES     365    365       Phosphoserine.
FT   MUTAGEN       9      9       C->A: Appears to be unable to inactivate
FT                                ManR, since ManR does not show any
FT                                decrease in its DNA-binding activity in
FT                                the presence of this mutant.
FT   STRAND        2      8
FT   HELIX        14     30
FT   STRAND       33     40
FT   STRAND       43     46
FT   HELIX        50     55
FT   STRAND       57     65
FT   HELIX        70     72
FT   STRAND       75     80
FT   HELIX        82     87
FT   HELIX        89     98
SQ   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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