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 01-MAY-2013, entry version 87.
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 MASS
RP 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 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 -!- 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 -!- 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 a sole carbon source.
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; 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; K02793; -.
DR KO; K02794; -.
DR KO; K02795; -.
DR ProtClustDB; CLSK886127; -.
DR BioCyc; BSUB:BSU12010-MONOMER; -.
DR EvolutionaryTrace; O31645; -.
DR GO; GO:0016021; C:integral to 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: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_2.
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; SSF55804; PTrfase/Anion_transptr; 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 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
//
