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UniProtKB/Swiss-Prot entry P27623


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name TAGD_BACSU
Primary accession number P27623
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1992
Sequence was last modified on August 1, 1992 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 86)
Name and origin of the protein
Protein name Glycerol-3-phosphate cytidylyltransferase
Synonyms GCT
Gro-PCT
EC 2.7.7.39
CDP-glycerol pyrophosphorylase
Teichoic acid biosynthesis protein D
Gene name
Name: tagD
OrderedLocusNames: BSU35740
From
Bacillus subtilis [TaxID: 1423] [HAMAP proteome]
Taxonomy Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=1906926 [NCBI, ExPASy, EBI, Israel, Japan]
Maueel C., Young M., Karamata D.;
"Genes concerned with synthesis of poly(glycerol phosphate), the essential teichoic acid in Bacillus subtilis strain 168, are organized in two divergent transcription units.";
J. Gen. Microbiol. 137:929-941(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
PubMed=8393871 [NCBI, ExPASy, EBI, Israel, Japan]
Park Y.S., Sweitzer T.D., Dixon J.E., Kent C.;
"Expression, purification, and characterization of CTP:glycerol-3-phosphate cytidylyltransferase from Bacillus subtilis.";
J. Biol. Chem. 268:16648-16654(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
DOI=10.1038/36786; PubMed=9384377 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[4]
MUTAGENESIS OF ASP-11; HIS-14; HIS-17; ASP-38; ARG-55; ARG-63; ASP-66; TRP-74; HIS-84; ASP-94; ARG-113; THR-114; SER-118 AND THR-119.
DOI=10.1074/jbc.272.24.15161; PubMed=9182537 [NCBI, ExPASy, EBI, Israel, Japan]
Park Y.S., Gee P., Sanker S., Schurter E.J., Zuiderweg E.R., Kent C.;
"Identification of functional conserved residues of CTP:glycerol-3-phosphate cytidylyltransferase. Role of histidines in the conserved HXGH in catalysis.";
J. Biol. Chem. 272:15161-15166(1997).
[5]
MECHANISM.
DOI=10.1074/jbc.M107198200; PubMed=11487587 [NCBI, ExPASy, EBI, Israel, Japan]
Sanker S., Campbell H.A., Kent C.;
"Negative cooperativity of substrate binding but not enzyme activity in wild-type and mutant forms of CTP:glycerol-3-phosphate cytidylyltransferase.";
J. Biol. Chem. 276:37922-37928(2001).
[6]
REGULATION BY YYCF/YYCG.
DOI=10.1046/j.1365-2958.2003.03661.x; PubMed=12950927 [NCBI, ExPASy, EBI, Israel, Japan]
Howell A., Dubrac S., Andersen K.K., Noone D., Fert J., Msadek T., Devine K.;
"Genes controlled by the essential YycG/YycF two-component system of Bacillus subtilis revealed through a novel hybrid regulator approach.";
Mol. Microbiol. 49:1639-1655(2003).
[7]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF COMPLEX WITH CTP.
DOI=10.1016/S0969-2126(99)80178-6; PubMed=10508782 [NCBI, ExPASy, EBI, Israel, Japan]
Weber C.H., Park Y.S., Sanker S., Kent C., Ludwig M.L.;
"A prototypical cytidylyltransferase: CTP:glycerol-3-phosphate cytidylyltransferase from Bacillus subtilis.";
Structure 7:1113-1124(1999).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M57497; AAA22843.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z99122; CAB15591.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A49757; A49757.
RefSeq NP_391455.1; -.
3D structure databases
PDB
1COZ; X-ray; 2.00 A; A/B=1-129.[ExPASy / RCSB / EBI]
1N1D; X-ray; 2.00 A; A/B/C/D=1-129.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1COZ; -.
1N1D; -.
ModBase P27623.
Enzyme and pathway databases
BioCyc BSUB224308:BSU3572-MON; -.
MetaCyc:MON-8809; -.
Organism-specific databases
SubtiList BG10449; tagD. [Micado]
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0050897; Molecular function: cobalt ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0047348; Molecular function: glycerol-3-phosphate cytidylyltransferase activity (inferred from electronic annotation from InterPro).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030145; Molecular function: manganese ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004595; Molecular function: pantetheine-phosphate adenylyltransferase activity (inferred from electronic annotation from InterPro).
GO:0015937; Biological process: coenzyme A biosynthetic process (inferred from electronic annotation from InterPro).
GO:0019350; Biological process: teichoic acid biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR004821; Cyt_trans_rel.
IPR004820; Cytidylyltransf.
IPR006409; G3P_cytidyltrfase.
IPR001980; LPS_biosynth.
IPR014729; Rossmann-like_a/b/a_fold.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
Pfam PF01467; CTP_transf_2; 1.
Pfam graphical view of domain structure.
PRINTS PR01020; LPSBIOSNTHSS.
TIGRFAMs TIGR00125; cyt_tran_rel; 1.
TIGR01518; g3p_cytidyltrns; 1.
BLOCKS P27623.
ProtoNet P27623.
Genome annotation databases
GeneID 936809; -.
GenomeReviews AL009126_GR; BSU35740.
KEGG bsu:BSU35740; -.
NMPDR fig|224308.1.peg.3581; -.
Phylogenomic databases
HOGENOM P27623; -.
Genome annotation databases
CMR P27623; BSU35740.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cell wall biogenesis/degradation; Cobalt; Complete proteome; Cytoplasm; Iron; Magnesium; Manganese; Nucleotidyltransferase; Teichoic acid biosynthesis; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   129  129     Glycerol-3-phosphate cytidylyltransferase. PRO_0000208466
ACT_SITE   14    14         
ACT_SITE   17    17         
MUTAGEN   11    11        D->A,E: 0.1% of wild-type activity. 
MUTAGEN   14    14        H->A: Complete loss of activity. 
MUTAGEN   17    17        H->A: Complete loss of activity. 
MUTAGEN   38    38        D->A: 8% of wild-type activity, but 7-fold decrease in substrate affinity. 
MUTAGEN   55    55        R->A: 0.25% of wild-type activity. 
MUTAGEN   55    55        R->K: 23% of wild-type activity. 
MUTAGEN   63    63        R->A: 14% of wild-type activity. 
MUTAGEN   66    66        D->A: Complete loss of activity, and widespread change in 3D-structure. 
MUTAGEN   66    66        D->E: 16% of wild-type activity. 
MUTAGEN   74    74        W->A: 50% of wild-type activity, but 9-fold decrease in substrate affinity. 
MUTAGEN   84    84        H->A: Complete loss of activity. 
MUTAGEN   94    94        D->A: 18% of wild-type activity, but 100-fold decrease in substrate affinity. 
MUTAGEN   113   113        R->A: 1.75% of wild-type activity. 
MUTAGEN   113   113        R->K: Complete loss of activity. 
MUTAGEN   114   114        T->A: 9% of wild-type activity. 
MUTAGEN   118   118        S->A: 6% of wild-type activity. 
MUTAGEN   119   119        T->A: 8% of wild-type activity. 
STRAND   3     8  6      
HELIX   15    25  11      
STRAND   28    36  9      
HELIX   38    44  7      
HELIX   52    59  8      
STRAND   67    71  5      
HELIX   77    83  7      
STRAND   87    92  6      
HELIX   93    95  3      
TURN   96    99  4      
HELIX   100   102  3      
TURN   103   105  3      
STRAND   106   111  6      
HELIX   119   124  6      
Sequence information
Length: 129 AA [This is the length of the unprocessed precursor] Molecular weight: 15272 Da [This is the MW of the unprocessed precursor] CRC64: B07F532D9AAE0869 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKKVITYGTF DLLHWGHIKL LERAKQLGDY LVVAISTDEF NLQKQKKAYH SYEHRKLILE 

        70         80         90        100        110        120 
TIRYVDEVIP EKNWEQKKQD IIDHNIDVFV MGDDWEGKFD FLKDQCEVVY LPRTEGISTT 


KIKEEIAGL 

P27623 in FASTA format

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