P27623 (TAGD_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glycerol-3-phosphate cytidylyltransferase
Short name=GCT
Short name=Gro-PCT
EC=2.7.7.39

Alternative name(s):
CDP-glycerol pyrophosphorylase
Teichoic acid biosynthesis protein D

Gene names

Name:	tagD
Ordered Locus Names:	BSU35740

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

Protein attributes

Sequence length	129 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Provides activated glycerol phosphate for teichoic acid synthesis, via incorporation into both the linkage unit and the teichoic acid polymer by TagB and TagF.
Catalytic activity	CTP + sn-glycerol 3-phosphate = diphosphate + CDP-glycerol. Ref.8
Cofactor	Divalent metal cations. Prefers cobalt, magnesium, manganese or iron.
Enzyme regulation	Inhibited by the divalent cations cadmium, mercury, tin, copper and zinc.
Pathway	Cell wall biogenesis; poly(glucopyranosyl N-acetylgalactosamine 1-phosphate) teichoic acid biosynthesis. Cell wall biogenesis; poly(glycerol phosphate) teichoic acid biosynthesis.
Subunit structure	Homodimer. Ref.8
Subcellular location	Cytoplasm.
Induction	Positively regulated by YycF. Mainly expressed during exponential growth and rapidly shut off as cells enter the stationary phase. Ref.6
Miscellaneous	Proceeds via a random order reaction mechanism where there is negative cooperativity in the binding of substrates but not in catalysis.
Sequence similarities	Belongs to the cytidylyltransferase family.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation Teichoic acid biosynthesis
Cellular component	Cytoplasm
Ligand	Cobalt Iron Magnesium Manganese
Molecular function	Nucleotidyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	teichoic acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	glycerol-3-phosphate cytidylyltransferase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 129

129

Glycerol-3-phosphate cytidylyltransferase

PRO_0000208466

Regions

Nucleotide binding

9 – 10

2

CTP

Nucleotide binding

14 – 17

4

CTP

Nucleotide binding

113 – 120

8

CTP

Sites

Binding site

44

1

Substrate

Binding site

46

1

CTP

Binding site

77

1

Substrate

Experimental info

Mutagenesis

11

1

D → A or E: 0.1% of wild-type activity. Ref.4

Mutagenesis

14

1

H → A: Complete loss of activity. Ref.4

Mutagenesis

17

1

H → A: Complete loss of activity. Ref.4

Mutagenesis

38

1

D → A: 8% of wild-type activity, but 7-fold decrease in substrate affinity. Ref.4

Mutagenesis

44

1

K → A: Reduces affinity for glycerol 3-phosphate about 100-fold. Ref.8

Mutagenesis

46

1

K → A: Reduces affinity for glycerol 3-phosphate about 100-fold. Ref.8

Mutagenesis

55

1

R → A: 0.25% of wild-type activity. Ref.4

Mutagenesis

55

1

R → K: 23% of wild-type activity. Ref.4

Mutagenesis

63

1

R → A: 14% of wild-type activity. Ref.4

Mutagenesis

66

1

D → A: Complete loss of activity, and widespread change in 3D-structure. Ref.4

Mutagenesis

66

1

D → E: 16% of wild-type activity. Ref.4

Mutagenesis

74

1

W → A: 50% of wild-type activity, but 9-fold decrease in substrate affinity. Ref.4

Mutagenesis

84

1

H → A: Complete loss of activity. Ref.4

Mutagenesis

94

1

D → A: 18% of wild-type activity, but 100-fold decrease in substrate affinity. Ref.4

Mutagenesis

113

1

R → A: 1.75% of wild-type activity. Ref.4

Mutagenesis

113

1

R → K: Complete loss of activity. Ref.4

Mutagenesis

114

1

T → A: 9% of wild-type activity. Ref.4

Mutagenesis

118

1

S → A: 6% of wild-type activity. Ref.4

Mutagenesis

119

1

T → A: 8% of wild-type activity. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

129

Helix Strand Turn

Details...

Beta strand

3 – 8

6

Helix

15 – 25

11

Beta strand

28 – 36

9

Helix

38 – 44

7

Helix

52 – 59

8

Beta strand

67 – 71

5

Helix

74 – 76

3

Helix

77 – 83

7

Beta strand

87 – 92

6

Helix

93 – 95

3

Turn

96 – 99

4

Helix

100 – 102

3

Turn

103 – 105

3

Beta strand

106 – 111

6

Helix

119 – 124

6

Sequences

	Sequence		Length	Mass (Da)
	P27623 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: B07F532D9AAE0869	FASTA	129	15,272
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genes concerned with synthesis of poly(glycerol phosphate), the essential teichoic acid in Bacillus subtilis strain 168, are organized in two divergent transcription units." Maueel C., Young M., Karamata D. J. Gen. Microbiol. 137:929-941(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"Expression, purification, and characterization of CTP:glycerol-3-phosphate cytidylyltransferase from Bacillus subtilis." Park Y.S., Sweitzer T.D., Dixon J.E., Kent C. J. Biol. Chem. 268:16648-16654(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
[3]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." 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. Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[4]	"Identification of functional conserved residues of CTP:glycerol-3-phosphate cytidylyltransferase. Role of histidines in the conserved HXGH in catalysis." Park Y.S., Gee P., Sanker S., Schurter E.J., Zuiderweg E.R., Kent C. J. Biol. Chem. 272:15161-15166(1997) [PubMed] [Europe PMC] [Abstract] Cited for: 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.
[5]	"Negative cooperativity of substrate binding but not enzyme activity in wild-type and mutant forms of CTP:glycerol-3-phosphate cytidylyltransferase." Sanker S., Campbell H.A., Kent C. J. Biol. Chem. 276:37922-37928(2001) [PubMed] [Europe PMC] [Abstract] Cited for: MECHANISM.
[6]	"Genes controlled by the essential YycG/YycF two-component system of Bacillus subtilis revealed through a novel hybrid regulator approach." Howell A., Dubrac S., Andersen K.K., Noone D., Fert J., Msadek T., Devine K. Mol. Microbiol. 49:1639-1655(2003) [PubMed] [Europe PMC] [Abstract] Cited for: REGULATION BY YYCF/YYCG.
[7]	"A prototypical cytidylyltransferase: CTP:glycerol-3-phosphate cytidylyltransferase from Bacillus subtilis." Weber C.H., Park Y.S., Sanker S., Kent C., Ludwig M.L. Structure 7:1113-1124(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF COMPLEX WITH CTP.
[8]	"Glycerol-3-phosphate cytidylyltransferase. Structural changes induced by binding of CDP-glycerol and the role of lysine residues in catalysis." Pattridge K.A., Weber C.H., Friesen J.A., Sanker S., Kent C., Ludwig M.L. J. Biol. Chem. 278:51863-51871(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH CDP-GLYCEROL, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF LYS-44 AND LYS-46.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M57497 Genomic DNA. Translation: AAA22843.1.
AL009126 Genomic DNA. Translation: CAB15591.1.

PIR

A49757.

RefSeq

NP_391455.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1COZ	X-ray	2.00	A/B	1-129	[»]
1N1D	X-ray	2.00	A/B/C/D	1-129	[»]

ProteinModelPortal

P27623.

SMR

P27623. Positions 1-126.

ModBase

Search...

Protein-protein interaction databases

STRING

224308.BSU35740.

Proteomic databases

PaxDb

P27623.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAB15591; CAB15591; BSU35740.

GeneID

936809.

KEGG

bsu:BSU35740.

PATRIC

18979164. VBIBacSub10457_3744.

Organism-specific databases

GenoList

BSU35740. [Micado]

Phylogenomic databases

eggNOG

COG0615.

HOGENOM

HOG000284153.

KO

K00980.

OMA

HYGHVRL.

ProtClustDB

CLSK887975.

Enzyme and pathway databases

BioCyc

BSUB:BSU35740-MONOMER.
MetaCyc:MONOMER-8809.

UniPathway

UPA00789.
UPA00827.

Family and domain databases

Gene3D

3.40.50.620. 1 hit.

InterPro

IPR004821. Cyt_trans-like.
IPR006409. G3P_cytidylTrfase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]

Pfam

PF01467. CTP_transf_2. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00125. cyt_tran_rel. 1 hit.
TIGR01518. g3p_cytidyltrns. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P27623.

Entry information

Entry name

TAGD_BACSU

Accession

Primary (citable) accession number: P27623

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	May 1, 2013
This is version 125 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program