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| PROSITE documentation PDOC00094 |
Hexapeptide-repeat containing-transferases signature
Description
On the basis of sequence similarity, a number of transferases have been
proposed [1,2,3,4] to belong to a single family. These proteins are:
- Serine O-acetyltransferase (EC 2.3.1.30) (SAT) (gene cysE), an enzyme
involved in cysteine biosynthesis.
- Azotobacter chroococcum nitrogen fixation protein nifP. NifP is most
probably a SAT involved in the optimization of nitrogenase activity.
- Escherichia coli thiogalactoside acetyltransferase (EC 2.3.1.18) (gene
lacA), an enzyme involved in the biosynthesis of lactose.
- UDP-N-acetylglucosamine acyltransferase (EC 2.3.1.129) (gene lpxA), an
enzyme involved in the biosynthesis of lipid A, a phosphorylated glycolipid
that anchors the lipopolysaccharide to the outer membrane of the cell.
- UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase (EC 2.3.1.-)
(gene lpxD or firA), which is also involved in the biosynthesis of lipid A.
- Chloramphenicol O-acetyltransferase (CAT) (EC 2.3.1.28) from Agrobacterium
tumefaciens, Bacillus sphaericus, Escherichia coli plasmid IncFII NR79,
Pseudomonas aeruginosa, Staphylococcus aureus plasmid pIP630. These CAT are
not evolutionary related to the main family of CAT (see <PDOC00093>).
- Rhizobium nodulation protein nodL. NodL is an acetyltransferase involved in
the O-acetylation of Nod factors.
- Bacterial maltose O-acetyltransferase (EC 2.3.1.79).
- Bacterial tetrahydrodipicolinate N-succinyltransferase (EC 2.3.1.117) (gene
dapD) which catalyzes the fourth step in the biosynthesis of
diaminopimelate and lysine from aspartate semialdehyde.
- Bacterial N-acetylglucosamine-1-phosphate uridyltransferase (EC 2.7.7.23)
(gene glmU or gcaD or tms), an enzyme involved in peptidoglycan and
lipopolysaccharide biosynthesis.
- Staphylococcus aureus protein capG which is involved in biosynthesis of
type 1 capsular polysaccharide.
- Yeast hypothetical protein YJL218w, which is highly similar to Escherichia
coli lacA.
- Fission yeast hypothetical protein SpAC18B11.09c.
- Methanococcus jannaschii hypothetical protein MJ1064.
These proteins have been shown [3,4] to contain a repeat structure composed of
tandem repeats of a [LIV]-G-x(4) hexapeptide which, in the tertiary structure
of lpxA [5], has been shown to form a left-handed parallel β helix. Our
signature pattern is based on a fourfold repeat of this hexapeptide.
Roy P.H.
July 1998 / Text revised.
Technical section
PROSITE method (with tools and information) covered by this documentation:
| HEXAPEP_TRANSFERASES, PS00101; Hexapeptide-repeat containing-transferases signature (PATTERN) |
| Consensus pattern: |
[LIV]-[GAED]-x(2)-[STAV]-x-[LIV]-x(3)-[LIVAC]-x-[LIV]-[GAED]-x(2)-[STAVR]-x-[LIV]-[GAED]-x(2)-[STAV]-x-[LIV]-x(3)-[LIV]
|
| Sequences known to belong to this class detected by the pattern: |
ALL |
| Other sequence(s) detected in Swiss-Prot: |
2. |
|
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|
| Matching PDB structures:
1G95 1G97 1HM0 1HM8 ... [ALL] |
References
| 1 |
Authors |
Downie J.A. |
| Title |
The nodL gene from Rhizobium leguminosarum is homologous to the acetyl transferases encoded by lacA and cysE. |
| Source |
Mol. Microbiol. 3:1649-1651(1989). |
| PubMed ID |
2615659 |
| 2 |
Authors |
Parent R., Roy P.H. |
| Title |
The chloramphenicol acetyltransferase gene of Tn2424: a new breed of cat. |
| Source |
J. Bacteriol. 174:2891-2897(1992). |
| PubMed ID |
1314803 |
| 3 |
Authors |
Vaara M. |
| Title |
Eight bacterial proteins, including UDP-N-acetylglucosamine acyltransferase (LpxA) and three other transferases of Escherichia coli, consist of a six-residue periodicity theme. |
| Source |
FEMS Microbiol. Lett. 76:249-254(1992). |
| PubMed ID |
1427014 |
| 4 |
Authors |
Vuorio R., Haerkonen T., Tolvanen M., Vaara M. |
| Title |
The novel hexapeptide motif found in the acyltransferases LpxA and LpxD of lipid A biosynthesis is conserved in various bacteria. |
| Source |
FEBS Lett. 337:289-292(1994). |
| PubMed ID |
8293817 |
| 5 |
Authors |
Raetz C.R.H., Roderick S.L. |
| Title |
A left-handed parallel beta helix in the structure of UDP-N-acetylglucosamine acyltransferase. |
| Source |
Science 270:997-1000(1995). |
| PubMed ID |
7481807 |
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