Summary: FemAB family
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FemAB family Provide feedback
The femAB operon codes for two nearly identical approximately 50-kDa proteins involved in the formation of the Staphylococcal pentaglycine interpeptide bridge in peptidoglycan [1]. These proteins are also considered as a factor influencing the level of methicillin resistance [2].
Literature references
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Ehlert K, Schroder W, Labischinski H; , J Bacteriol 1997;179:7573-7576.: Specificities of FemA and FemB for different glycine residues: FemB cannot substitute for FemA in staphylococcal peptidoglycan pentaglycine side chain formation. PUBMED:9393725 EPMC:9393725
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Vannuffel P, Heusterspreute M, Bouyer M, Vandercam B, Philippe M, Gala JL; , Res Microbiol 1999;150:129-141.: Molecular characterization of femA from Staphylococcus hominis and Staphylococcus saprophyticus, and femA-based discrimination of staphylococcal species. PUBMED:10209768 EPMC:10209768
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Berger-Bachi B, Barberis-Maino L, Strassle A, Kayser FH; , Mol Gen Genet 1989;219:263-269.: FemA, a host-mediated factor essential for methicillin resistance in Staphylococcus aureus: molecular cloning and characterization. PUBMED:2559314 EPMC:2559314
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Stranden AM, Ehlert K, Labischinski H, Berger-Bachi B; , J Bacteriol 1997;179:9-16.: Cell wall monoglycine cross-bridges and methicillin hypersusceptibility in a femAB null mutant of methicillin-resistant Staphylococcus aureus. PUBMED:8981974 EPMC:8981974
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Henze U, Sidow T, Wecke J, Labischinski H, Berger-Bachi B; , J Bacteriol 1993;175:1612-1620.: Influence of femB on methicillin resistance and peptidoglycan metabolism in Staphylococcus aureus. PUBMED:8383661 EPMC:8383661
Internal database links
SCOOP: | Acetyltransf_6 FemAB_like |
Similarity to PfamA using HHSearch: | FemAB_like Acetyltransf_6 |
External database links
SCOP: | 1p4n |
This tab holds annotation information from the InterPro database.
InterPro entry IPR003447
The entry represents the FemABX peptidyl transferase family.
FemABX peptidyl transferases catalyse the incorporation of amino acid(s) into the interchain peptide bridge of peptidoglycan using aminoacyl-tRNA as the amino acid donor, a reaction involved in the synthesis of the bacterial cell wall. The femABX enzymes catalyse the addition of amino acids to a peptidoglycan precursor, which in most cases is a lipid-linked sugar pentapeptide or, alternatively, a soluble nucleotide precursor for W. viridescens femX. The resulting branched peptide chain consists of one to five amino acids and is cross-linked to a pentapeptide of a neighbouring disaccharide chain by a transpeptidase in the final step of peptidoglycan synthesis. The interchain peptide and the femABX enzymes for their synthesis are found in several Gram-positive bacteria and in some Gram-negative, mainly pathogenic species. The femABX transferases differ by type, position and number of amino acids that are incoporated into the interchain. Some femABX proteins function as immunity factors that protect producers of interpeptide-specific endopeptidases against their own products. In addition, the interpeptide plays an important role in cell separation and virulence [ PUBMED:11083873 , PUBMED:12604510 , PUBMED:12679335 , PUBMED:14962386 ].
Some proteins known to belong to the femABX peptidyl transferase family:
- Staphylococcal femA and femB, factors essential for expression of methicillin resistance. FemA adds glycines 2 and 3 of the pentaglycine interpeptide, while femB adds glycines 4 and 5.
- Staphylococcal fmhB (for fem homologue) or femX, which incorporates the first glycine of the pentaglycine interchain peptide in peptidoglycan.
- Weissella viridescens femX, which catalyses the transfer of an L-alanine from Ala-tRNA to the epsilon-amino group of L-lysine of UDP-MurNAc pentapeptide [ PUBMED:12679335 , PUBMED:14962386 ].
- Streptococcus pneumoniae fibA/murM and fibB/murN, which synthesize branched structured cell wall muropeptides that are strain-specific.
- Staphylococcus capitis epr (endopeptidase resistance), which renders the cells resistant to glycylglycine endopeptidase by increasing the serine content and decreasing the glycine content of the interpeptide chains.
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
Molecular function | aminoacyltransferase activity (GO:0016755) |
Biological process | cell wall macromolecule biosynthetic process (GO:0044038) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan Acetyltrans (CL0257), which has the following description:
This clan contains families related to N-acetyltransferases. N-acetyltransferases catalyse the transfer of acetyl groups from acetyl-CoA to arylamines.
The clan contains the following 50 members:
Acetyltransf_1 Acetyltransf_10 Acetyltransf_13 Acetyltransf_15 Acetyltransf_16 Acetyltransf_17 Acetyltransf_18 Acetyltransf_19 Acetyltransf_3 Acetyltransf_4 Acetyltransf_5 Acetyltransf_6 Acetyltransf_7 Acetyltransf_8 Acetyltransf_9 Acetyltransf_CG AstA ATE_C ATE_N Autoind_synth CFAP61_N DUF1122 DUF1248 DUF1999 DUF5613 DUF5645 FemAB FemAB_like FR47 Gly_acyl_tr_C GNAT_acetyltr_2 GNAT_acetyltran GNAT_C GNAT_like HAT_KAT11 HlyC Leu_Phe_trans LPG_synthase_C MCD Mig-14 MOZ_SAS NAT NMT NMT_C NodA ODC_AZ PanZ Phage_T7_Gp13 Pho86 T_hemolysinAlignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...
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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
Seed (21) |
Full (3105) |
Representative proteomes | UniProt (18470) |
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RP15 (401) |
RP35 (1443) |
RP55 (3304) |
RP75 (5584) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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Seed (21) |
Full (3105) |
Representative proteomes | UniProt (18470) |
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RP15 (401) |
RP35 (1443) |
RP55 (3304) |
RP75 (5584) |
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Raw Stockholm | |||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
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Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
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Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
Seed source: | Pfam-B_1214 (release 5.2) |
Previous IDs: | none |
Type: | Family |
Sequence Ontology: | SO:0100021 |
Author: |
Bateman A |
Number in seed: | 21 |
Number in full: | 3105 |
Average length of the domain: | 200.3 aa |
Average identity of full alignment: | 16 % |
Average coverage of the sequence by the domain: | 90.27 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 408 | ||||||||||||
Family (HMM) version: | 19 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the FemAB domain has been found. There are 16 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.
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AlphaFold Structure Predictions
The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.