KEGG   ENZYME: 2.3.2.18
Entry
EC 2.3.2.18                 Enzyme                                 
Name
N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase;
femB (gene name);
N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-ditrans,octacis-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase
Class
Transferases;
Acyltransferases;
Aminoacyltransferases
Sysname
MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-tri-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc:glycine glycyltransferase
Reaction(IUBMB)
MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-tri-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc + 2 glycyl-tRNAGly = MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-penta-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc + 2 tRNAGly [RN:R08778]
Reaction(KEGG)
R08778
Substrate
MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-tri-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc;
glycyl-tRNA(Gly) [CPD:C02412]
Product
MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-penta-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc;
tRNA(Gly) [CPD:C01642]
Comment
This Staphylococcus aureus enzyme catalyses the successive transfer of two Gly moieties from charged tRNAs to MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-tri-Gly)-D-Ala-D-Ala-diphosphoundecaprenyl-GlcNAc, attaching them to the three Gly molecules that were previously attached to the N6 of the L-Lys at position 3 of the pentapeptide by EC 2.3.2.16 (lipid II:glycine glycyltransferase) and EC 2.3.2.17 (N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase). This is the last step in the synthesis of the pentaglycine interpeptide bridge that is used in this organism for the crosslinking of different glycan strands to each other.
History
EC 2.3.2.18 created 2010
Pathway
ec00550  Peptidoglycan biosynthesis
ec01100  Metabolic pathways
Orthology
K11695  peptidoglycan pentaglycine glycine transferase (the fourth and fifth glycine)
Genes
SDOSD1155_09030
SAUSA1207(femB)
SAVSAV1375(femB)
SAWSAHV_1363(femB)
SAHSaurJH1_1465
SAJSaurJH9_1436
SAMMW1262(femB)
SASSAS1315
SARSAR1388(femB)
SACSACOL1411
SAXUSA300HOU_1310(femB)
SAASAUSA300_1270(femB)
SAOSAOUHSC_01374
SAENWMN_1287(femB)
SADSAAV_1357
SUUM013TW_1321(femB)
SUVSAVC_06125
SUESAOV_1385
SUJSAA6159_01242(femB)
SUKSAA6008_01340(femB)
SUCECTR2_1232
SUTSAT0131_01447
SUQHMPREF0772_11832(femB)
SUZMS7_1332(femB)
SUDST398NM01_1376
SUXSAEMRSA15_12230(femB)
SUWSATW20_13750(femB)
SUGSAPIG1376
SUFSARLGA251_12840(femB)
SAUASAAG_01985
SAUERSAU_001256(femB)
SAUNSAKOR_01312
SAUSSA40_1252(femB)
SAUUSA957_1267(femB)
SAUGSA268_1272(femB)
SAUZSAZ172_1386(femB)
SAUTSAI1T1_2009900(femB)
SAUJSAI2T2_1009920(femB)
SAUKSAI3T3_1009910(femB)
SAUQSAI4T8_1009900(femB)
SAUVSAI7S6_1009910(femB)
SAUWSAI5S5_1009870(femB)
SAUXSAI6T6_1009880(femB)
SAUYSAI8T7_1009910(femB)
SAUFX998_1383(femB)
SABSAB1230(femB)
SUYSA2981_1329(femB)
SAUBC248_1413(femB)
SAUMBN843_12890
SAUCCA347_1312(femB)
SAURSABB_00137(femB)
SAUIAZ30_06700
SAUDCH52_12190
SAMSNI36_06785
SUHSAMSHR1132_12180
SERSERP0947(femB)
SEPSE_1058
SEPPSEB_01084
SEPSDP17_12(femB)
SHASH1531(femB)
SHHShL2_01410(femB)
SSPSSP1370
SCASCA_1020(femB)
SLGSLGD_01473
SLNSLUG_14710(femB)
SSDSPSINT_1098
SDTSPSE_1402(femB)
SDPNCTC12225_01612(femB)
SWAA284_06760
SPASSTP1_2405(femB)
SXYBE24_04245
SXLSXYLSMQ121_1408
SXOSXYL_01494(femB)
SHUSHYC_07540(femB-2)
SCAPAYP1020_0684(femB)
SSCHLH95_06780
SSCZRN70_07250
SAGQEP23_02885
SEQOSE1039_12210
SSIFAL483_04835
SCVA4G25_02375
SPETCEP67_01505
SLZB5P37_11055
SNLBJD96_07450
SKLC7J89_08930
SFQC7J90_08610
SHOMEGX58_10980
SMUSC7J88_02965
SCARDWB96_07500
SCHRDWB92_07040
SARLSAP2_14550(femB)
SPICSAMEA4384060_1556(femB)
SSHNCTC13712_01368(femB)
SSIMSAMEA4384339_1274(femB)
SDBCNQ82_06935
SLLOISP08_07245
SAULI6G39_06605
SSACI6I31_08960
SRAILN051_06400
SPSDJMB28_07765
SSCUCEP64_06425
SFFFOB90_00660
SSTESAMEA4384403_1394(femB)
MLENH3V22_01680
MVTI6J10_04360
MCLMCCL_1042(femB)
MCAKMCCS_12190(femB)
MBOEHT586_06625
MARYLAU42_05605
MBRUMGG13_06060
SHVAAT16_07825
JEAJEM45_01590
NAMPKPF49_04525
GOTAXE85_06540
GMONCTC11323_00360(femB_2)
GEQCG018_00155
GSAFOC50_02540
CLOHMPREF0868_0450
FROAALO17_03260
AMUOKWG62_11055
TPYCQ11_07650
 » show all
Reference
1  [PMID:9393725]
  Authors
Ehlert K, Schroder W, Labischinski H
  Title
Specificities of FemA and FemB for different glycine residues: FemB cannot substitute for FemA in staphylococcal peptidoglycan pentaglycine side chain formation.
  Journal
J Bacteriol 179:7573-6 (1997)
DOI:10.1128/JB.179.23.7573-7576.1997
  Sequence
Reference
2  [PMID:14523106]
  Authors
Rohrer S, Berger-Bachi B
  Title
Application of a bacterial two-hybrid system for the analysis of protein-protein  interactions between FemABX family proteins.
  Journal
Microbiology 149:2733-8 (2003)
DOI:10.1099/mic.0.26315-0
  Sequence
Reference
3  [PMID:15228543]
  Authors
Schneider T, Senn MM, Berger-Bachi B, Tossi A, Sahl HG, Wiedemann I
  Title
In vitro assembly of a complete, pentaglycine interpeptide bridge containing cell wall precursor (lipid II-Gly5) of Staphylococcus aureus.
  Journal
Mol Microbiol 53:675-85 (2004)
DOI:10.1111/j.1365-2958.2004.04149.x
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 2.3.2.18
IUBMB Enzyme Nomenclature: 2.3.2.18
ExPASy - ENZYME nomenclature database: 2.3.2.18
BRENDA, the Enzyme Database: 2.3.2.18
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