KEGG   ENZYME: 2.3.2.17
Entry
EC 2.3.2.17                 Enzyme                                 
Name
N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase;
femA (gene name);
N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-glycyl)-D-alanyl-D-alanine-ditrans,octacis-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase
Class
Transferases;
Acyltransferases;
Aminoacyltransferases
Sysname
MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc:glycine glycyltransferase
Reaction(IUBMB)
MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc + 2 glycyl-tRNAGly = MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-tri-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc + 2 tRNAGly [RN:R08777]
Reaction(KEGG)
R08777
Substrate
MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc;
glycyl-tRNA(Gly) [CPD:C02412]
Product
MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-tri-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc;
tRNA(Gly) [CPD:C01642]
Comment
This enzyme catalyses the successive transfer of two Gly moieties from charged tRNAs to MurNAc-L-Ala-D-isoglutaminyl-L-Lys-(N6-Gly)-D-Ala-D-Ala-diphospho-ditrans,octacis-undecaprenyl-GlcNAc, attaching them to a Gly residue previously attached by EC 2.3.2.16 (lipid II:glycine glycyltransferase) to the N6 of the L-Lys at position 3 of the pentapeptide. This is the second step in the synthesis of the pentaglycine interpeptide bridge that is used by Staphylococcus aureus for the crosslinking of different glycan strands to each other. The next step is catalysed by EC 2.3.2.18 (N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine glycyltransferase). This enzyme is essential for methicillin resistance [1].
History
EC 2.3.2.17 created 2010
Pathway
ec00550  Peptidoglycan biosynthesis
ec01100  Metabolic pathways
Orthology
K11694  peptidoglycan pentaglycine glycine transferase (the second and third glycine)
Genes
SDOSD1155_09025
SAUSA1206(femA)
SAVSAV1374(femA)
SAWSAHV_1362(femA)
SAHSaurJH1_1464
SAJSaurJH9_1435
SAMMW1261(femA)
SASSAS1314
SARSAR1387(femA)
SACSACOL1410(femA)
SAXUSA300HOU_1309(femA)
SAASAUSA300_1269(femA)
SAOSAOUHSC_01373
SAENWMN_1286(femA)
SADSAAV_1356(femA)
SUUM013TW_1320(femA)
SUVSAVC_06120
SUESAOV_1384
SUJSAA6159_01241(femA)
SUKSAA6008_01339(femA)
SUCECTR2_1231
SUTSAT0131_01446
SUQHMPREF0772_11833
SUZMS7_1331
SUDST398NM01_1375
SUXSAEMRSA15_12220(femA)
SUWSATW20_13740(femA)
SUGSAPIG1375
SUFSARLGA251_12830(femA)
SAUASAAG_01984
SAUERSAU_001255(femA)
SAUNSAKOR_01311
SAUSSA40_1251(femA)
SAUUSA957_1266(femA)
SAUGSA268_1271(femA)
SAUZSAZ172_1385(femA)
SAUTSAI1T1_2009890
SAUJSAI2T2_1009910
SAUKSAI3T3_1009900
SAUQSAI4T8_1009890
SAUVSAI7S6_1009900
SAUWSAI5S5_1009860
SAUXSAI6T6_1009870
SAUYSAI8T7_1009900
SAUFX998_1382(femA)
SABSAB1229(femA)
SUYSA2981_1328(femA)
SAUBC248_1412(femA)
SAUMBN843_12880
SAUCCA347_1311(femA)
SAURSABB_00138(femA)
SAUIAZ30_06695
SAUDCH52_12195
SAMSNI36_06780
SUHSAMSHR1132_12170
SERSERP0946(femA)
SEPSE_1057
SEPPSEB_01083
SEPSDP17_11(femA)
SHASH1532(femA)
SHHShL2_01411(femA)
SSPSSP1371
SCASCA_1019(femA)
SLGSLGD_01472
SLNSLUG_14700(femA)
SSDSPSINT_1097
SDTSPSE_1403(femA)
SDPNCTC12225_01613(femA)
SWAA284_06765
SPASSTP1_2404(femA2)
SXYBE24_04240
SXLSXYLSMQ121_1409
SXOSXYL_01495(femA)
SHUSHYC_07545(femA)
SCAPAYP1020_0683(femA_1)
SSCHLH95_06785
SSCZRN70_07255
SAGQEP23_02880
SEQOSE1039_12200
SSIFAL483_04840
SCVA4G25_02380
SPETCEP67_01500
SLZB5P37_11050
SCOHBZ166_11435
SNLBJD96_07455
SKLC7J89_08935
SFQC7J90_08605
SHOMEGX58_10985
SMUSC7J88_02970
SCARDWB96_07505
SCHRDWB92_07045
SARLSAP2_14560(femA)
SPICSAMEA4384060_1557(femA_2)
SSHNCTC13712_01367(femA_2)
SSIMSAMEA4384339_1273(femA_1)
SDBCNQ82_06930
SLLOISP08_07250
SAULI6G39_06610
SSACI6I31_08955
SSCUCEP64_06430
SFFFOB90_00655
SSTESAMEA4384403_1395(femA_2)
MLENH3V22_01675
MVTI6J10_04355
MCLMCCL_1041(femA)
MCAKMCCS_12180(femA_2)
MACRBHM04_03940
MBOEHT586_06620
MARYLAU42_05600
MBRUMGG13_06055
SHVAAT16_07830
SBACBVH56_04465
JEAJEM45_01585
NAMPKPF49_04530
STKSTP_0736
SIKK710_1043
SIQDQ08_04760
SIODW64_04755
SIZSI82_04955
AURHMPREF9243_1998
AUNAWM73_08575
CLOHMPREF0868_0449
FSAC5Q98_04585 C5Q98_04590
FROAALO17_08210
CIUG4D55_16055
BULLJOS54_00595
ERBA4V01_18990
MEDWNCTC10132_00151(pta)
TPYOX956_00015
TBWNCTC13354_00397(femA_1) NCTC13354_00788(femA_2)
ASGFB03_01025 FB03_03630
ACTTDDD63_00835 DDD63_07185
FSLEJO69_08725
FLHEJ997_09975
 » show all
Reference
1  [PMID:2559314]
  Authors
Berger-Bachi B, Barberis-Maino L, Strassle A, Kayser FH
  Title
FemA, a host-mediated factor essential for methicillin resistance in Staphylococcus aureus: molecular cloning and characterization.
  Journal
Mol Gen Genet 219:263-9 (1989)
DOI:10.1007/BF00261186
  Sequence
[sau:SA1206]
Reference
2  [PMID:7590176]
  Authors
Johnson S, Kruger D, Labischinski H
  Title
FemA of Staphylococcus aureus: isolation and immunodetection.
  Journal
FEMS Microbiol Lett 132:221-8 (1995)
DOI:10.1111/j.1574-6968.1995.tb07837.x
  Sequence
Reference
3  [PMID:12176388]
  Authors
Benson TE, Prince DB, Mutchler VT, Curry KA, Ho AM, Sarver RW, Hagadorn JC, Choi GH, Garlick RL
  Title
X-ray crystal structure of Staphylococcus aureus FemA.
  Journal
Structure 10:1107-15 (2002)
DOI:10.1016/S0969-2126(02)00807-9
  Sequence
Reference
4  [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: 2.3.2.17
IUBMB Enzyme Nomenclature: 2.3.2.17
ExPASy - ENZYME nomenclature database: 2.3.2.17
BRENDA, the Enzyme Database: 2.3.2.17

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