KEGG   ENZYME: 3.1.1.103
Entry
EC 3.1.1.103                Enzyme                                 
Name
teichoic acid D-alanine hydrolase;
fmtA (gene name)
Class
Hydrolases;
Acting on ester bonds;
Carboxylic-ester hydrolases
Sysname
teichoic acid D-alanylhydrolase
Reaction(IUBMB)
[(4-D-Ala)-(2-GlcNAc)-Rib-ol-P]n-[Gro-P]m-beta-D-ManNAc-(1->4)-alpha-D-GlcNAc-P-peptidoglycan + n H2O = [(2-GlcNAc)-Rib-ol-P]n-[Gro-P]m-beta-D-ManNAc-(1->4)-alpha-D-GlcNAc-P-peptidoglycan + n D-alanine [RN:R11965]
Reaction(KEGG)
R11965
Substrate
[(4-D-Ala)-(2-GlcNAc)-Rib-ol-P]n-[Gro-P]m-beta-D-ManNAc-(1->4)-alpha-D-GlcNAc-P-peptidoglycan;
H2O [CPD:C00001]
Product
[(2-GlcNAc)-Rib-ol-P]n-[Gro-P]m-beta-D-ManNAc-(1->4)-alpha-D-GlcNAc-P-peptidoglycan;
D-alanine [CPD:C00133]
Comment
The enzyme, characterized from the bacterium Staphylococcus aureus, removes D-alanine groups from the teichoic acid produced by this organism, thus modulating the electrical charge of the bacterial surface. The activity greatly increases methicillin resistance in MRSA strains.
History
EC 3.1.1.103 created 2018
Orthology
K22580  teichoic acid D-alanine hydrolase
Genes
SDOSD1155_07555
SRDSD10_11505
BCBBCB4264_A3498
BCYBcer98_2742
BTBBMB171_C3163 BMB171_P0160
BTTHD73_3735
BTHRYBT1520_18415
BTHIBTK_18405
BTCCT43_CH4049
BTMMC28_2645
BTGBTB_c41780(pbpX3)
BTHTH175_ch4115
BTHUYBT1518_22395
BTHYAQ980_12640
BWEBcerKBAB4_3210
BWWbwei_1441
BMYOBG05_2505
BTYBtoyo_0712
BBYCY96_19305
BMOBMLA2C4_18155
SAUSA0909(fmtA)
SAVSAV1057(fmt)
SAWSAHV_1049(fmt)
SAHSaurJH1_1139
SAJSaurJH9_1116
SAMMW0940(fmt)
SASSAS0992
SARSAR1030(fmt)
SACSACOL1066
SAXUSA300HOU_1001(fmt1)
SAASAUSA300_0959(fmt)
SAOSAOUHSC_00998
SAENWMN_0926
SADSAAV_1021
SUUM013TW_0988(fmtA)
SUVSAVC_04450
SUESAOV_1003
SUJSAA6159_00913(fmtA)
SUKSAA6008_01012
SUCECTR2_912
SUTSAT0131_01092
SUQHMPREF0772_12177
SUZMS7_1014(fmtA)
SUDST398NM01_1054
SUXSAEMRSA15_08880(fmt)
SUWSATW20_10530(fmt)
SUGSAPIG1054
SUFSARLGA251_09710(fmt)
SAUASAAG_02168
SAUERSAU_000944(fmtA)
SAUNSAKOR_00978
SAUSSA40_0927(fmt)
SAUUSA957_0942(fmt)
SAUGSA268_0945(fmt)
SAUZSAZ172_0997(fmtA)
SAUTSAI1T1_2007480
SAUJSAI2T2_1007500
SAUKSAI3T3_1007490
SAUQSAI4T8_1007480
SAUVSAI7S6_1007490(fmtA)
SAUWSAI5S5_1007450(fmtA)
SAUXSAI6T6_1007460(fmtA)
SAUYSAI8T7_1007490(fmtA)
SAUFX998_1056
SABSAB0923(fmt)
SUYSA2981_1011(fmtA)
SAUBC248_1082(fmt)
SAUMBN843_9630
SAUCCA347_973(fmtA)
SAURSABB_01023(fmtA)
SAUIAZ30_05045
SAUDCH52_00600
SAMSNI36_05060
SUHSAMSHR1132_09050
SERSERP0641
SEPSE_0754
SEPPSEB_00730
SEPSDP17_2087(fmtA)
SHASH1907(fmt)
SHHShL2_01771
SSPSSP1736
SCASCA_0665
SLGSLGD_01819
SLNSLUG_18150(fmt)
SSDSPSINT_0518
SDTSPSE_1942(fmtA)
SDPNCTC12225_02173(fmtA)
SWAA284_08550
SPASSTP1_2114
SXYBE24_02600
SXLSXYLSMQ121_1737
SXOSXYL_01880(fmtA)
SHUSHYC_01895
SCAPAYP1020_0379(pbpX)
SSCHLH95_09295
SSCZRN70_10070
SAGQEP23_08225
SEQOSE1039_08140
SSIFAL483_06610 AL483_06615
SCVA4G25_04610
SLZB5P37_08435
SCOHBZ166_00595
SURYMUA21_03785
SNLBJD96_09640
SKLC7J89_10440
SHOMEGX58_01415
SCARDWB96_09410
SCHRDWB92_01740
SARLSAP2_17690
SPICSAMEA4384060_1899(fmtA_2)
SSHNCTC13712_01002(fmtA_1)
SSIMSAMEA4384339_0968(fmtA_1)
SLLOISP08_08725
SAULI6G39_08025
SSACI6I31_07495
SPSDJMB28_09405
STASHYI43_08930
SEDAMNY58_09315
SCAQQMO72_09345
SROTML435_04800(fmtA)
STAPAOB58_946
SGAIK3U27_02865
SSUCACSSAF_09260
SSCUCEP64_08355
SFFFOB90_10230
SSTESAMEA4384403_1803(fmtA)
MLENH3V22_13610
MVTI6J10_02355
MARYLAU42_03235 LAU42_03240
MPSHQA539_03075
MAEQACMGE4_07365
MCLMCCL_0555 MCCL_0556
MCAKMCCS_07680(pbpX_2)
SAGSAG0658
SANgbs0640
SAKSAK_0786
SGCA964_0654
SAGSSaSA20_0551
SAGLGBS222_0540
SAGMBSA_7450
SAGPV193_03115
SAGCDN94_03115
SAGTGBSCOH1_0580
SAGEEN72_04025
SAGGEN73_03725
SAGNW903_0749
SAGJID870_05980
LJFFI9785_1472(pbpX) FI9785_1730
LJHLJP_1717c
LJNT285_07215 T285_08775
LACLBA1605(pbpX)
LAFSD55_1605(pbpX2)
LGALGAS_1459
LHElhv_1192
LHLLBHH_0974
LHRR0052_05750
LHVlhe_1083
LHDHUO_06210
LCRLCRIS_00552(pbp1)
LKEWANG_0789
LGLAO203_08705
LTAH1A07_08850
LCLLOCK919_2316
LPILBPG_02057
LCXLCA12A_0680
LRHLGG_02141
LRGLRHM_2058
LROLOCK900_2102
LRUHMPREF0538_21124
LRTLRI_1866
LRRN134_10195
LVALV515_05195
LFNLF145_07135
LPORPRK60_03620
LZYLZ3411_1809
LSALCA_0648
LCVFBA2_03350
LHBD1010_12850
LCILCK_00771
EHREHR_00080
EDULIU_05530
ETHCK496_08425
 » show all
Reference
1  [PMID:9371333]
  Authors
Komatsuzawa H, Sugai M, Ohta K, Fujiwara T, Nakashima S, Suzuki J, Lee CY, Suginaka H
  Title
Cloning and characterization of the fmt gene which affects the methicillin resistance level and autolysis in the presence of triton X-100 in methicillin-resistant Staphylococcus aureus.
  Journal
Antimicrob Agents Chemother 41:2355-61 (1997)
DOI:10.1128/AAC.41.11.2355
  Sequence
[sau:SA0909]
Reference
2  [PMID:22564846]
  Authors
Qamar A, Golemi-Kotra D
  Title
Dual roles of FmtA in Staphylococcus aureus cell wall biosynthesis and autolysis.
  Journal
Antimicrob Agents Chemother 56:3797-805 (2012)
DOI:10.1128/AAC.00187-12
Reference
3  [PMID:26861022]
  Authors
Rahman MM, Hunter HN, Prova S, Verma V, Qamar A, Golemi-Kotra D
  Title
The Staphylococcus aureus Methicillin Resistance Factor FmtA Is a d-Amino Esterase That Acts on Teichoic Acids.
  Journal
MBio 7:e02070-15 (2016)
DOI:10.1128/mBio.02070-15
Other DBs
ExplorEnz - The Enzyme Database: 3.1.1.103
IUBMB Enzyme Nomenclature: 3.1.1.103
ExPASy - ENZYME nomenclature database: 3.1.1.103
BRENDA, the Enzyme Database: 3.1.1.103
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