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
SDO: SD1155_07555
BSR: I33_1881
BSL: A7A1_3392
BSH: BSU6051_16950(pbpX)
BSY: I653_08695
BSUT: BSUB_01826(pbpX)
BSUL: BSUA_01826(pbpX)
BSUS: Q433_09635
BSS: BSUW23_08715(pbpX)
BST: GYO_2049
BSO: BSNT_08209(pbpX)
BSQ: B657_16950(pbpX)
BSX: C663_1738(pbpX)
BLI: BL02713(pbpX)
BLD: BLi00181(pbpX)
BLH: BaLi_c02020(pbpX)
BAQ: BACAU_1650(pbpX)
BYA: BANAU_1650(pbpX)
BAMP: B938_08705
BAML: BAM5036_1616(pbpX)
BAMA: RBAU_1656(pbpX)
BAMN: BASU_1635(pbpX)
BAMB: BAPNAU_2072(pbpX)
BAMT: AJ82_09540
BAMY: V529_16380(ampC)
BMP: NG74_01740(pbpX_2)
BAO: BAMF_1767(pbpX)
BAZ: BAMTA208_08665(pbpX)
BQL: LL3_01854(pbpX)
BXH: BAXH7_01767(pbpX)
BQY: MUS_1851(pbpX)
BAMI: KSO_010955
BAMC: U471_17200
BAMF: U722_08880
BCQ: BCQ_3295(bla) BCQ_3833
BTM: MC28_2645
BTG: BTB_c41780(pbpX3)
BMYC: DJ92_1138
BJS: MY9_1841
BACW: QR42_08215
BACP: SB24_01310
BACB: OY17_11475
BACY: QF06_07515
BACL: BS34A_18620(pbpX)
BALM: BsLM_1791
BGY: BGLY_0167
SAU: SA0909(fmtA)
SAV: SAV1057(fmt)
SAW: SAHV_1049(fmt)
SAM: MW0940(fmt)
SAS: SAS0992
SAR: SAR1030(fmt)
SAC: SACOL1066
SAX: USA300HOU_1001(fmt1)
SAA: SAUSA300_0959(fmt)
SAE: NWMN_0926
SAD: SAAV_1021
SUU: M013TW_0988(fmtA)
SUE: SAOV_1003
SUC: ECTR2_912
SUZ: MS7_1014(fmtA)
SUX: SAEMRSA15_08880(fmt)
SUW: SATW20_10530(fmt)
SUG: SAPIG1054
SUF: SARLGA251_09710(fmt)
SAUA: SAAG_02168
SAUE: RSAU_000944(fmtA)
SAUS: SA40_0927(fmt)
SAUU: SA957_0942(fmt)
SAUG: SA268_0945(fmt)
SAUZ: SAZ172_0997(fmtA)
SAUV: SAI7S6_1007490(fmtA)
SAUW: SAI5S5_1007450(fmtA)
SAUX: SAI6T6_1007460(fmtA)
SAUY: SAI8T7_1007490(fmtA)
SAUF: X998_1056
SAB: SAB0923(fmt)
SUY: SA2981_1011(fmtA)
SAUB: C248_1082(fmt)
SAUM: BN843_9630
SAUC: CA347_973(fmtA)
SAUR: SABB_01023(fmtA)
SAUI: AZ30_05045
SAUD: CH52_00600
SAMS: NI36_05060
SER: SERP0641
SEP: SE0754
SEPP: SEB_00730
SEPS: DP17_2087(fmtA)
SHA: SH1907(fmt)
SSP: SSP1736
SCA: SCA_0665
SLN: SLUG_18150(fmt)
SDT: SPSE_1942(fmtA)
SPAS: STP1_2114
SXO: SXYL_01880(fmtA)
SCAP: AYP1020_0379(pbpX)
SSCH: LH95_09295
SSCZ: RN70_10070
SAGQ: EP23_08225
SDP: NCTC12225_02173(fmtA)
SARL: SAP2_17690
MCAK: MCCS_07670(pbpX_1) MCCS_07680(pbpX_2)
LMOC: LMOSLCC5850_0533(pbpX)
LMOE: BN418_0618
LMOB: BN419_0627
LMOD: LMON_0540
LMOW: AX10_11220
LMOQ: LM6179_0845(pbpX)
LMR: LMR479A_0552(pbpX)
LMOM: IJ09_07650
LMOG: BN389_05770(pbpX)
LMP: MUO_02950
LMOL: LMOL312_0548(pbpX)
LMOX: AX24_15625
LMQ: LMM7_0570(yfeW)
LML: lmo4a_0555(pbpX)
LMS: LMLG_2787
LMW: LMOSLCC2755_0545(pbpX)
LMX: LMOSLCC2372_0549(pbpX)
LMZ: LMOSLCC2482_0542(pbpX)
LMON: LMOSLCC2376_0519(pbpX)
LMOS: LMOSLCC7179_0515(pbpX)
LMOO: LMOSLCC2378_0564(pbpX)
LMOY: LMOSLCC2479_0547(pbpX)
LMOT: LMOSLCC2540_0545(pbpX)
LMOA: LMOATCC19117_0570(pbpX)
LMOK: CQ02_02930
LWE: lwe0501
LGZ: NCTC10812_00946(fmtA_1) NCTC10812_01209(fmtA_2)
SAG: SAG0658
SAN: gbs0640
SAK: SAK_0786
SGC: A964_0654
SAGM: BSA_7450
SAGP: V193_03115
SAGC: DN94_03115
SAGE: EN72_04025
SAGG: EN73_03725
SAGN: W903_0749
LJH: LJP_1717c
LAC: LBA0059(pbpX) LBA0858 LBA1006 LBA1605(pbpX)
LSA: LCA_0648
LGA: LGAS_1459
LKE: WANG_0789 WANG_1631(pbpX)
LRH: LGG_02141
LRG: LRHM_2058
LRA: LRHK_2149
LRE: Lreu_1924
LRF: LAR_1801
LRT: LRI_1866
LBN: LBUCD034_0131(pbpX1)
PPE: PEPE_0564
PPEN: T256_03075
EHR: EHR_00080
EMU: EMQU_0916
EDU: LIU_05530
MPS: MPTP_1050
MPX: MPD5_0898
LCI: LCK_00771
WCE: WS08_0647
WCT: WS74_0649
MPW: MPR_1758
EAO: BD94_0966
 » 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)
  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
LinkDB

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