FMTA_STAAC
ID FMTA_STAAC Reviewed; 397 AA.
AC Q5HH27;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Teichoic acid D-alanine hydrolase;
DE EC=3.1.1.103 {ECO:0000250|UniProtKB:Q7A2T0};
DE AltName: Full=Teichoic acid D-alanine esterase;
DE Flags: Precursor;
GN Name=fmtA; Synonyms=fmt; OrderedLocusNames=SACOL1066;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
RN [2]
RP FUNCTION.
RX PubMed=9371333; DOI=10.1128/aac.41.11.2355;
RA Komatsuzawa H., Sugai M., Ohta K., Fujiwara T., Nakashima S., Suzuki J.,
RA Lee C.Y., Suginaka H.;
RT "Cloning and characterization of the fmt gene which affects the methicillin
RT resistance level and autolysis in the presence of triton X-100 in
RT methicillin-resistant Staphylococcus aureus.";
RL Antimicrob. Agents Chemother. 41:2355-2361(1997).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10471551; DOI=10.1128/aac.43.9.2121;
RA Komatsuzawa H., Ohta K., Labischinski H., Sugai M., Suginaka H.;
RT "Characterization of fmtA, a gene that modulates the expression of
RT methicillin resistance in Staphylococcus aureus.";
RL Antimicrob. Agents Chemother. 43:2121-2125(1999).
CC -!- FUNCTION: Catalyzes the liberation of D-alanyl moieties present on wall
CC teichoic acid (WTA) and lipoteichoic acid (LTA) (By similarity).
CC Affects the methicillin resistance level and autolysis in the presence
CC of Triton X-100 as well as the cell wall structure (PubMed:9371333,
CC PubMed:10471551). {ECO:0000250|UniProtKB:Q7A2T0,
CC ECO:0000269|PubMed:10471551, ECO:0000269|PubMed:9371333}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(4-D-Ala)-(2-GlcNAc)-Rib-ol-P]n-[Gro-P]m-beta-D-ManNAc-
CC (1->4)-alpha-D-GlcNAc-P-peptidoglycan + n H2O = [(2-GlcNAc)-Rib-ol-
CC P]n-[Gro-P]m-beta-D-ManNAc-(1->4)-alpha-D-GlcNAc-P-peptidoglycan + n
CC D-alanine.; EC=3.1.1.103; Evidence={ECO:0000250|UniProtKB:Q7A2T0};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10471551};
CC Peripheral membrane protein {ECO:0000269|PubMed:10471551}.
CC -!- INDUCTION: Transcription is dose dependently increased by the addition
CC of beta-lactam antibiotics, fosfomycin, and bacitracin.
CC -!- MISCELLANEOUS: Inactivation of fmtA results in reduction of the
CC methicillin resistance and in a modification of the cell wall
CC structure.
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DR EMBL; CP000046; AAW36530.1; -; Genomic_DNA.
DR RefSeq; WP_000671243.1; NC_002951.2.
DR AlphaFoldDB; Q5HH27; -.
DR SMR; Q5HH27; -.
DR MEROPS; S12.006; -.
DR EnsemblBacteria; AAW36530; AAW36530; SACOL1066.
DR KEGG; sac:SACOL1066; -.
DR HOGENOM; CLU_020027_0_0_9; -.
DR OMA; WWKGYNT; -.
DR Proteomes; UP000000530; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 3.40.710.10; -; 1.
DR InterPro; IPR001466; Beta-lactam-related.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR Pfam; PF00144; Beta-lactamase; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
PE 2: Evidence at transcript level;
KW Antibiotic resistance; Cell membrane; Cell wall biogenesis/degradation;
KW Hydrolase; Membrane; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..397
FT /note="Teichoic acid D-alanine hydrolase"
FT /id="PRO_0000043099"
SQ SEQUENCE 397 AA; 46067 MW; 414664A674A19394 CRC64;
MKFNKVKLVI HACVLLFIII SIALIFHRLQ TKTHSIDPIH KETKLSDNEK YLVDRNKEKV
APSKLKEVYN SKDPKYKKID KYLQSSLFNG SVAIYENGKL KMSKGYGYQD FEKGIKNTPN
TMFLIGSAQK FSTGLLLKQL EEEHKININD PVSKYLPWFK TSKPIPLKDL MLHQSGLYKY
KSSKDYKNLD QAVKAIQKRG IDPKKYKKHM YNDGNYLVLA KVIEEVTGKS YAENYYTKIG
DPLKLQHTAF YDEQPFKKYL AKGYAYNSTG LSFLRPNILD QYYGAGNLYM TPTDMGKLIT
QIQQYKLFSP KITNPLLHEF GTKKYPDEYR YGFYAKPTLN RLNGGFFGQV FTVYYNDKYV
VVLALNVKGN NEVRIKHIYN DILKQNKPYN TKGVIVQ