ID   FMTA_STAA8              Reviewed;         397 AA.
AC   Q2FZK3;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Teichoic acid D-alanine hydrolase {ECO:0000305};
DE            EC=3.1.1.103 {ECO:0000250|UniProtKB:Q7A2T0};
DE   AltName: Full=Teichoic acid D-alanine esterase {ECO:0000305};
DE   Flags: Precursor;
GN   Name=fmtA; Synonyms=fmt; OrderedLocusNames=SAOUHSC_00998;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
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.
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:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
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; CP000253; ABD30122.1; -; Genomic_DNA.
DR   RefSeq; WP_000671243.1; NZ_LS483365.1.
DR   RefSeq; YP_499550.1; NC_007795.1.
DR   AlphaFoldDB; Q2FZK3; -.
DR   SMR; Q2FZK3; -.
DR   STRING; 1280.SAXN108_1054; -.
DR   MEROPS; S12.006; -.
DR   EnsemblBacteria; ABD30122; ABD30122; SAOUHSC_00998.
DR   GeneID; 3920398; -.
DR   KEGG; sao:SAOUHSC_00998; -.
DR   PATRIC; fig|93061.5.peg.916; -.
DR   eggNOG; COG1680; Bacteria.
DR   HOGENOM; CLU_020027_0_0_9; -.
DR   OMA; WWKGYNT; -.
DR   PRO; PR:Q2FZK3; -.
DR   Proteomes; UP000008816; 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; Reference proteome; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..397
FT                   /note="Teichoic acid D-alanine hydrolase"
FT                   /id="PRO_0000248948"
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