ID   FMTA_STAAR              Reviewed;         397 AA.
AC   Q6GI27;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=SAR1030;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
CC   -!- FUNCTION: Catalyzes the liberation of D-alanyl moieties present on wall
CC       teichoic acid (WTA) and lipoteichoic acid (LTA). Affects the
CC       methicillin resistance level and autolysis in the presence of Triton X-
CC       100 as well as the cell wall structure. {ECO:0000250|UniProtKB:Q7A2T0}.
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}.
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DR   EMBL; BX571856; CAG40034.1; -; Genomic_DNA.
DR   RefSeq; WP_000671206.1; NC_002952.2.
DR   AlphaFoldDB; Q6GI27; -.
DR   SMR; Q6GI27; -.
DR   MEROPS; S12.006; -.
DR   KEGG; sar:SAR1030; -.
DR   HOGENOM; CLU_020027_0_0_9; -.
DR   OMA; WWKGYNT; -.
DR   OrthoDB; 537440at2; -.
DR   Proteomes; UP000000596; 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   3: Inferred from homology;
KW   Antibiotic resistance; Cell membrane; Cell wall biogenesis/degradation;
KW   Hydrolase; Membrane; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..397
FT                   /note="Teichoic acid D-alanine hydrolase"
FT                   /id="PRO_0000043102"
SQ   SEQUENCE   397 AA;  46035 MW;  265F6F2ABE0980FC CRC64;
     MKFNKEKLVI HACVLLFIII SIGLVFHRLQ TKTNSIEPIH KETKLSDNAK YLVDRNKGKG
     EPSKLKEVYN SKDPKYKKID RYLQNSLFNG SVAVYENGKL KMSKGYGYQD FEKGIKNTPN
     TMFLIGSAQK FSTGLLLKQL EEEHKININD PVSKYIPWFK TSKPIPLKDL MLHQSGLYKY
     KSSKDYKNLD QAVRAIQKRG IDPKKYKKHM YNDGNYLVLA KVIEEVTGKS YAENYYTKIG
     DPLKLQHSAF YDEKSFRKYF AKGYSYNSTG LSFLKPNVLE QYYGAGNIYM TPTDMGKLIT
     QIQQYKLFSP KITNPLLHEF GTKQYPDEYR YGFYVKPTLN RLNGGLFGQV FTVYYNDKYV
     VVLALNVKGN NEVRIKHIYN DILKQNKPYN TKGVIVQ