ID   FMTA_STAAW              Reviewed;         397 AA.
AC   Q7A185;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=MW0940;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
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; BA000033; BAB94805.1; -; Genomic_DNA.
DR   RefSeq; WP_000671245.1; NC_003923.1.
DR   AlphaFoldDB; Q7A185; -.
DR   SMR; Q7A185; -.
DR   MEROPS; S12.006; -.
DR   EnsemblBacteria; BAB94805; BAB94805; BAB94805.
DR   KEGG; sam:MW0940; -.
DR   HOGENOM; CLU_020027_0_0_9; -.
DR   OMA; WWKGYNT; -.
DR   Proteomes; UP000000418; 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..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..397
FT                   /note="Teichoic acid D-alanine hydrolase"
FT                   /id="PRO_0000043104"
SQ   SEQUENCE   397 AA;  46067 MW;  415A8A54684F6194 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 GTKQYPDEYR YGFYAKPTLN RLNGGFFGQV FTVYYNDKYV
     VVLALNVKGN NEVRIKHIYN DILKQNKPYN TKGVIVQ