ID   FMTA_STAAM              Reviewed;         397 AA.
AC   Q7A2T0;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Teichoic acid D-alanine hydrolase;
DE            EC=3.1.1.103 {ECO:0000269|PubMed:26861022};
DE   AltName: Full=Teichoic acid D-alanine esterase;
DE   Flags: Precursor;
GN   Name=fmtA; Synonyms=fmt; OrderedLocusNames=SAV1057;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
RN   [2]
RP   FUNCTION.
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=22564846; DOI=10.1128/aac.00187-12;
RA   Qamar A., Golemi-Kotra D.;
RT   "Dual roles of FmtA in Staphylococcus aureus cell wall biosynthesis and
RT   autolysis.";
RL   Antimicrob. Agents Chemother. 56:3797-3805(2012).
RN   [3]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=26861022; DOI=10.1128/mbio.02070-15;
RA   Rahman M.M., Hunter H.N., Prova S., Verma V., Qamar A., Golemi-Kotra D.;
RT   "The Staphylococcus aureus methicillin resistance factor FmtA is a D-amino
RT   esterase that acts on teichoic acids.";
RL   MBio 7:E02070-E2070(2016).
CC   -!- FUNCTION: Catalyzes the liberation of D-alanyl moieties present on wall
CC       teichoic acid (WTA) and lipoteichoic acid (LTA) (PubMed:26861022).
CC       Affects the methicillin resistance level and autolysis in the presence
CC       of Triton X-100 as well as the cell wall structure (PubMed:22564846).
CC       {ECO:0000269|PubMed:22564846, ECO:0000269|PubMed:26861022}.
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:0000269|PubMed:26861022};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
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DR   EMBL; BA000017; BAB57219.1; -; Genomic_DNA.
DR   RefSeq; WP_000671245.1; NC_002758.2.
DR   AlphaFoldDB; Q7A2T0; -.
DR   SMR; Q7A2T0; -.
DR   MEROPS; S12.006; -.
DR   PaxDb; Q7A2T0; -.
DR   EnsemblBacteria; BAB57219; BAB57219; SAV1057.
DR   KEGG; sav:SAV1057; -.
DR   HOGENOM; CLU_020027_0_0_9; -.
DR   OMA; WWKGYNT; -.
DR   PhylomeDB; Q7A2T0; -.
DR   BioCyc; SAUR158878:SAV_RS05700-MON; -.
DR   Proteomes; UP000002481; 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   1: Evidence at protein 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_0000043100"
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