FMTA_STAAU
ID FMTA_STAAU Reviewed; 397 AA.
AC O50608;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 107.
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;
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=KSA8, and NCTC 10443 / 64/9204;
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 [2]
RP FUNCTION.
RC STRAIN=KSA8;
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; AB009635; BAA24012.1; -; Genomic_DNA.
DR RefSeq; WP_000671245.1; NZ_WYDB01000003.1.
DR PDB; 5ZH8; X-ray; 2.60 A; A/B=1-397.
DR PDBsum; 5ZH8; -.
DR AlphaFoldDB; O50608; -.
DR SMR; O50608; -.
DR MEROPS; S12.006; -.
DR OMA; WWKGYNT; -.
DR BioCyc; MetaCyc:MON-19973; -.
DR BRENDA; 3.1.1.103; 3352.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0001896; P:autolysis; IDA:CACAO.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:1900192; P:positive regulation of single-species biofilm formation; IDA:CACAO.
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 3D-structure; Antibiotic resistance; Cell membrane;
KW Cell wall biogenesis/degradation; 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_0000043098"
FT HELIX 47..55
FT /evidence="ECO:0007829|PDB:5ZH8"
FT HELIX 74..85
FT /evidence="ECO:0007829|PDB:5ZH8"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:5ZH8"
FT STRAND 99..110
FT /evidence="ECO:0007829|PDB:5ZH8"
FT TURN 111..114
FT /evidence="ECO:0007829|PDB:5ZH8"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:5ZH8"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:5ZH8"
FT HELIX 129..142
FT /evidence="ECO:0007829|PDB:5ZH8"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:5ZH8"
FT HELIX 167..171
FT /evidence="ECO:0007829|PDB:5ZH8"
FT HELIX 189..199
FT /evidence="ECO:0007829|PDB:5ZH8"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:5ZH8"
FT HELIX 213..227
FT /evidence="ECO:0007829|PDB:5ZH8"
FT HELIX 231..238
FT /evidence="ECO:0007829|PDB:5ZH8"
FT TURN 239..244
FT /evidence="ECO:0007829|PDB:5ZH8"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:5ZH8"
FT HELIX 254..259
FT /evidence="ECO:0007829|PDB:5ZH8"
FT STRAND 264..273
FT /evidence="ECO:0007829|PDB:5ZH8"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:5ZH8"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:5ZH8"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:5ZH8"
FT HELIX 292..303
FT /evidence="ECO:0007829|PDB:5ZH8"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:5ZH8"
FT HELIX 310..318
FT /evidence="ECO:0007829|PDB:5ZH8"
FT STRAND 320..325
FT /evidence="ECO:0007829|PDB:5ZH8"
FT STRAND 327..330
FT /evidence="ECO:0007829|PDB:5ZH8"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:5ZH8"
FT STRAND 340..346
FT /evidence="ECO:0007829|PDB:5ZH8"
FT STRAND 349..355
FT /evidence="ECO:0007829|PDB:5ZH8"
FT STRAND 357..367
FT /evidence="ECO:0007829|PDB:5ZH8"
FT HELIX 371..379
FT /evidence="ECO:0007829|PDB:5ZH8"
FT TURN 380..382
FT /evidence="ECO:0007829|PDB:5ZH8"
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
