LDT1_MYCTO
ID LDT1_MYCTO Reviewed; 251 AA.
AC Q7DAG3;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2014, sequence version 2.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=L,D-transpeptidase 1;
DE Short=LDT 1;
DE EC=2.3.2.-;
DE AltName: Full=Ldt(Mt1);
DE Flags: Precursor;
GN Name=ldtA; OrderedLocusNames=MT0125;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
RN [2]
RP DISRUPTION PHENOTYPE.
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=24464457; DOI=10.1128/jb.01396-13;
RA Schoonmaker M.K., Bishai W.R., Lamichhane G.;
RT "Nonclassical transpeptidases of Mycobacterium tuberculosis alter cell
RT size, morphology, the cytosolic matrix, protein localization, virulence,
RT and resistance to beta-lactams.";
RL J. Bacteriol. 196:1394-1402(2014).
CC -!- FUNCTION: Generates 3->3 cross-links in peptidoglycan, catalyzing the
CC cleavage of the mDap(3)-D-Ala(4) bond of a tetrapeptide donor stem and
CC the formation of a bond between the carbonyl of mDap(3) of the donor
CC stem and the side chain of mDap(3) of the acceptor stem. Is specific
CC for donor substrates containing a stem tetrapeptide since it cannot use
CC pentapeptide stems (By similarity). {ECO:0000250}.
CC -!- ACTIVITY REGULATION: Is irreversibly inactivated by the beta-lactams
CC carbapenems via the formation of a covalent adduct resulting from
CC acylation of the catalytic Cys. {ECO:0000250}.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Lack of this gene alone does not alter in vitro
CC and in vivo growth rate or colony and cell shape and morphology. But
CC loss of both LdtMt1 and LdtMt2 severely alters cellular shape,
CC intracellular morphology, physiology and virulence: the length of
CC mutant cells are shorter than wild-type, they have deep surface
CC depressions and bulges, they possess large unstained vacuole-like
CC structures, the thickness of the peptidoglycan layer is smaller, the
CC protein localization is altered, and in vitro and in vivo growth and
CC virulence are severely attenuated. Moreover, double-mutant cells are
CC more sensitive to vancomycin and amoxicillin-clavulanate.
CC {ECO:0000269|PubMed:24464457}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK44348.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE000516; AAK44348.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_003400856.1; NZ_KK341227.1.
DR AlphaFoldDB; Q7DAG3; -.
DR SMR; Q7DAG3; -.
DR EnsemblBacteria; AAK44348; AAK44348; MT0125.
DR KEGG; mtc:MT0125; -.
DR PATRIC; fig|83331.31.peg.132; -.
DR HOGENOM; CLU_039404_0_2_11; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR CDD; cd16913; YkuD_like; 1.
DR Gene3D; 2.40.440.10; -; 1.
DR InterPro; IPR041280; Big_10.
DR InterPro; IPR005490; LD_TPept_cat_dom.
DR InterPro; IPR038063; Transpep_catalytic_dom.
DR Pfam; PF17964; Big_10; 1.
DR Pfam; PF03734; YkuD; 1.
DR SUPFAM; SSF141523; SSF141523; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Cell shape; Cell wall biogenesis/degradation;
KW Peptidoglycan synthesis; Periplasm; Signal; Transferase.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..251
FT /note="L,D-transpeptidase 1"
FT /id="PRO_0000430331"
FT DOMAIN 129..249
FT /note="YkuD"
FT ACT_SITE 208
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 226
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 190
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 203..204
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 226
FT /note="Binds to carbapenem drug (covalent)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 251 AA; 26916 MW; E074256B6445EABC CRC64;
MRRVVRYLSV VVAITLMLTA ESVSIATAAV PPLQPIPGVA SVSPANGAVV GVAHPVVVTF
TTPVTDRRAV ERSIRISTPH NTTGHFEWVA SNVVRWVPHR YWPPHTRVSV GVQELTEGFE
TGDALIGVAS ISAHTFTVSR NGEVLRTMPA SLGKPSRPTP IGSFHAMSKE RTVVMDSRTI
GIPLNSSDGY LLTAHYAVRV TWSGVYVHSA PWSVNSQGYA NVSHGCINLS PDNAAWYFDA
VTVGDPIEVV G
