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L,D-transpeptidase 1 (LDT 1) (EC 2.3.2.-) (Ldt(Mt1))

 LDT1_MYCTO              Reviewed;         251 AA.
Q7DAG3;
01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
01-OCT-2014, sequence version 2.
07-JUN-2017, entry version 58.
RecName: Full=L,D-transpeptidase 1;
Short=LDT 1;
EC=2.3.2.-;
AltName: Full=Ldt(Mt1);
Flags: Precursor;
Name=ldtA; OrderedLocusNames=MT0125;
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83331;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CDC 1551 / Oshkosh;
PubMed=12218036; DOI=10.1128/JB.184.19.5479-5490.2002;
Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H.,
Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D.,
Salzberg S.L., Delcher A., Utterback T.R., Weidman J.F., Khouri H.M.,
Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C.,
Fraser C.M.;
"Whole-genome comparison of Mycobacterium tuberculosis clinical and
laboratory strains.";
J. Bacteriol. 184:5479-5490(2002).
[2]
DISRUPTION PHENOTYPE.
STRAIN=CDC 1551 / Oshkosh;
PubMed=24464457; DOI=10.1128/JB.01396-13;
Schoonmaker M.K., Bishai W.R., Lamichhane G.;
"Nonclassical transpeptidases of Mycobacterium tuberculosis alter cell
size, morphology, the cytosolic matrix, protein localization,
virulence, and resistance to beta-lactams.";
J. Bacteriol. 196:1394-1402(2014).
-!- FUNCTION: Generates 3->3 cross-links in peptidoglycan, catalyzing
the cleavage of the mDap(3)-D-Ala(4) bond of a tetrapeptide donor
stem and the formation of a bond between the carbonyl of mDap(3)
of the donor stem and the side chain of mDap(3) of the acceptor
stem. Is specific for donor substrates containing a stem
tetrapeptide since it cannot use pentapeptide stems (By
similarity). {ECO:0000250}.
-!- ENZYME REGULATION: Is irreversibly inactivated by the beta-lactams
carbapenems via the formation of a covalent adduct resulting from
acylation of the catalytic Cys. {ECO:0000250}.
-!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
-!- SUBUNIT: Monomer. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
-!- DISRUPTION PHENOTYPE: Lack of this gene alone does not alter in
vitro and in vivo growth rate or colony and cell shape and
morphology. But loss of both LdtMt1 and LdtMt2 severely alters
cellular shape, intracellular morphology, physiology and
virulence: the length of mutant cells are shorter than wild-type,
they have deep surface depressions and bulges, they possess large
unstained vacuole-like structures, the thickness of the
peptidoglycan layer is smaller, the protein localization is
altered, and in vitro and in vivo growth and virulence are severly
attenuated. Moreover, double-mutant cells are more sensitive to
vancomycin and amoxicillin-clavulanate.
{ECO:0000269|PubMed:24464457}.
-!- SEQUENCE CAUTION:
Sequence=AAK44348.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AE000516; AAK44348.1; ALT_INIT; Genomic_DNA.
RefSeq; WP_003400856.1; NZ_KK341227.1.
ProteinModelPortal; Q7DAG3; -.
SMR; Q7DAG3; -.
EnsemblBacteria; AAK44348; AAK44348; MT0125.
KEGG; mtc:MT0125; -.
PATRIC; fig|83331.31.peg.132; -.
HOGENOM; HOG000241380; -.
OrthoDB; POG091H07H2; -.
UniPathway; UPA00219; -.
Proteomes; UP000001020; Chromosome.
GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
InterPro; IPR005490; LD_TPept_cat_dom.
Pfam; PF03734; YkuD; 1.
3: Inferred from homology;
Acyltransferase; Cell shape; Cell wall biogenesis/degradation;
Complete proteome; Peptidoglycan synthesis; Periplasm; Signal;
Transferase.
SIGNAL 1 28 {ECO:0000255}.
CHAIN 29 251 L,D-transpeptidase 1.
/FTId=PRO_0000430331.
DOMAIN 129 249 YkuD.
REGION 203 204 Substrate binding. {ECO:0000250}.
ACT_SITE 208 208 Proton donor/acceptor. {ECO:0000250}.
ACT_SITE 226 226 Nucleophile. {ECO:0000250}.
BINDING 190 190 Substrate. {ECO:0000250}.
BINDING 228 228 Substrate. {ECO:0000250}.
SITE 226 226 Binds to carbapenem drug (covalent).
{ECO:0000250}.
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


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