LDT4_MYCTU
ID LDT4_MYCTU Reviewed; 366 AA.
AC O07436; I6WXN8; L0T2T1;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=L,D-transpeptidase 4;
DE Short=LDT 4;
DE EC=2.3.2.-;
DE AltName: Full=Ldt(Mt4);
GN OrderedLocusNames=Rv0192, RVBD_0192; ORFNames=P425_00200;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RG The Broad Institute Genome Sequencing Platform;
RA Galagan J., Kreiswirth B., Dobos K., Fortune S., Fitzgerald M., Young S.K.,
RA Zeng Q., Gargeya S., Abouelleil A., Alvarado L., Berlin A.M., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Gnerre S., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The genome sequence of Mycobacterium tuberculosis H37Rv.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A.M., Kreiswirth B., Gomez J., Victor T., Desjardins C., Abeel T.,
RA Young S., Zeng Q., Gargeya S., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., Murphy C., Naylor J., Pearson M., Poon T.W.,
RA Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The genome sequence of Mycobacterium tuberculosis H37Rv.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND ACTIVITY
RP REGULATION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=24041897; DOI=10.1128/aac.01663-13;
RA Cordillot M., Dubee V., Triboulet S., Dubost L., Marie A., Hugonnet J.E.,
RA Arthur M., Mainardi J.L.;
RT "In vitro cross-linking of Mycobacterium tuberculosis peptidoglycan by L,D-
RT transpeptidases and inactivation of these enzymes by carbapenems.";
RL Antimicrob. Agents Chemother. 57:5940-5945(2013).
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. {ECO:0000269|PubMed:24041897}.
CC -!- ACTIVITY REGULATION: Is irreversibly inactivated by the beta-lactams
CC carbapenems via the formation of a covalent adduct resulting from
CC enzyme acylation; imipenem is the most efficient drug for in vitro
CC LdtMt4 inactivation. {ECO:0000269|PubMed:24041897}.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
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DR EMBL; CP003248; AFN48041.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP42919.1; -; Genomic_DNA.
DR EMBL; JLDD01000001; KBJ41300.1; -; Genomic_DNA.
DR RefSeq; NP_214706.1; NC_000962.3.
DR RefSeq; WP_003916225.1; NZ_NVQJ01000001.1.
DR AlphaFoldDB; O07436; -.
DR SMR; O07436; -.
DR STRING; 83332.Rv0192; -.
DR PaxDb; O07436; -.
DR DNASU; 886768; -.
DR GeneID; 886768; -.
DR KEGG; mtu:Rv0192; -.
DR KEGG; mtv:RVBD_0192; -.
DR TubercuList; Rv0192; -.
DR eggNOG; COG1376; Bacteria.
DR OMA; IIINFQV; -.
DR PhylomeDB; O07436; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0071972; F:peptidoglycan L,D-transpeptidase activity; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0018104; P:peptidoglycan-protein cross-linking; IBA:GO_Central.
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 1: Evidence at protein level;
KW Acyltransferase; Cell shape; Cell wall biogenesis/degradation;
KW Peptidoglycan synthesis; Reference proteome; Transferase.
FT CHAIN 1..366
FT /note="L,D-transpeptidase 4"
FT /id="PRO_0000430336"
FT DOMAIN 226..348
FT /note="YkuD"
FT REGION 21..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..114
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 307
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 325
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 289
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 302..303
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 327
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 325
FT /note="Binds to carbapenem drug (covalent)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 366 AA; 38904 MW; 6B66589CE4C3F323 CRC64;
MPHWAEERHR RESNYVALEA GLDEGESIRR SEHSRSGCGA DAGCWRCRGG PGRGSRRSRR
SRGPGGTAGP VDPPAVDLLA PPPDPLALPP ALDPLAPPPP DPLAPPPPDP LAVPVAAGPV
AGQDPTSFVG PPPFRPPTFN PVDGAMVGVA KPIVINFAVP IADRAMAESA IHISSIPPVP
GKFYWMSPTQ VRWRPFEFWP ANTAVNIDAA GTKSSFRTGD SLVATADDAT HQMTITRNGV
VQKTFPMSMG MVSGGHQTPN GTYYVLEKFA TVVMDSSTYG VPVNSAQGYK LTVSDAVRID
NSGNFVHSAP WSVADQGKRN VTHGCINLSP ANAKWFYDNF GSGDPVVVKN SVGTYNKNDG
AQDWQI
