ID   A0A3Q9IWR6_9MICO        Unreviewed;       493 AA.
AC   A0A3Q9IWR6;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=L,D-transpeptidase catalytic domain-containing protein {ECO:0000259|Pfam:PF03734};
GN   ORFNames=CVS47_00640 {ECO:0000313|EMBL:AZS36041.1};
OS   Microbacterium lemovicicum.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1072463 {ECO:0000313|EMBL:AZS36041.1, ECO:0000313|Proteomes:UP000276888};
RN   [1] {ECO:0000313|EMBL:AZS36041.1, ECO:0000313|Proteomes:UP000276888}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Viu22 {ECO:0000313|EMBL:AZS36041.1,
RC   ECO:0000313|Proteomes:UP000276888};
RA   ORTET P.;
RT   "Microbacterium lemovicicum sp. nov., a bacterium isolated from a natural
RT   uranium-rich soil.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
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DR   EMBL; CP031423; AZS36041.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3Q9IWR6; -.
DR   KEGG; mlv:CVS47_00640; -.
DR   OrthoDB; 3176960at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000276888; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd16913; YkuD_like; 1.
DR   Gene3D; 2.40.440.10; L,D-transpeptidase catalytic domain-like; 1.
DR   InterPro; IPR005490; LD_TPept_cat_dom.
DR   InterPro; IPR038063; Transpep_catalytic_dom.
DR   PANTHER; PTHR30582; L,D-TRANSPEPTIDASE; 1.
DR   PANTHER; PTHR30582:SF2; SLL0670 PROTEIN; 1.
DR   Pfam; PF03734; YkuD; 1.
DR   SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276888};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        51..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          373..491
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   493 AA;  50475 MW;  9169584491AD6412 CRC64;
     MTDLATKPNA DEAPSGVPSD APTTPIQSGG DGAAFGYEWA PAEPAPKKRH LGLWIGIPAA
     AAVVGLVAAS LVLIAPGSAI AGVPVGGMTP GSAAEAVQNR LAETTVVLTG AGGDVAVSGA
     DLGATVDAQA LADAAFAQNP MWNPTAWFAA PIDAPVTVDP ATATEALREA VPGLYSEPVG
     AQVAFDANTA SFAVTAAQSG EGVDVAAVQG ALQDAFESGA TSIDLAPALV PIDSSTTTEL
     AQATADKLNG VLDTVGFYIG DERTVPVDRA VAASWLTVTP AENGDFTVTA DAAAIQPTVD
     GLAAAVNRDV VNATVITDSS GNALSDLTAG VVGRALDSTD GVAGAFATQL ADGNGVYPLA
     VSEVPFTTTT LARRIEVDLS AQRTYLFENN AVVQSWAVSS GLTPNDTPTG DFRMQAHVRI
     QGMGNRDLTK EPHYYTPDVP YVSYFNGDIA FHGTYWHNNF GNPMSHGCIN MTIDAAQYVY
     DWAPLGTEVS VYY
//