ID A0A1D8AYS0_9BACT Unreviewed; 143 AA.
AC A0A1D8AYS0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=L,D-transpeptidase catalytic domain {ECO:0000313|EMBL:AOS46038.1};
GN ORFNames=Verru16b_03132 {ECO:0000313|EMBL:AOS46038.1};
OS Lacunisphaera limnophila.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae;
OC Lacunisphaera.
OX NCBI_TaxID=1838286 {ECO:0000313|EMBL:AOS46038.1, ECO:0000313|Proteomes:UP000095228};
RN [1] {ECO:0000313|EMBL:AOS46038.1, ECO:0000313|Proteomes:UP000095228}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IG16b {ECO:0000313|EMBL:AOS46038.1,
RC ECO:0000313|Proteomes:UP000095228};
RA Rast P., Gloeckner I., Jogler M., Boedeker C., Jeske O., Wiegand S.,
RA Reinhardt R., Schumann P., Rohde M., Spring S., Gloeckner F.O., Jogler C.;
RT "Three novel species with peptidoglycan cell walls form the new genus
RT Lacunisphaera gen. nov. in the family Opitutaceae of the verrucomicrobial
RT subdivision 4.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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DR EMBL; CP016094; AOS46038.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D8AYS0; -.
DR STRING; 1838286.Verru16b_03132; -.
DR KEGG; obg:Verru16b_03132; -.
DR PATRIC; fig|1838286.3.peg.3155; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000095228; Chromosome.
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 Pfam; PF03734; YkuD; 1.
DR SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000095228};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 21..141
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 143 AA; 15770 MW; 3959FCDDE014A5F3 CRC64;
MVRSHVISTS LRPPSNVKDS LGTPRGLHEI AEKVGAGQPP GIVFKARVAT GQHYSELSAA
EQARNLITTR ILWLRGLEPG HNAGTAATGE VVDTYARYVY IHGTNHEERL GRPFSGGCIE
MNNLEILALF DEIRPRDQVW IED
//
