ID   A0A011PSL3_9PROT        Unreviewed;       340 AA.
AC   A0A011PSL3;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=L,D-transpeptidase catalytic domain protein {ECO:0000313|EMBL:EXI69364.1};
DE   Flags: Precursor;
GN   ORFNames=AW08_00575 {ECO:0000313|EMBL:EXI69364.1};
OS   Candidatus Accumulibacter adjunctus.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Candidatus Accumulibacter.
OX   NCBI_TaxID=1454001 {ECO:0000313|EMBL:EXI69364.1, ECO:0000313|Proteomes:UP000020218};
RN   [1] {ECO:0000313|EMBL:EXI69364.1, ECO:0000313|Proteomes:UP000020218}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK-12 {ECO:0000313|Proteomes:UP000020218};
RA   Skennerton C.T., Barr J.J., Slater F.R., Bond P.L., Tyson G.W.;
RT   "Expanding our view of genomic diversity in Candidatus Accumulibacter
RT   clades.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
CC   -!- SIMILARITY: Belongs to the YkuD family.
CC       {ECO:0000256|ARBA:ARBA00005992}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EXI69364.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JFAX01000002; EXI69364.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A011PSL3; -.
DR   STRING; 1454001.AW08_00575; -.
DR   PATRIC; fig|1454001.3.peg.548; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000020218; Unassembled WGS sequence.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProt.
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   InterPro; IPR016915; UCP029342.
DR   PANTHER; PTHR30582; L,D-TRANSPEPTIDASE; 1.
DR   PANTHER; PTHR30582:SF34; L,D-TRANSPEPTIDASE YCIB-RELATED; 1.
DR   Pfam; PF03734; YkuD; 1.
DR   PIRSF; PIRSF029342; UCP029342_ErfK/YbiS/YcfS/YnhG; 1.
DR   SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000020218};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..340
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001462993"
FT   DOMAIN          60..167
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
SQ   SEQUENCE   340 AA;  36655 MW;  64356D36513E3D1C CRC64;
     MTKLYMMAVA LFLGLAGSVQ AERTPFWGAR EPVPFETPAD QLRNGEFTWA PPLAPAGPIL
     VLVSLEEQRA YTYRNGLLTG VASVSTGKPG YETPSGVFQT FLKDKDHHST KYHNAAMPYT
     QKFTQDGVAL HAGGVPGYPE SHGCVHLPSE FARLLFDAAP KGMTVVIAKA GSAPEEFRHP
     AFLSPLTEAG GRAEHRRLPV ATSHRWEPEK SPSGPLSILL SRYDERILVL RSGVEIGRAK
     AAFHKPKQPV GSHVFVAKEG AQPGGLLQHR WVGVALVGHM GDADTRPDPR VVDEVTVPAD
     FQALLAAEIR PGTTLMVTDA PVLEHTTGLD MAVLSSFPGH
//