ID   A0A418PZ34_9SPHN        Unreviewed;       193 AA.
AC   A0A418PZ34;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=L,D-transpeptidase catalytic domain-containing protein {ECO:0000259|Pfam:PF03734};
GN   ORFNames=D3M59_07255 {ECO:0000313|EMBL:RIX29111.1};
OS   Sphingomonas edaphi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=2315689 {ECO:0000313|EMBL:RIX29111.1, ECO:0000313|Proteomes:UP000285023};
RN   [1] {ECO:0000313|EMBL:RIX29111.1, ECO:0000313|Proteomes:UP000285023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAC4 {ECO:0000313|EMBL:RIX29111.1,
RC   ECO:0000313|Proteomes:UP000285023};
RA   Seo T.;
RT   "Sphingomonas sp. DAC4.";
RL   Submitted (SEP-2018) 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:RIX29111.1}.
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DR   EMBL; QXTF01000002; RIX29111.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A418PZ34; -.
DR   OrthoDB; 463216at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000285023; 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   PANTHER; PTHR30582; L,D-TRANSPEPTIDASE; 1.
DR   PANTHER; PTHR30582:SF34; L,D-TRANSPEPTIDASE YCIB-RELATED; 1.
DR   Pfam; PF03734; YkuD; 1.
DR   SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..193
FT                   /note="L,D-transpeptidase catalytic domain-containing
FT                   protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019074236"
FT   DOMAIN          83..191
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
SQ   SEQUENCE   193 AA;  20928 MW;  0BA85D3858C6A20D CRC64;
     MRKILAALTV GGALALAACS TTAPPPPVPR IATPKFVPPA TNYRWTNGFS ASGFEAMHAM
     IGRTSLRPGE FHWSPNVPVD GDVAITVDIA NQVAFIFKGA QLIGVTNVST GKKGHPTPLG
     FWKINWKREK YFSRKYDNAP MPWMQNIDDK GIAFHGGKTP GFPASHGCIR LPMAFAKHLF
     TLTKKGDKVV IEG
//