ID   A0A1Y6F3Q8_9SPHN        Unreviewed;       464 AA.
AC   A0A1Y6F3Q8;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=L,D-transpeptidase catalytic domain {ECO:0000313|EMBL:SMQ69558.1};
GN   ORFNames=SAMN06297468_1742 {ECO:0000313|EMBL:SMQ69558.1};
OS   Altererythrobacter xiamenensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Altererythrobacter.
OX   NCBI_TaxID=1316679 {ECO:0000313|EMBL:SMQ69558.1, ECO:0000313|Proteomes:UP000194420};
RN   [1] {ECO:0000313|Proteomes:UP000194420}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Varghese N., Submissions S.;
RL   Submitted (APR-2017) 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}.
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DR   EMBL; FXWG01000002; SMQ69558.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y6F3Q8; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000194420; 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; IPR045380; LD_TPept_scaffold_dom.
DR   InterPro; IPR038063; Transpep_catalytic_dom.
DR   PANTHER; PTHR41533:SF2; BLR7131 PROTEIN; 1.
DR   PANTHER; PTHR41533; L,D-TRANSPEPTIDASE HI_1667-RELATED; 1.
DR   Pfam; PF20142; Scaffold; 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   Reference proteome {ECO:0000313|Proteomes:UP000194420};
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..464
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012757433"
FT   DOMAIN          78..191
FT                   /note="L,D-transpeptidase scaffold"
FT                   /evidence="ECO:0000259|Pfam:PF20142"
FT   DOMAIN          222..369
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
SQ   SEQUENCE   464 AA;  50987 MW;  BF20F39CB90EE803 CRC64;
     MRSSVGKWMV SAAAVSVACT AWAQEAQPES LLPEDDTIEA QADPESFDEA FPKMVSDPLV
     QGNLDAEPAP LVVPWSVANA EALLQVIEGI GAEGLNPSDY DGQALSTAIA SGPSSELDEI
     ASKNFVWLVE DLRDGRTPMD ARKQWFVVDP DRDRFRTSDL LAKAVESGDI AGTLEQLHPT
     HPDYGHLKEA LAETPESDTR TRKLIRANMD RWRWLARDLG KQYLITNVPE YQLRLTVNDK
     IISTYRTIVG KPGRTATPQL AEKVEGVVFN PTWTVPQSIV KGEGLGAKVL NNPAWARRAG
     YKATKGANGW ISVVQQPGPG NSLGQMKLEM PNRHAIFFHD TPSRHLFNND DRALSHGCIR
     TERALELAIT MAILGKGASK EEAVEIATSG EYTLVPIERE MPAYITYFTM ATDINGELST
     FKDIYDRDAP VLASLDAPRV NNRAQETDEE VIVIENDPRA IGAD
//