ID   A0A1H4BGS0_9SPHI        Unreviewed;       573 AA.
AC   A0A1H4BGS0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Murein L,D-transpeptidase YcbB/YkuD {ECO:0000313|EMBL:SEA47002.1};
GN   ORFNames=SAMN05443550_103331 {ECO:0000313|EMBL:SEA47002.1};
OS   Pedobacter hartonius.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=425514 {ECO:0000313|EMBL:SEA47002.1, ECO:0000313|Proteomes:UP000198850};
RN   [1] {ECO:0000313|EMBL:SEA47002.1, ECO:0000313|Proteomes:UP000198850}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19033 {ECO:0000313|EMBL:SEA47002.1,
RC   ECO:0000313|Proteomes:UP000198850};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FNRA01000003; SEA47002.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H4BGS0; -.
DR   STRING; 425514.SAMN05443550_103331; -.
DR   OrthoDB; 9778545at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000198850; Unassembled WGS sequence.
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   Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 1.
DR   InterPro; IPR005490; LD_TPept_cat_dom.
DR   InterPro; IPR045380; LD_TPept_scaffold_dom.
DR   InterPro; IPR002477; Peptidoglycan-bd-like.
DR   InterPro; IPR036365; PGBD-like_sf.
DR   InterPro; IPR036366; PGBDSf.
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; PF01471; PG_binding_1; 1.
DR   Pfam; PF20142; Scaffold; 1.
DR   Pfam; PF03734; YkuD; 1.
DR   SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
DR   SUPFAM; SSF47090; PGBD-like; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000198850};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          102..242
FT                   /note="L,D-transpeptidase scaffold"
FT                   /evidence="ECO:0000259|Pfam:PF20142"
FT   DOMAIN          275..326
FT                   /note="Peptidoglycan binding-like"
FT                   /evidence="ECO:0000259|Pfam:PF01471"
FT   DOMAIN          354..502
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
SQ   SEQUENCE   573 AA;  65387 MW;  62AFA34EF3544497 CRC64;
     MTGYRGSQHK TISGTSPQKI YTGIRKSGIL IILSSMNRYI KTLSPKIILL LLLFAGCRQK
     EVKVERDLTI TPKNAVTKLL IDSLQMEKYI STQGLEDSSA NRLRNFYNSR NFQFAWLAEN
     GLAEQAKVFY ELDKNYISAS RDSTDADQAL HRQLGTLISK DTLIRSASAE LVNLELSLTQ
     HFFNFVTYAY AGKLDPAALQ WYIPRRKLDA VALLDSLVAK KGTSLENWEP VNLYYKTLNK
     ELLRWYGIRQ RGSWEKISPG KTKYIAGDTC MVISRIKQRL ADFGDLDPAD STPVFNEALG
     LAVKKAQKQF GLTESGRIDR TLIAALNIPA ELRIRQLLIN LERMKWTPSI PESKFILVNI
     PEYKLHVFES GKEVLNMGIV VGKAANKTVI FSNELKNIVF SPYWNIPPSI VRAEILPEMR
     KNKYYLAEKN MEQYGTSEGL PLIRQKPGNT NSLGRVKFLF PNSYNIYLHD TPAKSLFAEE
     KRAFSHGCIR LAQPKKLAGY LLADRSEWTG KKIDRAMNSK TEIWVNMKQP VPVFITYFTS
     WVDKDGLLNF REDLYGHDQA MARQMFKSEE SKK
//