ID A0A196N697_9SPHN Unreviewed; 330 AA.
AC A0A196N697;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=YkuD domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=A7X12_21505 {ECO:0000313|EMBL:OAN62761.1};
OS Sphingomonas sp. TDK1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=453247 {ECO:0000313|EMBL:OAN62761.1, ECO:0000313|Proteomes:UP000078445};
RN [1] {ECO:0000313|EMBL:OAN62761.1, ECO:0000313|Proteomes:UP000078445}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TDK1 {ECO:0000313|EMBL:OAN62761.1,
RC ECO:0000313|Proteomes:UP000078445};
RA Takahashi S.;
RT "Draft Genome Sequences of Sphingobium sp. strain TCM1 and Sphingomonas sp.
RT strain TDK1, Haloalkyl Organophosphorus Flame Retardant-Degrading
RT Bacteria.";
RL Submitted (MAY-2016) 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:OAN62761.1}.
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DR EMBL; LXVY01000025; OAN62761.1; -; Genomic_DNA.
DR RefSeq; WP_064312163.1; NZ_LXVY01000025.1.
DR AlphaFoldDB; A0A196N697; -.
DR STRING; 453247.A7X12_21505; -.
DR OrthoDB; 9787225at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000078445; 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 Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 1.
DR InterPro; IPR005490; LD_TPept_cat_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; PTHR30582:SF30; BLR4375 PROTEIN; 1.
DR PANTHER; PTHR30582; L,D-TRANSPEPTIDASE; 1.
DR Pfam; PF01471; PG_binding_1; 1.
DR Pfam; PF03734; YkuD; 1.
DR SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
DR SUPFAM; SSF47090; PGBD-like; 1.
PE 3: Inferred from homology;
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..330
FT /note="YkuD domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008272666"
FT DOMAIN 31..83
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 196..325
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
SQ SEQUENCE 330 AA; 35737 MW; 5ED4FEC2641B1A02 CRC64;
MRKWVFGTAV LLAAPALAQT PAPKPSIDLN ILHAQVILDH LGFGPGILDG RAGQSLTAAV
RGLQEARGLK VTGVIDPATL AVLHQYRALR PVRILAVGAE TMQGPFVDPI PKDLGQQGKL
KALGYRNPLE KLAEMFHTTP EVIGALNPGV TTIKAGTMLR LPNALPGSRA YPAEWKPEWR
QTLNMLNVDP RQPQADHIVV DKSEGVLKVF GAGNRLVAQF SATMGSEHDP LPIGSWKING
VDTNPKFHYN PKLFWDAKKG DDPAMLPPGP NGPVGVVWID LSKEHYGIHG TPEPQTIGRT
ESHGCIRLTN WDAARVALMV KPGTPARFRE
//
