ID W1IXT9_9GAMM Unreviewed; 571 AA.
AC W1IXT9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Putative L,D-transpeptidase YcbB {ECO:0000313|EMBL:CDL82648.1};
DE EC=2.-.-.- {ECO:0000313|EMBL:CDL82648.1};
GN Name=ycbB {ECO:0000313|EMBL:CDL82648.1};
GN ORFNames=XSR1_220030 {ECO:0000313|EMBL:CDL82648.1};
OS Xenorhabdus szentirmaii DSM 16338.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=1427518 {ECO:0000313|EMBL:CDL82648.1, ECO:0000313|Proteomes:UP000019202};
RN [1] {ECO:0000313|EMBL:CDL82648.1, ECO:0000313|Proteomes:UP000019202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16338 {ECO:0000313|EMBL:CDL82648.1,
RC ECO:0000313|Proteomes:UP000019202};
RA Gualtieri M., Ogier J.C., Pages S., Givaudan A., Gaudriault S.;
RT "Draft genome sequence and annotation of the entomopathogenic bacteria,
RT Xenorhabdus cabanillasi strain JM26 and Xenorhabdus szentirmai strain DSM
RT 16338.";
RL Submitted (NOV-2013) 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:CDL82648.1}.
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DR EMBL; CBXF010000080; CDL82648.1; -; Genomic_DNA.
DR RefSeq; WP_038237232.1; NZ_NIBV01000002.1.
DR AlphaFoldDB; W1IXT9; -.
DR STRING; 1427518.XSR1_220030; -.
DR OrthoDB; 9778545at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000019202; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProt.
DR GO; GO:0016757; F:glycosyltransferase 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; L,D-TRANSPEPTIDASE HI_1667-RELATED; 1.
DR PANTHER; PTHR41533:SF1; L,D-TRANSPEPTIDASE YCBB-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 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000019202};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CDL82648.1}.
FT DOMAIN 87..217
FT /note="L,D-transpeptidase scaffold"
FT /evidence="ECO:0000259|Pfam:PF20142"
FT DOMAIN 242..299
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 329..496
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
SQ SEQUENCE 571 AA; 64751 MW; 6263F18414684CD2 CRC64;
MAKNTIRLLK VSFIFSALVI SEGLANQQNG LVVNGVQQLS EEQKKADIVV SADKTIPIFS
VHSVDENRKQ LQNWLPQQVK PIFFERLVTL YSANKMQPLW TDKKAVQQFE NQLIEISLAG
FQPQFEKWLM QLNSPELSDI GRDIILSDAM LGYLHFINNV QKKGDAWLYG KNTYKIDLPP
SNVIDKWQQS INDNLVLSYI KGLSPNHPMY ENMRKEMLSQ LSDNQSWPEF SFKGTLRPGQ
NSDSVIELRK ILVRTGTLDS SDAKAESQVY SKELVAAVKR FQALHGLSVD GVIGKSTKVW
LNTTPKIRAR IMALNIQRLR IIPGNIATGI LVNIPDYSLF YYLNGKEVLS SKVVVGRSSR
KTPIMSSELN NVVINPPWTV PTSMTRKDIA PRAMNDPNYF RSRGYTVFSS WSNDASVVDP
STINWGVITP SNFPYRLRQA PGPGNSLGRF KFNMPNSEAI YLHDTPNKAS FSREMRAVSS
GCVRVNKAPE LANMLLGDAG WDKTKVSNSL KTWTTKYVNI PKKIPVFLYY QTAWVNEKDE
PQYRADIYSY DESARQQSEP LFKFLVSRND L
//
