ID W1J9N3_9GAMM Unreviewed; 575 AA.
AC W1J9N3;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Putative L,D-transpeptidase YcbB {ECO:0000313|EMBL:CDL87409.1};
DE EC=2.-.-.- {ECO:0000313|EMBL:CDL87409.1};
GN Name=ycbB {ECO:0000313|EMBL:CDL87409.1};
GN ORFNames=XCR1_900029 {ECO:0000313|EMBL:CDL87409.1};
OS Xenorhabdus cabanillasii JM26.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=1427517 {ECO:0000313|EMBL:CDL87409.1, ECO:0000313|Proteomes:UP000019197};
RN [1] {ECO:0000313|EMBL:CDL87409.1, ECO:0000313|Proteomes:UP000019197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JM26 {ECO:0000313|EMBL:CDL87409.1,
RC ECO:0000313|Proteomes:UP000019197};
RA Gualtieri M., Ogier J.C., Pages S., Givaudan A., Gaudriault S.;
RT "Draft genome sequence and annotation of the entomopathogenic bacterium,
RT Xenorhabdus cabanillasi strain JM26.";
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:CDL87409.1}.
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DR EMBL; CBXE010000487; CDL87409.1; -; Genomic_DNA.
DR RefSeq; WP_038269293.1; NZ_NJGH01000011.1.
DR AlphaFoldDB; W1J9N3; -.
DR OrthoDB; 9778545at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000019197; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CDL87409.1}.
FT DOMAIN 87..217
FT /note="L,D-transpeptidase scaffold"
FT /evidence="ECO:0000259|Pfam:PF20142"
FT DOMAIN 244..301
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 329..497
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
SQ SEQUENCE 575 AA; 65540 MW; CE77693088A3020A CRC64;
MANNAVRLLK FYFIYSILVV SEGTFASQQN GLIANDVQQF SGKQKKADIN ITSTQIASVF
STSSLEESKK QLQNLLPRKI TFVFSEQLAR LYSVNNMKPL WRDKNAIQYF ERQLFDLSLA
GFQPQFGQWL VQLNSPELSD MGRDIILSDA MLGYLHFINN IHNKGDLWLY GKTPYKIDLP
SSDSIEKWQK HISSNSLSDY ISGLSPNHSM YENMRSEMLK QLLDKQPWSE FSMKETLRPG
QSSKSIIALR NILIRAGTLE SSAVRPENKV YNKELVAAVK RFQSLHGLSA DGVIGQSTRV
WLNTTPQTRA RIMALNMQRL RIIPDNLPTA ILVNIPNYSL FYYLDGEKVL TSKVVVGRPS
RKTPIMSSEM NNVVINPPWT VPVSMTRKDI APRAMRDPNY FRSRGYTVFS SWHSDATVIN
PSSINWRVIT PGNFPYRIRQ APGPTNSLGR FKFNMPNSEA IYLHDTPNQA LFNREMRAVS
SGCVRVNKAP ELANMLLGDA GWDKSRVSNS LKTWTTRYVN IPKKIPVFLY YQTAWVDEKG
KPQYRADIYK YDNNARKKSE LVSQILAIKS DTLSP
//
