ID A0A1Y2STI4_9GAMM Unreviewed; 573 AA.
AC A0A1Y2STI4;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Murein L,D-transpeptidase {ECO:0000313|EMBL:OTA21677.1};
GN ORFNames=Xbed_00427 {ECO:0000313|EMBL:OTA21677.1};
OS Xenorhabdus beddingii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=40578 {ECO:0000313|EMBL:OTA21677.1, ECO:0000313|Proteomes:UP000194204};
RN [1] {ECO:0000313|EMBL:OTA21677.1, ECO:0000313|Proteomes:UP000194204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4764 {ECO:0000313|EMBL:OTA21677.1,
RC ECO:0000313|Proteomes:UP000194204};
RA Tobias N.J., Wolff H., Djahanschiri B., Ebersberger I., Bode H.B.;
RT "Deconstructing symbiosis and pathogenesis requirements using a combined
RT genomic-metabolomic approach.";
RL Submitted (JAN-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}.
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:OTA21677.1}.
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DR EMBL; MUBK01000002; OTA21677.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2STI4; -.
DR STRING; 40578.Xbed_00427; -.
DR OrthoDB; 9778545at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000194204; 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 Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..573
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012418037"
FT DOMAIN 88..218
FT /note="L,D-transpeptidase scaffold"
FT /evidence="ECO:0000259|Pfam:PF20142"
FT DOMAIN 243..299
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 330..497
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
FT REGION 36..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 573 AA; 64531 MW; 773680E48D34DE31 CRC64;
MAKNSVRLLK VSFICSALAV SEGTFATQQN DQASSDVQQL AGEQKKEGSL ASSDQTIPIS
PIKSIGENRK QLQNGLPQQV KPVFLDRLVT LYTANEMKLL WTDKKAIQQF ESQLFEISLA
GFQPQFEKWL VQLDSPELSD MGRDIILSDA MLGYLHFING VKKKGDSWLY SKTPYKVDLP
PAHLIDKWQQ HINNHDTLTY ITALSPHHPM YENMRKEMLA QLADKQPWTE FSLKGTLRPG
QSSESVIALR KILVRSGTLE PSAIKSDNKI YAKELTAAVK RFQTLHGLSA DGVIGQSTKI
WLNTTPQMRA RIMALNIQRL RIIPGDIPTG ILVNIPNYSL FYYSDGKEVL SSKVVVGRPS
RKTPIMSSQL NNVVINPPWT VPTSMTRKDI APRAMRDPNY FRTRGYTVFS SWSNDAKVID
PLSINWGVIT PDNFPYRIRQ APGPTNSLGR FKFNMPNSEA IYLHDTPNQA SFSREMRAVS
SGCVRVNKAP ELANMLLGDA GWNKDKVKGS LKTWGTKYVN IPQKIPVFLY YQTAWVDEGG
VPQYRADIYG YDMNARQPSE WLSKILAARK DLS
//