ID A0A9X0UGV8_VIBME Unreviewed; 512 AA.
AC A0A9X0UGV8;
DT 08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2023, sequence version 1.
DT 28-JAN-2026, entry version 10.
DE SubName: Full=L,D-transpeptidase family protein {ECO:0000313|EMBL:MBC5850145.1};
GN ORFNames=H8Q88_04125 {ECO:0000313|EMBL:MBC5850145.1};
OS Vibrio metschnikovii.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Vibrionales;
OC Vibrionaceae; Vibrio.
OX NCBI_TaxID=28172 {ECO:0000313|EMBL:MBC5850145.1, ECO:0000313|Proteomes:UP000615796};
RN [1] {ECO:0000313|EMBL:MBC5850145.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=M13F {ECO:0000313|EMBL:MBC5850145.1};
RA Zheng L.;
RT "Genome Sequencing and Pan-Genome Analysis of Migratory bird Vibrio
RT Strains, Inner Mongolia.";
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|PROSITE-ProRule:PRU01373}.
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:MBC5850145.1}.
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DR EMBL; JACRUP010000001; MBC5850145.1; -; Genomic_DNA.
DR RefSeq; WP_187025355.1; NZ_JACRUP010000001.1.
DR AlphaFoldDB; A0A9X0UGV8; -.
DR Proteomes; UP000615796; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-ARBA.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-UniRule.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-UniRule.
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; IPR052905; LD-transpeptidase_YkuD-like.
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.
DR PROSITE; PS52029; LD_TPASE; 1.
PE 3: Inferred from homology;
KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|PROSITE-
KW ProRule:PRU01373};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|PROSITE-ProRule:PRU01373};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984,
KW ECO:0000256|PROSITE-ProRule:PRU01373};
KW Reference proteome {ECO:0000313|Proteomes:UP000615796};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..512
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5040734359"
FT DOMAIN 287..464
FT /note="L,D-TPase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS52029"
FT ACT_SITE 421
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01373"
FT ACT_SITE 440
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01373"
SQ SEQUENCE 512 AA; 58973 MW; B6C865FB68B8A1A5 CRC64;
MKRYSLMAIV LLWISFPLFA NTPVVQLSDL KGQSEYALHY PQQVEKLYQR NQYQLIWRDE
LSRVYFEQQL ALIHQANISP LFSKRYKQLR ALSEQQAWVQ YDVLATDTII GYLSYAQLAP
QQGIDWFFNG KLNHVLPLPS ASSRLALSVA AGTPAIADLV LQHAPQDPAY HQLVYAHGFL
SALKATPLPL YRQAGLKRPG DKLDDRLTLI QRLALVNIDV TVIRDDVSWY DNSLIEPIKH
FQQLHGLNAD GVIGPQTLKW LNLSVEERLG LIALNAERMR LWPTSNTSIV VNVPSFELKY
WHAGENVFQS KVVVGRISRP TPVMTTRLDS LIVNPTWNIP YKIMVEDILP MAKRDLRYLD
RQNLEILPRW GATQTLDPTS IDWENISLEA FPYRMRQRAG YHNALGLYKF NTPNRRAIFL
HDTPSKYLFE RDSRAFSSGC IRVEHADQFA NLLLTKQGLD SRQFAPQSSP VNQAIPLRQR
IPVQIIYQTA WYDAGQLHFR EDIYRLDKLV TQ
//
