ID A0A073J5F8_9RHOB Unreviewed; 459 AA.
AC A0A073J5F8;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=L,D-transpeptidase YkuD {ECO:0008006|Google:ProtNLM};
GN ORFNames=SUH3_02435 {ECO:0000313|EMBL:KEJ97863.1};
OS Pseudosulfitobacter pseudonitzschiae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Pseudosulfitobacter.
OX NCBI_TaxID=1402135 {ECO:0000313|EMBL:KEJ97863.1, ECO:0000313|Proteomes:UP000027746};
RN [1] {ECO:0000313|EMBL:KEJ97863.1, ECO:0000313|Proteomes:UP000027746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H3 {ECO:0000313|EMBL:KEJ97863.1,
RC ECO:0000313|Proteomes:UP000027746};
RA Lai Q., Hong Z.;
RT "Sulfitobacter sp. H3 (MCCC 1A00686) Genome Sequencing.";
RL Submitted (JAN-2014) 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:KEJ97863.1}.
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DR EMBL; JAMD01000001; KEJ97863.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A073J5F8; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000027746; 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 Reference proteome {ECO:0000313|Proteomes:UP000027746};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..459
FT /note="L,D-transpeptidase YkuD"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001690268"
FT DOMAIN 186..237
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 327..455
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
FT REGION 29..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 459 AA; 47979 MW; E6E725CA80AEF1DA CRC64;
MSYTSHIARI TLLTLIASPL VAQTPTTTQL DPAPIVPPVT QQPIAPQQAP AAPQSDAPAA
GDPIIPMAES ALDDVQVEPG VQGNPSDTRI PSVSELSKAL QDKENGETQG DVGLGTDNVI
TINPDTVEPN PGPPQDTGQA TGQGVGGITP AAQPPIPSQP VTPATVNAAS YSGVGGLPEG
RSPVTVKLQV LLDRAGVSVS IIDGVKGGMT ESALKAYEAR MGLPVDGLLD AEVWDMLGGN
DIDVYMKQYT ITEADTQGLS APLPRDYGEL AKLDRMGYTS VSEKLAERFH MSESFLKLVN
PGAGFYAGET IVVVEPGANA VGKVVKIIID KSDRRLRAWD ATGTEIANYP VAIGSAGTPS
PSGHMTVEAV ALEPTYHYNP SVNFKQGDND KPLTLPPGPN GPVGLVWIDL SKPTYGIHGT
PEPASLFTAH SHGCVRMANW DAQELASLVS EGVIVDFRE
//
