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Database: UniProt
Entry: A0A0D0QCB6_9RHOB
LinkDB: A0A0D0QCB6_9RHOB
Original site: A0A0D0QCB6_9RHOB 
ID   A0A0D0QCB6_9RHOB        Unreviewed;       371 AA.
AC   A0A0D0QCB6;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=YkuD domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=Wenmar_01537 {ECO:0000313|EMBL:KIQ69967.1};
OS   Wenxinia marina DSM 24838.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Wenxinia.
OX   NCBI_TaxID=1123501 {ECO:0000313|EMBL:KIQ69967.1, ECO:0000313|Proteomes:UP000035100};
RN   [1] {ECO:0000313|EMBL:KIQ69967.1, ECO:0000313|Proteomes:UP000035100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24838 {ECO:0000313|EMBL:KIQ69967.1,
RC   ECO:0000313|Proteomes:UP000035100};
RA   Fiebig A., Goeker M., Klenk H.-P.P.;
RL   Submitted (JAN-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:KIQ69967.1}.
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DR   EMBL; AONG01000008; KIQ69967.1; -; Genomic_DNA.
DR   RefSeq; WP_018301099.1; NZ_KN848372.1.
DR   AlphaFoldDB; A0A0D0QCB6; -.
DR   STRING; 1123501.Wenmar_01537; -.
DR   PATRIC; fig|1123501.6.peg.1627; -.
DR   eggNOG; COG1376; Bacteria.
DR   OrthoDB; 9787225at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000035100; 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:UP000035100};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..371
FT                   /note="YkuD domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002219121"
FT   DOMAIN          99..150
FT                   /note="Peptidoglycan binding-like"
FT                   /evidence="ECO:0000259|Pfam:PF01471"
FT   DOMAIN          239..368
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
FT   REGION          37..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   371 AA;  38617 MW;  746E092A9B285680 CRC64;
     MRPFPLILLA LAAHGAAAQN AAPTLDEILD AFERAPTSDL APAPAPAAAP PQAPEVVAAP
     QTAPAAPEAA TDRMPTPAEI ESVTYAGGPL PEGRSALTVK LQILLDRSGI SPGVIDGWRG
     GMSESAIAAF ETRAGLPVDG ILDPEVWAQL GGDEPGAVLA SYTVVPADLE NLSGELPSDY
     ALLAQLPHLG HERASERIAE FFHMTEEFLI GLNPGATFQP GETLTVAALG AHAAEPVAAI
     VIDKTTRRLT GYDAAGNLVV NYPVTVGSTD TPSPSGHVTV ERIALMPEYS YNPENFIQGD
     NMSRLTLPPG PNGPVGSVWI ALSKPSYGIH GTPEPSSLFR SQSHGCVRLT NWDAEELAGL
     VTPGVSVVFQ D
//
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