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Database: UniProt
Entry: A0A109BQB1_HYPSL
LinkDB: A0A109BQB1_HYPSL
Original site: A0A109BQB1_HYPSL 
ID   A0A109BQB1_HYPSL        Unreviewed;       428 AA.
AC   A0A109BQB1;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=L,D-transpeptidase YcbB {ECO:0008006|Google:ProtNLM};
GN   ORFNames=APY04_0005 {ECO:0000313|EMBL:KWT73024.1};
OS   Hyphomicrobium sulfonivorans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Hyphomicrobiaceae; Hyphomicrobium.
OX   NCBI_TaxID=121290 {ECO:0000313|EMBL:KWT73024.1, ECO:0000313|Proteomes:UP000059074};
RN   [1] {ECO:0000313|EMBL:KWT73024.1, ECO:0000313|Proteomes:UP000059074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WDL6 {ECO:0000313|EMBL:KWT73024.1,
RC   ECO:0000313|Proteomes:UP000059074};
RA   Albers P.;
RT   "Transcriptomic analysis of a linuron degrading triple-species bacterial
RT   consortium.";
RL   Submitted (OCT-2015) 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:KWT73024.1}.
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DR   EMBL; LMTR01000002; KWT73024.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A109BQB1; -.
DR   STRING; 121290.APY04_0005; -.
DR   PATRIC; fig|121290.4.peg.3262; -.
DR   OMA; EVPVYFV; -.
DR   OrthoDB; 9778545at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000059074; 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; 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; 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:UP000059074};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          113..171
FT                   /note="Peptidoglycan binding-like"
FT                   /evidence="ECO:0000259|Pfam:PF01471"
FT   DOMAIN          199..367
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
SQ   SEQUENCE   428 AA;  46871 MW;  01A4E6A70A8BEE66 CRC64;
     MPDLREGYVS LKRWAALAAP VLVAGGVLAA SHAGAQEFLR FGPAGEGPSQ ARSGGYDRSF
     IREWQANPPK GYPTLNKANL EPTRKAVARY EQIVATGGFP LVPQVELEPG MTDAAVSVLR
     RRLQRSGDLD AAETNYPEHY GSDLVTAVKR FQASNGLAPT GVVDRRTIAA LNIPSEVRLA
     QLKTNLTRLN DLAGMVRKRY VMVNIPAAQI EAVENNAVAM RYSGVVGKPD RPTPLLRSTI
     TDLAFNPPWT LPPTVIKEDL IPKGRDMQSK GQNVLVKYGI DAYEGGKKLD PEAINWASNR
     PFQLTYRQIA GKENPLGFLK INFANSESVY MHDSPKESLF GRNFRAASSG CVRVQNIGDL
     ATWLLAGQGT ADQVEHLRES GETRTVRLRR PVPLYFAYVT AWATPDGVIQ FRPDLYLKDG
     VGKVAAAY
//
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