ID A0A1I3P5R2_9RHOB Unreviewed; 548 AA.
AC A0A1I3P5R2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Murein L,D-transpeptidase YcbB/YkuD {ECO:0000313|EMBL:SFJ16888.1};
GN ORFNames=SAMN04488138_102208 {ECO:0000313|EMBL:SFJ16888.1};
OS Celeribacter halophilus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Celeribacter.
OX NCBI_TaxID=576117 {ECO:0000313|EMBL:SFJ16888.1, ECO:0000313|Proteomes:UP000183299};
RN [1] {ECO:0000313|EMBL:SFJ16888.1, ECO:0000313|Proteomes:UP000183299}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.8891 {ECO:0000313|EMBL:SFJ16888.1,
RC ECO:0000313|Proteomes:UP000183299};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FORY01000002; SFJ16888.1; -; Genomic_DNA.
DR RefSeq; WP_066606193.1; NZ_QKZJ01000002.1.
DR AlphaFoldDB; A0A1I3P5R2; -.
DR STRING; 576117.SAMN04488138_102208; -.
DR OrthoDB; 9778545at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000183299; 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; 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:SF2; BLR7131 PROTEIN; 1.
DR PANTHER; PTHR41533; L,D-TRANSPEPTIDASE HI_1667-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 Reference proteome {ECO:0000313|Proteomes:UP000183299};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..44
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 45..548
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010198580"
FT DOMAIN 64..196
FT /note="L,D-transpeptidase scaffold"
FT /evidence="ECO:0000259|Pfam:PF20142"
FT DOMAIN 224..278
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 308..468
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
SQ SEQUENCE 548 AA; 60705 MW; 73BF8A6D4585597F CRC64;
MLFFPVSRLS QPRFAHKSLK AGLLAMSLAL TGAPLVLAPA PVQAQQVSAF MQSVAEAASS
SKVLSEFYRA NGYKPVFTDN SARAKARRQA LLRAVNAAPA KGLAPYDTSL LVANLRAIKS
DRDLGRAEVA MAQLFLDYAR DIQTGQLVPS RIDSGLVRQV PYRDGLAVLT NFTKSNPQAY
LRKLEPSSPE YARLLKEKAN LEQVLGKGGW GQTVPGSKYE PGDSGNGVVI LRNRLMAMGY
LPRSAATTYD AKMQKAVQQF QMDHGLTADG VAGKATLDEV NVGPEKRLAS ILVALERERW
INMPLGERHV WVNLTDFSAK IIDDGRVTFE TRSVIGQNVG DRRSPEFSDE MEHLVINPTW
NVPRSIAVKE YLPMMQKNPN AAGHLRLVDS RGRTVNRANV DFSQYTSRSF PFNLKQPPSN
RNALGLVKFM FPNKYNIYLH DTPSKSLFGR EVRAFSHGCI RLQQPFDFAY ALLAKQTSDP
EGFFQAKLKS GVESVVPLEK HVPVHLIYRT AVSKPKGGME YRRDIYGRDA KIWAALQNKG
VQLRSVGG
//
