ID A0A1Y5REM9_9RHOB Unreviewed; 528 AA.
AC A0A1Y5REM9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Murein L,D-transpeptidase {ECO:0000313|EMBL:SLN15765.1};
GN ORFNames=ROA7023_00225 {ECO:0000313|EMBL:SLN15765.1};
OS Roseisalinus antarcticus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseisalinus.
OX NCBI_TaxID=254357 {ECO:0000313|EMBL:SLN15765.1, ECO:0000313|Proteomes:UP000193900};
RN [1] {ECO:0000313|EMBL:SLN15765.1, ECO:0000313|Proteomes:UP000193900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7023 {ECO:0000313|EMBL:SLN15765.1,
RC ECO:0000313|Proteomes:UP000193900};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FWFZ01000001; SLN15765.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5REM9; -.
DR OrthoDB; 9778545at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000193900; 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:UP000193900};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..528
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012147595"
FT DOMAIN 57..192
FT /note="L,D-transpeptidase scaffold"
FT /evidence="ECO:0000259|Pfam:PF20142"
FT DOMAIN 218..274
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 302..449
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
SQ SEQUENCE 528 AA; 58788 MW; 5AB1AA198CAE89E6 CRC64;
MKFAKTSARR SLIATLTAAG LLFAAAAPPA FSQGVETQIR VTAFAQAVAE AAARDDDLAA
FYRARAFEGI WTGTDSDAVM RRNAFISALD QAAQHGLPAI RFNTRAAISL LQGASTPAEK
GRAEVEMSRL LLDYARTLNS GLLQPRQVVS HIRREVHLRD RGEMLDAFMD NPNAMLRGLA
PSTPEYQRLM QAKMRLESLL PRGGFGPAVQ STIRPGDQGA QVVALRNRLM AMDLLGHTVS
GRYDTKMQEA VRSFQESMGL EQDAIVGGAT LTALNVDARD RLESVLVAME RERWFNNLDR
GDRYVWVNLV DFTAAIMDHD RETFRTKSVI GAQAGDRQTV EFSDTMEYME INPYWYVPRS
IINGEYGGRV PAGFEAVDYR GRIVQTSSAQ NVSVRQRPGP RNALGSVKFM FPNQYNIYLH
DTPSQSLFSR TVRTFSHGCI RLDDPHEFAY ALLAAQMDDP EPYFQRILRS GANTRVPLET
PLPVHLIYRT AFTSVDGRVH YRNDVYNRDA RIWNALAAEG VVIGDVSG
//
