ID Q6LPP0_PHOPR Unreviewed; 572 AA.
AC Q6LPP0;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE RecName: Full=Murein L,D-transpeptidase {ECO:0008006|Google:ProtNLM};
GN Name=VP1916 {ECO:0000313|EMBL:CAG20736.1};
GN OrderedLocusNames=PBPRA2351 {ECO:0000313|EMBL:CAG20736.1};
OS Photobacterium profundum (strain SS9).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=298386 {ECO:0000313|EMBL:CAG20736.1, ECO:0000313|Proteomes:UP000000593};
RN [1] {ECO:0000313|Proteomes:UP000000593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1253 / SS9 {ECO:0000313|Proteomes:UP000000593};
RX PubMed=15746425; DOI=10.1126/science.1103341;
RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA Bartlett D.H., Valle G.;
RT "Life at depth: Photobacterium profundum genome sequence and expression
RT analysis.";
RL Science 307:1459-1461(2005).
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; CR378670; CAG20736.1; -; Genomic_DNA.
DR RefSeq; WP_011219024.1; NC_006370.1.
DR AlphaFoldDB; Q6LPP0; -.
DR STRING; 298386.PBPRA2351; -.
DR KEGG; ppr:PBPRA2351; -.
DR eggNOG; COG2989; Bacteria.
DR HOGENOM; CLU_020360_3_0_6; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000593; Chromosome 1.
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; 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; 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:UP000000593};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..572
FT /note="Murein L,D-transpeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004276999"
FT DOMAIN 82..212
FT /note="L,D-transpeptidase scaffold"
FT /evidence="ECO:0000259|Pfam:PF20142"
FT DOMAIN 282..305
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 333..496
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
SQ SEQUENCE 572 AA; 65660 MW; E219A3FB894C5BAC CRC64;
MAMIRQSCIS LLLISIISIS VSANEPLLTP TPSLLSEQNI NTQQQFISEP VVSPETALQQ
QKSLLWVKEV ADDLSSIQYI DKLAQLYASI AYTPIWQDAF AATELEEQLR IVALSRVSSD
LSRRYSQLKH YKLANDWRQY DLLATDTLLA YMSYIENLPK FGRGWLFGTG IDVPLPLPTK
IQTGRLLDAI DNNRMRYFVT SLKPVNDNYN KMILAMQTLE VSESEHWPGF YQQGIIRLGD
RLKDPDSLIT ILERMGDITE YDADRMRTSQ LRSLTIPLSL GVKTFQKRHG LKVDGVIGPK
TRYWLAITPK ERIRVLALNA QRVRLWPAEY NSVLIVNIPG YELNLWLDNK HVFDSKVIVG
RPSRRTPLIS SRVNSVVFNP YWNVPKSIMR KDILPKARRD RSYLYRHNYA VIRSWNSSEQ
IPIHTIHPSM LYAKTFPYRL RQKPGNKNAL GLYKFIIPND NSIYLHDTPA KSLFNKDDRA
FSSGCVRVEN ADVLALILLN YSGVTDQRFY ELSGRKQTKT IGLRNKVKVH LIYQTAWVDD
GGLVNFRDDV YLYDKVGGGS QSDQKYTSAY NH
//