ID   K4KPV9_SIMAS            Unreviewed;       540 AA.
AC   K4KPV9;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=Peptidoglycan binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   OrderedLocusNames=M5M_15045 {ECO:0000313|EMBL:AFV00144.1};
OS   Simiduia agarivorans (strain DSM 21679 / JCM 13881 / BCRC 17597 / SA1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Simiduia.
OX   NCBI_TaxID=1117647 {ECO:0000313|EMBL:AFV00144.1, ECO:0000313|Proteomes:UP000000466};
RN   [1] {ECO:0000313|EMBL:AFV00144.1, ECO:0000313|Proteomes:UP000000466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21679 / JCM 13881 / BCRC 17597 / SA1
RC   {ECO:0000313|Proteomes:UP000000466};
RX   PubMed=23405302; DOI=10.1128/genomeA.00039-12;
RA   Lin S.Y., Shieh W.Y., Chen J.S., Tang S.L.;
RT   "Complete genome sequence of Simiduia agarivorans SA1(T), a marine
RT   bacterium able to degrade a variety of polysaccharides.";
RL   Genome Announc. 1:E00039-E00039(2013).
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; CP003746; AFV00144.1; -; Genomic_DNA.
DR   RefSeq; WP_015048296.1; NZ_ATUQ01000010.1.
DR   AlphaFoldDB; K4KPV9; -.
DR   STRING; 1117647.M5M_15045; -.
DR   KEGG; saga:M5M_15045; -.
DR   eggNOG; COG2989; Bacteria.
DR   HOGENOM; CLU_020360_3_4_6; -.
DR   OrthoDB; 9778545at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000466; Chromosome.
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:UP000000466};
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..540
FT                   /note="Peptidoglycan binding domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003878582"
FT   DOMAIN          50..186
FT                   /note="L,D-transpeptidase scaffold"
FT                   /evidence="ECO:0000259|Pfam:PF20142"
FT   DOMAIN          217..269
FT                   /note="Peptidoglycan binding-like"
FT                   /evidence="ECO:0000259|Pfam:PF01471"
FT   DOMAIN          297..463
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
SQ   SEQUENCE   540 AA;  60918 MW;  42D4313FF689518B CRC64;
     MIRLIKQLLL LSALFCSHVS AAESLRQQVE SWHAGFAAEA GGAMLHLPQD TARFYELSGF
     QYRWSVNSAG VLALSDEANA LFDFLGNIHL EGLLAVDYHY PALQAALARQ DWLAFDLLMT
     DAHLMLAHHL LKGKVDVASL NADWVANPRT RDLVQHLLPN GGDPVVEKLT ALRPSQARYD
     RLLSRLAWLT EHPASEWPAL AVSPKIEPGA SDARLASIAQ RLRYWGDLSD EDRLFNQYAS
     ELVDAVKRFQ MRHGLKQDGV IGKATLTQLN VTPAERARQL VANLERWRWL GEDFGHRFLL
     VNIADFSLTV YEAGQPAVRM PVIVGRHYRK TPVFSDRMRY LVFNPTWTVP VKLAVQDKLP
     DIQKDPDYLS RMGFKVYPHG SQVEVDPGTI DWATLTPRNF PYRLVQMPGP LNALGQVKFM
     FPNRYDVYLH DTPARELFQE EDRAFSSGCI RVADPMALAE YLLADQGIDR ATIDQWLAEG
     AIKTVNLKTA MPIHIEYWTA WVDREGTLHF RKDVYNRDAP LIAALAQPLT GQVPVQDTPG
//