ID A0A1H0KW34_9MICO Unreviewed; 296 AA.
AC A0A1H0KW34;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=L,D-transpeptidase catalytic domain {ECO:0000313|EMBL:SDO59996.1};
GN ORFNames=SAMN04489867_0121 {ECO:0000313|EMBL:SDO59996.1};
OS Pedococcus dokdonensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Pedococcus.
OX NCBI_TaxID=443156 {ECO:0000313|EMBL:SDO59996.1, ECO:0000313|Proteomes:UP000199077};
RN [1] {ECO:0000313|Proteomes:UP000199077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22329 {ECO:0000313|Proteomes:UP000199077};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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DR EMBL; LT629711; SDO59996.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0KW34; -.
DR STRING; 443156.SAMN04489867_0121; -.
DR OrthoDB; 9810670at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000199077; Chromosome i.
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; PTHR30582; L,D-TRANSPEPTIDASE; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 108..164
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 178..295
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
FT REGION 32..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 296 AA; 30120 MW; 61350AC148EADBC2 CRC64;
MDRRRTGARS ALAATVLVGA LALSGCGGIT FGKNTSGTPS AGGATSTTDP ATPTDPGTST
PEPTTPTTTT PAPTTTTVTP QPTSKPTPTK PKPKPTPVEG DTLHSGDRGP YVKQVQQQLS
ALGYWNGAAD GVYGGLTSQA VMALQKAAGL GRDGVFGPAT AKALRNGVRP QSRIGGTGIE
IDKARQVLLV VRGGKVTMIL NTSTGSGQQY TSGGATHTAL TPAGTYSTFR SVDHLDKGPL
GDLWRPRYFN GGIAVHGAGS VPGFPASHGC ARVSNPAMDM IWANGIMPIG GRVVVY
//