ID A0A0Q6FGP3_9ACTN Unreviewed; 324 AA.
AC A0A0Q6FGP3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Peptidoglycan-binding protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ASG49_01225 {ECO:0000313|EMBL:KQT93650.1};
OS Marmoricola sp. Leaf446.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Marmoricola.
OX NCBI_TaxID=1736379 {ECO:0000313|EMBL:KQT93650.1, ECO:0000313|Proteomes:UP000051542};
RN [1] {ECO:0000313|EMBL:KQT93650.1, ECO:0000313|Proteomes:UP000051542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf446 {ECO:0000313|EMBL:KQT93650.1,
RC ECO:0000313|Proteomes:UP000051542};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQT93650.1, ECO:0000313|Proteomes:UP000051542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf446 {ECO:0000313|EMBL:KQT93650.1,
RC ECO:0000313|Proteomes:UP000051542};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQT93650.1}.
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DR EMBL; LMRF01000001; KQT93650.1; -; Genomic_DNA.
DR RefSeq; WP_056536037.1; NZ_LMRF01000001.1.
DR AlphaFoldDB; A0A0Q6FGP3; -.
DR STRING; 1736379.ASG49_01225; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000051542; Unassembled WGS sequence.
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 PANTHER; PTHR30582:SF2; SLL0670 PROTEIN; 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.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000051542};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 121..176
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 210..321
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
FT REGION 40..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..79
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 324 AA; 34175 MW; C4B1FD86DC3F7027 CRC64;
MSGGSRGRRG RARAGVAGLA MLLAVVGVTT AAGWAVTRGG LLDRPGADVA SPAAAEPTTA
PTTPSPPTSP APPSANASPP ASPAASASGR RVLGARAPLP EERPRQVPRP GPRLLGPGDA
GPEVRELQSR LRQVAWFVGD VTDDYGTATE TAVRGFQAKR GIAVTGYVDQ RTRGRLAAMT
REPTRDELAN RFPGDGDTSA ALDPRCRTGR ALCVDKTSRT LRWVVDGTVL RSVSVRFGSS
YTPTREGQFA VERKSRDHVS SLYDSPMPFA MFFSGGQAVH YSADFAARGY AGASHGCVNV
RDLPGITWLY DQVSVGDKVV VYWS
//
