ID A0A0G3V305_9ACTN Unreviewed; 320 AA.
AC A0A0G3V305;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Peptidoglycan-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
DE Flags: Precursor;
GN ORFNames=IMCC26256_111514 {ECO:0000313|EMBL:AKL73790.1};
OS Actinobacteria bacterium IMCC26256.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1650658 {ECO:0000313|EMBL:AKL73790.1, ECO:0000313|Proteomes:UP000035517};
RN [1] {ECO:0000313|EMBL:AKL73790.1, ECO:0000313|Proteomes:UP000035517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC26256 {ECO:0000313|EMBL:AKL73790.1,
RC ECO:0000313|Proteomes:UP000035517};
RA Kim S.;
RT "Genome sequencing of freshwater Actinobacteria.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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DR EMBL; CP011489; AKL73790.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G3V305; -.
DR STRING; 1650658.IMCC26256_111514; -.
DR KEGG; abai:IMCC26256_111514; -.
DR PATRIC; fig|1650658.3.peg.1505; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000035517; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000035517};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..320
FT /note="Peptidoglycan-binding domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038639226"
FT DOMAIN 71..127
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 143..259
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
FT REGION 26..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 320 AA; 32955 MW; 1BDEFC1A2123839E CRC64;
MRPNRLIVFL AVVPLLGIAC SSNASRQGSL VTPTTRERRT TTTTEATTTT TTIPVTTTTK
APLLGLGQGS SGTAVLALQQ RLVALHYDLP EANGNFGAAT QQAVYAFQKV NGMARSGRAT
DDVLARLATA EIPTTMVPAA GGTHVEVDVA RQILFYVQGG VVGKVVAVST GSGNRFCNKG
RCDVAVTPGG AFRVRGKVRG WQVGELGRLY SPSYFNGNIA VHGSLSIPPT PASHGCVRVP
MTSADWLFAA MPNGMAVYVL NGPNVPPPFA DEAPTTTSQA PSTTTTTPSG SSSTSTSSSS
TTTSTTEPAT TSTTGIPAPL
//
