ID A0A1C4T478_9ACTN Unreviewed; 305 AA.
AC A0A1C4T478;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Putative peptidoglycan binding domain-containing protein {ECO:0000313|EMBL:SCE54290.1};
GN ORFNames=GA0115234_110944 {ECO:0000313|EMBL:SCE54290.1};
OS Streptomyces sp. DvalAA-43.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1839762 {ECO:0000313|EMBL:SCE54290.1, ECO:0000313|Proteomes:UP000199186};
RN [1] {ECO:0000313|EMBL:SCE54290.1, ECO:0000313|Proteomes:UP000199186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DvalAA-43 {ECO:0000313|EMBL:SCE54290.1,
RC ECO:0000313|Proteomes:UP000199186};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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; FMBW01000077; SCE54290.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C4T478; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000199186; 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:SF33; EXPORTED PROTEIN-RELATED; 1.
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 Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..305
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038448256"
FT DOMAIN 107..161
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 192..303
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
FT REGION 38..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..92
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 305 AA; 32415 MW; 9FA3B0E575B03A42 CRC64;
MMDSTTRSTS RTAIRGRAGT AAVLAVLAVA TAAGCEAQVT GSAPAAPAAP PRATATDDDK
PAAQPPSPSP AVPSPRATAP SPEAPTSPTP EPDPQGTTLM ASGSESGQVR ELQARLRQIG
HFDRSPTGYY GSVTVAAVRS FQDKRGLSRT GRTDTLTWRK LLGMTHEPTA AELNPPTTRQ
VAKPDKRCMT GRVLCISKNS RTLSWMIDGR VVSAMDVRFG SQYTPTREGT FSVYWKSRHH
VSTIYHTAMP YAMFFSGGQA VHYSADFAAR GYNGASHGCV NVRDEGKIAS LFAQVKNGDK
VVVYG
//