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Database: UniProt
Entry: A0A1C4T478_9ACTN
LinkDB: A0A1C4T478_9ACTN
Original site: A0A1C4T478_9ACTN 
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
//
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