ID A0A1Q5JGD4_9ACTN Unreviewed; 290 AA.
AC A0A1Q5JGD4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Peptidoglycan-binding protein {ECO:0000313|EMBL:OKJ68386.1};
GN ORFNames=AMK29_07960 {ECO:0000313|EMBL:OKJ68386.1};
OS Streptomyces sp. CB02261.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703940 {ECO:0000313|EMBL:OKJ68386.1, ECO:0000313|Proteomes:UP000186742};
RN [1] {ECO:0000313|EMBL:OKJ68386.1, ECO:0000313|Proteomes:UP000186742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB02261 {ECO:0000313|EMBL:OKJ68386.1,
RC ECO:0000313|Proteomes:UP000186742};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKJ68386.1}.
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DR EMBL; LIVX01000002; OKJ68386.1; -; Genomic_DNA.
DR RefSeq; WP_073810704.1; NZ_LIVX01000002.1.
DR AlphaFoldDB; A0A1Q5JGD4; -.
DR OrthoDB; 8887048at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000186742; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..290
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012321254"
FT DOMAIN 91..146
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 177..288
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
FT REGION 28..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 290 AA; 30812 MW; 39BCB35622E8826D CRC64;
MMRSSSVIRR AVLAAASVAL ATGCTAQAAG AGGGSGTATP TKASTTAAPT ATTTPTGDGT
PTDDGKAPSP SATTATGEPG SEVMMGDGDE SEQVRELQAR LRQLGHFDRA PTGFYGTMTA
GSVKAFQRKW DLPRTGSVDG ATWRKLLGTS RKPTADELKP ATTNALDTPD PRCMTGRVLC
ISKESRTLAW MIDGKVVSAM DVRFGSENTP TREGTFAVER KVRQDWSKLY HTPMPLSMYF
SRGQAVHYSS DFAARGYNGG SHGCVNVRDR AKLTTLFDQV KVGDKVVVHW
//
