ID A0A0G3UMB9_9ACTN Unreviewed; 304 AA.
AC A0A0G3UMB9;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Peptidoglycan-binding protein {ECO:0000313|EMBL:AKL67532.1};
GN ORFNames=M444_21405 {ECO:0000313|EMBL:AKL67532.1};
OS Streptomyces sp. Mg1.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=465541 {ECO:0000313|EMBL:AKL67532.1, ECO:0000313|Proteomes:UP000035653};
RN [1] {ECO:0000313|EMBL:AKL67532.1, ECO:0000313|Proteomes:UP000035653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mg1 {ECO:0000313|EMBL:AKL67532.1,
RC ECO:0000313|Proteomes:UP000035653};
RX PubMed=23908282;
RA Hoefler B.C., Konganti K., Straight P.D.;
RT "De Novo Assembly of the Streptomyces sp. Strain Mg1 Genome Using PacBio
RT Single-Molecule Sequencing.";
RL Genome Announc. 1:e00535-13(2013).
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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DR EMBL; CP011664; AKL67532.1; -; Genomic_DNA.
DR RefSeq; WP_047960669.1; NZ_DS570418.1.
DR AlphaFoldDB; A0A0G3UMB9; -.
DR KEGG; strm:M444_21405; -.
DR PATRIC; fig|465541.12.peg.4546; -.
DR OrthoDB; 8887048at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000035653; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000035653};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..304
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038747809"
FT DOMAIN 105..160
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 191..302
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
FT REGION 26..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 304 AA; 31877 MW; A126DEFA37AE8D79 CRC64;
MHRQRVMART LGLATAVALA ATACGSQKTE NTGSASTAPS ASAAVTTPES SPSSDDKPAG
DPSASPSASA SASASSASPS PSASASSSPS ASPSVKAVMA NGDDSEQVRE LQARLKQLKL
MSVAPTGFYG SKTTTAVKSF QSRNGLTASG SVDAETWKKI QGLTKKPTAD ELRPPTVNEV
DAPDPRCMTG RVMCISKESR TLAWMIDGKV ISTMDVRFGS ENTPTREGVF DVGWKAKEWT
STIYHTPMPY AMFFSGGQAV HYSADFAARG YSGASHGCVN VRDKAKLSKL FDDVKVGDKV
VVYW
//
