ID A0A429S9D0_9ACTN Unreviewed; 417 AA.
AC A0A429S9D0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=L,D-transpeptidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=EF918_03650 {ECO:0000313|EMBL:RSS83452.1};
OS Streptomyces sp. WAC06614.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2487416 {ECO:0000313|EMBL:RSS83452.1, ECO:0000313|Proteomes:UP000277644};
RN [1] {ECO:0000313|EMBL:RSS83452.1, ECO:0000313|Proteomes:UP000277644}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WAC06614 {ECO:0000313|EMBL:RSS83452.1,
RC ECO:0000313|Proteomes:UP000277644};
RA Culp E., Yim G., Waglechner N., Wang W., Pawlowski A.C., Wright G.D.;
RT "Unmasking the antibiotic production potential of Actinomycetes through
RT CRISPR/Cas9 inactivate of ubiquitous gene clusters.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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:RSS83452.1}.
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DR EMBL; RPRY01000014; RSS83452.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A429S9D0; -.
DR OrthoDB; 5242354at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000277644; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd16913; YkuD_like; 1.
DR Gene3D; 2.60.40.3710; -; 1.
DR Gene3D; 2.60.40.3780; -; 1.
DR Gene3D; 2.40.440.10; L,D-transpeptidase catalytic domain-like; 1.
DR InterPro; IPR041280; Big_10.
DR InterPro; IPR005490; LD_TPept_cat_dom.
DR InterPro; IPR038063; Transpep_catalytic_dom.
DR PANTHER; PTHR30582; L,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30582:SF35; L,D-TRANSPEPTIDASE 2; 1.
DR Pfam; PF17964; Big_10; 1.
DR Pfam; PF03734; YkuD; 1.
DR SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Reference proteome {ECO:0000313|Proteomes:UP000277644};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..417
FT /note="L,D-transpeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019527967"
FT DOMAIN 56..222
FT /note="Bacterial Ig"
FT /evidence="ECO:0000259|Pfam:PF17964"
FT DOMAIN 245..366
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
SQ SEQUENCE 417 AA; 45193 MW; 7C442475B2C97530 CRC64;
MKHTPRLWTV LSCAMLVASL GAGATACGSG DHPLSARPYD AADQVAFNQA AGSRPVDPDR
PLEVSVKGTG TGTRITDVTA VDTHGRRLAG ELSARGDRWH STAPLAAGVR YTVTVSTENE
RGAPGQRTLT FETAPAHKVL NVEFGPDAGK YGVGQPLTAE LNEPVHDKAA RAVVERALVV
DAKPNPVEGS WYWVDDTRLH FRPKDYWPAH STVSVRSNLE GIRVGDHLYG AAAKPLTLEI
GDRVEVITDA SAHYLTFKRN GEVINTIPVT TGKPGFSTRN GVKVVLGKQY YVQMRGDTVG
IGGSEYYNLP VYYATRVTWS GEYVHAAPWS IDSHGYANVS HGCTGMSTGN AAWFYENITE
GDLVTVINSI GEEMDPFGNG YGDWNLDWKD WREGSALLKG TQEGRSPVDV TRLRPQI
//
