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Database: UniProt
Entry: A0A372M0X5_9ACTN
LinkDB: A0A372M0X5_9ACTN
Original site: A0A372M0X5_9ACTN 
ID   A0A372M0X5_9ACTN        Unreviewed;       464 AA.
AC   A0A372M0X5;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=L,D-transpeptidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DY218_24305 {ECO:0000313|EMBL:RFU84175.1};
OS   Streptomyces triticagri.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2293568 {ECO:0000313|EMBL:RFU84175.1, ECO:0000313|Proteomes:UP000263094};
RN   [1] {ECO:0000313|EMBL:RFU84175.1, ECO:0000313|Proteomes:UP000263094}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEAU-YY421 {ECO:0000313|EMBL:RFU84175.1,
RC   ECO:0000313|Proteomes:UP000263094};
RA   Han C.;
RT   "Isolation, diversity and antifungal activity of Actinobacteria from
RT   wheat.";
RL   Submitted (AUG-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:RFU84175.1}.
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DR   EMBL; QUAK01000124; RFU84175.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A372M0X5; -.
DR   OrthoDB; 5242354at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000263094; 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.
PE   4: Predicted;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
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..464
FT                   /note="L,D-transpeptidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016943691"
FT   DOMAIN          113..266
FT                   /note="Bacterial Ig"
FT                   /evidence="ECO:0000259|Pfam:PF17964"
FT   DOMAIN          290..412
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
FT   REGION          34..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          445..464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   464 AA;  48296 MW;  E0FE7B0E7C062DF1 CRC64;
     MTSPATKSVG AFGALAGVLL IAAAGQCADD RATDAEGRSR TAPLATVSTA GAEDVTSPGA
     GCGGAGPGGL CLTGSTVPKR WQAPVGDGRG VVGRPAGSDG LLQVSAGRDD HRIVDVDVFF
     GVGHARGVDG RLASNGRVWR STVPLGAGRQ YALRVTTEDG SGRTARGSLA FRTAAPARGS
     ARLTPRFGPG PGSYGVGQPI VAELSRPVPA DDRAARAAVE RGLRVDARPR VEGAWHWVDS
     RTLHYRPRTY WPAHSRITVR SALEGTRIAD GVYGGPAEPL TLTIGARVEA VTDAATHTMT
     VLRDGEPVRE IPVTTGKAGF RTRGGIKVVL GKESAVRMRG ESIGIARGSG DYFDLPVRYA
     TRVTWSGEYV HAAPWSAGSH GVANVSHGCV GMSTADAAWF FDAVREGDIV EVVNSGGERM
     TPFDNGYGDW NVSWRSWRKG SALAAVGGQD GGARPDEGRL RPMA
//
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