ID A0A6H0D074_9ACTN Unreviewed; 386 AA. AC A0A6H0D074; DT 12-AUG-2020, integrated into UniProtKB/TrEMBL. DT 12-AUG-2020, sequence version 1. DT 24-JUL-2024, entry version 15. DE SubName: Full=L,D-transpeptidase {ECO:0000313|EMBL:QIS75873.1}; GN ORFNames=HB370_17650 {ECO:0000313|EMBL:QIS75873.1}; OS Streptomyces sp. DSM 40868. OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=2721173 {ECO:0000313|EMBL:QIS75873.1, ECO:0000313|Proteomes:UP000501663}; RN [1] {ECO:0000313|EMBL:QIS75873.1, ECO:0000313|Proteomes:UP000501663} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 40868 {ECO:0000313|EMBL:QIS75873.1, RC ECO:0000313|Proteomes:UP000501663}; RA David M., Lejeune C., Abreu S., Thibessard A., Leblond P., Chaminade P., RA Virolle M.-J.; RT "Is there a link between lipid content and antibiotic production in RT Streptomyces?"; RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000256|ARBA:ARBA00004752, ECO:0000256|PROSITE-ProRule:PRU01373}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP050504; QIS75873.1; -; Genomic_DNA. DR AlphaFoldDB; A0A6H0D074; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000501663; Chromosome. DR GO; GO:0005576; C:extracellular region; IEA:TreeGrafter. DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0071972; F:peptidoglycan L,D-transpeptidase activity; IEA:TreeGrafter. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-UniRule. DR GO; GO:0018104; P:peptidoglycan-protein cross-linking; IEA:TreeGrafter. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-UniRule. DR CDD; cd13432; LDT_IgD_like_2; 1. 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; IPR050979; LD-transpeptidase. 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; PS52029; LD_TPASE; 1. PE 4: Predicted; KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315}; KW Cell shape {ECO:0000256|PROSITE-ProRule:PRU01373}; KW Cell wall biogenesis/degradation {ECO:0000256|PROSITE-ProRule:PRU01373}; KW Peptidoglycan synthesis {ECO:0000256|PROSITE-ProRule:PRU01373}; KW Reference proteome {ECO:0000313|Proteomes:UP000501663}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 225..357 FT /note="L,D-TPase catalytic" FT /evidence="ECO:0000259|PROSITE:PS52029" FT ACT_SITE 305 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01373" FT ACT_SITE 326 FT /note="Nucleophile" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01373" SQ SEQUENCE 386 AA; 40408 MW; 169AAD85FE1D854F CRC64; MVGALTLTAC GGDASAKNDG KGGDAPKTSA AKIAISAKDG STGASINATG VKVSDGKLTE VKMTVAGSGQ AVPGAISADG HTWKPERRLE RGTKYEINAT AKDSEGRTAA ANAIFTTVSP ANSFIGTYTP DDGATVGVGM PVSFTFDKSI TDKKAVQSHI TVNTSSGQQV VGHWFGDRRL DFRPQEYWKA GSKVTMNIDL DGVQGAQGVY GVQKKSVSFT VGRSQVSTVD VNTQTMTVVR DGQTIKSVPI SAGSPEHTTY NGQMVISEKF TQTRMNGSTV GFGGEYDIPD VPHAMRLTTS GTFIHGNYWY NKGNPPFGRT GTSHGCVGLA DVQGAQGATS AKWFYDNTLI GDVVIVKNSP DTTVAPDNGL NGWNMQWSAW TAGSAV //