ID A0A0U3Q1H7_9ACTN Unreviewed; 400 AA. AC A0A0U3Q1H7; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 27-NOV-2024, entry version 33. DE RecName: Full=L,D-TPase catalytic domain-containing protein {ECO:0000259|PROSITE:PS52029}; GN ORFNames=AS200_16195 {ECO:0000313|EMBL:ALV33405.1}; OS Streptomyces sp. CdTB01. OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces. OX NCBI_TaxID=1725411 {ECO:0000313|EMBL:ALV33405.1, ECO:0000313|Proteomes:UP000068029}; RN [1] {ECO:0000313|EMBL:ALV33405.1, ECO:0000313|Proteomes:UP000068029} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CdTB01 {ECO:0000313|EMBL:ALV33405.1, RC ECO:0000313|Proteomes:UP000068029}; RA Tian Y., Zhou G., Yang H., Lu X.; RT "Complete genome sequence of the Streptomyces sp. strain CdTB01, a RT bacterium tolerant to cadmium."; RL Submitted (DEC-2015) 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; CP013743; ALV33405.1; -; Genomic_DNA. DR RefSeq; WP_058923070.1; NZ_CP013743.1. DR AlphaFoldDB; A0A0U3Q1H7; -. DR STRING; 1725411.AS200_16195; -. DR KEGG; scx:AS200_16195; -. DR OrthoDB; 5242354at2; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000068029; 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 FunFam; 2.40.440.10:FF:000005; L,D-transpeptidase 2; 1. DR FunFam; 2.60.40.3780:FF:000001; L,D-transpeptidase 2; 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. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 4: Predicted; KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315}; KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|PROSITE- KW ProRule:PRU01373}; KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316, KW ECO:0000256|PROSITE-ProRule:PRU01373}; KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, KW ECO:0000256|PROSITE-ProRule:PRU01373}; KW Reference proteome {ECO:0000313|Proteomes:UP000068029}; 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..400 FT /note="L,D-TPase catalytic domain-containing protein" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5039120881" FT DOMAIN 244..373 FT /note="L,D-TPase catalytic" FT /evidence="ECO:0000259|PROSITE:PS52029" FT REGION 35..59 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 324 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01373" FT ACT_SITE 342 FT /note="Nucleophile" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01373" SQ SEQUENCE 400 AA; 43625 MW; 3EC69C4188DDCED9 CRC64; MKDAHRRARR AGAALAAVLT WAGLLAGCTS PPRIDEALGK PPAPEDVIRV SPDDGSKSVR PDQRLVVRVP SGRLESVKVV KAQDAQESEV PGHVSEDGLR WEPDDGRLAL AAKYTVDAVA LDGHGRRSAR HTTFTTFVPD ERFVGYVTPE NRATVGTGMI VSLEFNREID NRAAVQRAIR VTARPAVEIR PHWFGKGRLD FRPEHYWKPG TQVTVDLRLR DVEGAPGVYG IQDRTFSFTV GRSQVSLVDA ARHTMQVRRD GALLATVPIT AGSPKHTTYN GKMVVMEMLE VTRMNSRTVG FGGEYDIPDV PHAMRLTDSG TFVHGNYWAP DAPGRVNVSH GCVGLRDVKG GGSGTPAGWF FDRSLIGDVI EVVHSNDKKV APDNGLGGWN MGWKEWKAGS //