ID A0A0U3Q1H7_9ACTN Unreviewed; 400 AA. AC A0A0U3Q1H7; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 13-SEP-2023, entry version 26. DE RecName: Full=Lipoprotein {ECO:0008006|Google:ProtNLM}; 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}. 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 EnsemblBacteria; ALV33405; ALV33405; AS200_16195. DR KEGG; scx:AS200_16195; -. DR OrthoDB; 5242354at2; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000068029; Chromosome. DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway. 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; IPR005490; LD_TPept_cat_dom. DR InterPro; IPR038063; Transpep_catalytic_dom. DR PANTHER; PTHR30582; L,D-TRANSPEPTIDASE; 1. DR PANTHER; PTHR30582:SF2; L,D-TRANSPEPTIDASE YCIB-RELATED; 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: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="Lipoprotein" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5039120881" FT DOMAIN 57..241 FT /note="Bacterial Ig" FT /evidence="ECO:0000259|Pfam:PF17964" FT DOMAIN 244..348 FT /note="YkuD" FT /evidence="ECO:0000259|Pfam:PF03734" FT REGION 35..59 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" 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 //