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Database: UniProt
Entry: A0A2M9K0C9_9ACTN
LinkDB: A0A2M9K0C9_9ACTN
Original site: A0A2M9K0C9_9ACTN 
ID   A0A2M9K0C9_9ACTN        Unreviewed;       419 AA.
AC   A0A2M9K0C9;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=L,D-transpeptidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CG723_05895 {ECO:0000313|EMBL:PJN12564.1};
OS   Streptomyces sp. CB01635.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2020326 {ECO:0000313|EMBL:PJN12564.1, ECO:0000313|Proteomes:UP000232157};
RN   [1] {ECO:0000313|Proteomes:UP000232157}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CB01635 {ECO:0000313|Proteomes:UP000232157};
RA   Pan G., Xu Z., Guo Z., Ma M., Yang D., Zhou H., Gansemans Y., Zhu X.,
RA   Zhao L.-X., Jiang Y., Cheng J., van Nieuwerburgh F., Suh J.W., Duan Y.,
RA   Shen B.;
RT   "Discovery of the Leinamycin Family of Natural Products by Mining
RT   Actinobacterial Genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 114:0-0(2017).
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:PJN12564.1}.
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DR   EMBL; NNBL01000002; PJN12564.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2M9K0C9; -.
DR   OrthoDB; 5242354at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000232157; 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:UP000232157};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..419
FT                   /note="L,D-transpeptidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038708553"
FT   DOMAIN          54..221
FT                   /note="Bacterial Ig"
FT                   /evidence="ECO:0000259|Pfam:PF17964"
FT   DOMAIN          246..367
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
SQ   SEQUENCE   419 AA;  44644 MW;  D6EB34F1643218A9 CRC64;
     MNNSPRIRMV MGCTLLVTAL GASVTGCSGS SHPLSAKPYD AAGEIGFSGE SGSKKADPDK
     PIEITSEGDE ARITDVTATD EIGRYVVGEL SADGSRWHST APLAADAHYT VHVSTEDDEG
     APGRKVLTFD TGHPDKKKSL KVTFGPEAGK YGVGQPVTAE LSAAVKDKAA RAVVERALKV
     DSEPAVAGSW TWVDDKTLHF RPEEYWPAGA TVEAHSTLDG IKIGDRLWGG ASKPLRLTIG
     DRIEAVTDAG SHQMTVYRNG RVINTIPVTT GKPGFETRNG VKVVLGKERF VRMRSTSIGI
     AEGSSESYDM PVYFATRVTW SGEYVHAAPW SQGSQGYANV SHGCTGMSMS NAEWFFNTVR
     TGDVVKVINS NGAQMDPFGN GFGDWNLSWK NWEKGSAVQA VAGDGGRSTV QAARLSPEV
//
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