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Database: UniProt
Entry: A0A3N1ANW7_9ACTN
LinkDB: A0A3N1ANW7_9ACTN
Original site: A0A3N1ANW7_9ACTN 
ID   A0A3N1ANW7_9ACTN        Unreviewed;       426 AA.
AC   A0A3N1ANW7;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=L,D-transpeptidase-like protein {ECO:0000313|EMBL:ROO58360.1};
GN   ORFNames=EDC02_0109 {ECO:0000313|EMBL:ROO58360.1};
OS   Micromonospora sp. Llam0.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=2485143 {ECO:0000313|EMBL:ROO58360.1, ECO:0000313|Proteomes:UP000275308};
RN   [1] {ECO:0000313|EMBL:ROO58360.1, ECO:0000313|Proteomes:UP000275308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Llam0 {ECO:0000313|EMBL:ROO58360.1,
RC   ECO:0000313|Proteomes:UP000275308};
RA   D'Agostino P.;
RT   "Genome mining of underrepresented organisms for secondary metabolites.";
RL   Submitted (NOV-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:ROO58360.1}.
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DR   EMBL; RJJY01000001; ROO58360.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N1ANW7; -.
DR   OrthoDB; 5242354at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000275308; 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:UP000275308};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..426
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018307164"
FT   DOMAIN          61..226
FT                   /note="Bacterial Ig"
FT                   /evidence="ECO:0000259|Pfam:PF17964"
FT   DOMAIN          249..369
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
FT   REGION          404..426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   426 AA;  45303 MW;  71B86138001DB77B CRC64;
     MHKVRRGWSV AVTLAVIAPA ALAGCGSDKT PRFVDGQVAT ASPTPSPEPF EFAIAPKADA
     KNLPISTEIG TTVSGGEVTS VTLVEDGGGE VSGSMRHDGT AWVPDKPLKN QKQYTATVVA
     TSSTGEEETK TTSFSTMGKS GSQTGTGLYL FDGRTYGVAM PVVVEFFPGI PEQERASVQK
     RMFVKTDPPQ PGTWYWVANG TQAFYRAPDF WQAGTTVTTR IALDGHPTGD GRYGDMDRGA
     TAKIGDKVTV EVDNATKQLS MFKNDELVKQ MPVSLGKPST PSSSGTMVVM DKQEQTVFDT
     FAELGPEEGY RTDISFAQRI TWGGEFIHAA PWSVGDQGVR NVSHGCVNLS MDNAKWLFNQ
     TKVGDPITVK GTERELADGN GWTAWNLTWD EFVKGSALPV PADLQPAGAA SPAPTTPAPV
     PTATSG
//
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