ID A0A2Z4VB30_9ACTN Unreviewed; 423 AA.
AC A0A2Z4VB30;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=L,D-transpeptidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=DRB96_27855 {ECO:0000313|EMBL:AWZ18277.1};
OS Streptomyces sp. ICC1.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2099583 {ECO:0000313|EMBL:AWZ18277.1, ECO:0000313|Proteomes:UP000250268};
RN [1] {ECO:0000313|EMBL:AWZ18277.1, ECO:0000313|Proteomes:UP000250268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICC1 {ECO:0000313|EMBL:AWZ18277.1,
RC ECO:0000313|Proteomes:UP000250268};
RA Gosse J.;
RT "Whole genome sequencing and metabolomic study of cave Streptomyces
RT isolates ICC1 and ICC4.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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DR EMBL; CP030287; AWZ18277.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z4VB30; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000250268; Chromosome.
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.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Reference proteome {ECO:0000313|Proteomes:UP000250268};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 53..215
FT /note="Bacterial Ig"
FT /evidence="ECO:0000259|Pfam:PF17964"
FT DOMAIN 239..360
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
FT REGION 400..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 423 AA; 44630 MW; 952C751885B40426 CRC64;
MEALRAELCG GLEQRLVRAT ARGAGSVVRD PSSGGAARAA APTVVLPTDA ASPLEITLAG
PGLLTYVTVH DGHGRYVGGA LGARGHRWAN TEPLRAGETY TVRVGAQDAA GTPVGVTMAF
RTAPATEDGR LTVEFGPKPG VYGAGQIVTA SLSHPVPAAD PAARARLERA LQVTSEPAVE
GAWHWVDDST LHYRPRSYWP AHTVVSVLSG LDGVEVADRE FGGASEPLRF TIGERIEAVT
DAAAHEMTVR RNGTVLRTIP VTTGKAGFLT RSGVKVVLGK EYKVRMRGDT VGIKRGTSEF
YDLPVFYATR VTWSGEYVHA APWSVEAQGE ENVSHGCTGM STADAAWFFN TVREGDVVSV
VNSGGERMTP FDNGFGDWNL DWAAWRAGSA LSAASAESPL APASPYASDR ASAHGPSRLR
PLT
//