ID L7F961_9ACTN Unreviewed; 420 AA.
AC L7F961;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=ErfK/YbiS/YcfS/YnhG {ECO:0000313|EMBL:ELP67220.1};
GN ORFNames=STRTUCAR8_03042 {ECO:0000313|EMBL:ELP67220.1};
OS Streptomyces turgidiscabies Car8.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=698760 {ECO:0000313|EMBL:ELP67220.1, ECO:0000313|Proteomes:UP000010931};
RN [1] {ECO:0000313|EMBL:ELP67220.1, ECO:0000313|Proteomes:UP000010931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Car8 {ECO:0000313|EMBL:ELP67220.1,
RC ECO:0000313|Proteomes:UP000010931};
RX PubMed=21087627; DOI=10.1016/j.plasmid.2010.11.002;
RA Huguet-Tapia J.C., Badger J.H., Loria R., Pettis G.S.;
RT "Streptomyces turgidiscabies Car8 contains a modular pathogenicity island
RT that shares virulence genes with other actinobacterial plant pathogens.";
RL Plasmid 65:118-124(2011).
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:ELP67220.1}.
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DR EMBL; AEJB01000299; ELP67220.1; -; Genomic_DNA.
DR RefSeq; WP_006377659.1; NZ_AEJB01000299.1.
DR AlphaFoldDB; L7F961; -.
DR STRING; 85558.T45_03916; -.
DR PATRIC; fig|698760.3.peg.4042; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000010931; 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:UP000010931};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..420
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003973308"
FT DOMAIN 56..222
FT /note="Bacterial Ig"
FT /evidence="ECO:0000259|Pfam:PF17964"
FT DOMAIN 245..368
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
FT REGION 45..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 420 AA; 45098 MW; 92BA373E997EE427 CRC64;
MRHSPRNRTV VSCTLLVAAL GASAAACGSD GHPLSAEPYD AADQISFGGS VGDGKKADPD
KPLEVTSDDS DDRITDVTAV DAAGRYVAGE LSADGSRWHS TSPLAAGARY TVRVSTEDED
GAPGRETRTF DTSRPTTKKR LNVTFGPKTG TYGVGQPVTA QLSEPVRGKA QRAIVERALK
VDSTPTTEGA WHWVDDKELH YRPKEYWPAK ATVQVRSNLP GLKIADRLWG GTAKPLKFTT
GDRVIAVTDA SSHEMTVYKN DKVINTIPVT TGKPGFDTRN GVKVVLGKEY FVRMRGTSIG
IAEGSADSYD LPVYYATRVT WSGEYVHAAP WSEGSQGSAN VSHGCTGMST SNAEWFYDNV
REGDVVKVVN SDGNTMETFG NGFGDWNLDW KKWQGGSALT ATSPEGADPA KQVRLTPESI
//
