ID A0A1G9BLZ3_9ACTN Unreviewed; 412 AA.
AC A0A1G9BLZ3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Lipoprotein-anchoring transpeptidase ErfK/SrfK {ECO:0000313|EMBL:SDK40538.1};
GN ORFNames=SAMN05421806_107136 {ECO:0000313|EMBL:SDK40538.1};
OS Streptomyces indicus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=417292 {ECO:0000313|EMBL:SDK40538.1, ECO:0000313|Proteomes:UP000199155};
RN [1] {ECO:0000313|EMBL:SDK40538.1, ECO:0000313|Proteomes:UP000199155}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.5727 {ECO:0000313|EMBL:SDK40538.1,
RC ECO:0000313|Proteomes:UP000199155};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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DR EMBL; FNFF01000007; SDK40538.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9BLZ3; -.
DR STRING; 417292.SAMN05421806_107136; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000199155; 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; 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: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 Lipoprotein {ECO:0000313|EMBL:SDK40538.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199155};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..412
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038420988"
FT DOMAIN 65..227
FT /note="Bacterial Ig"
FT /evidence="ECO:0000259|Pfam:PF17964"
FT DOMAIN 249..381
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
FT REGION 28..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 412 AA; 43645 MW; A69DABB386C0623A CRC64;
MTDSKRSRGL VAVSALLGGV LVLSACSSGD EGTKGKDSQQ EKTDQAAAQD TSAARISVSP
KNGSKNASIN NAGKVTVKDG TLTEVTMTTA DGTKVAGSLS ADKKTWKPDA QLERATTYKV
AVVAKDSEGR DAHENTTFTT VAPTNSFIGN FTPEDGSTVG VGMPVSINFD KAIENKAHVQ
KGITVTSSSG QEVVGHWFNS QRIDFRPEDY WKAGSTVTLD LKLDGVEGAD GVYGVQQKSI
TFKIGRSQVS TVDAKTKQMT VERDGKVIKT IPISAGAPEN KTYEGEMVIS EKFKETRMNG
ATVGFTDDDG KGEYDIKDVP HAMRLSTSGT FIHGNYWGKG IFGSANTSHG CVGLQDAKGA
DDPNTPGAWF YDNSMVGDVV IVKNTGDKTI APDNGLNGWN MSWAEWTAGS QA
//
