ID A0A1I2LR16_9ACTN Unreviewed; 449 AA.
AC A0A1I2LR16;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Lipoprotein-anchoring transpeptidase ErfK/SrfK {ECO:0000313|EMBL:SFF80910.1};
GN ORFNames=SAMN05216251_13014 {ECO:0000313|EMBL:SFF80910.1};
OS Actinacidiphila alni.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Actinacidiphila.
OX NCBI_TaxID=380248 {ECO:0000313|EMBL:SFF80910.1, ECO:0000313|Proteomes:UP000199323};
RN [1] {ECO:0000313|EMBL:SFF80910.1, ECO:0000313|Proteomes:UP000199323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.3510 {ECO:0000313|EMBL:SFF80910.1,
RC ECO:0000313|Proteomes:UP000199323};
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; FONG01000030; SFF80910.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2LR16; -.
DR STRING; 380248.SAMN05216251_13014; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000199323; 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.
PE 4: Predicted;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Lipoprotein {ECO:0000313|EMBL:SFF80910.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199323};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 101..264
FT /note="Bacterial Ig"
FT /evidence="ECO:0000259|Pfam:PF17964"
FT DOMAIN 286..420
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
FT REGION 36..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 449 AA; 46325 MW; 341DFE8403E8E5B0 CRC64;
MTPPDTGNAP AKRSPITRRR TLAAVAVLMG GAVALTACGG HDDGDSKAAG SGPSTSASSP
SQSPSPSASA SASAQAKKED AAAAKQASDA KITIAPKDGS TGASIHNDAK VTVAGGTLTS
VTMTSKATGN KIPGTISADR TSWRPDVALA RGTQYTISAA ATDAKGRAAA ANGTFATVSA
SSSFIGYFTP EDGSTVGVGM PVSINFDKAI TDRAAVESGI TVTSSSGQRV EGHWFSSTRL
DFRPEQYWQA GSHVSLKLHL DGVKGAAGVY GVQDKTVNFT VGRSQVSTVD ARTHQMTVVR
DGKVIRTIPI SAGAPDHSTY NGQMVISEKY EKTRMNGATV GFTEDDGKGE YDIPDVPHAM
RLSNSGTFIH GNYWGSKSIF GTANTSHGCV GLSDTKGGKD PDTPAAWFYN NSMVGDVVVV
KDSADKTIQP DNGLNGWNLS WAAWTAPQA
//
