ID A0A255GQ54_9ACTN Unreviewed; 470 AA.
AC A0A255GQ54;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Mannosyl-glycoprotein endo-beta-N-acetylglucosamidase-like domain-containing protein {ECO:0000259|SMART:SM00047};
GN ORFNames=CGZ94_02160 {ECO:0000313|EMBL:OYO17711.1};
OS Enemella evansiae.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Enemella.
OX NCBI_TaxID=2016499 {ECO:0000313|EMBL:OYO17711.1, ECO:0000313|Proteomes:UP000215896};
RN [1] {ECO:0000313|EMBL:OYO17711.1, ECO:0000313|Proteomes:UP000215896}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML 030167 {ECO:0000313|EMBL:OYO17711.1,
RC ECO:0000313|Proteomes:UP000215896};
RA Bernier A.-M., Bernard K., Domingo M.-C.;
RT "Draft whole genome sequences of clinical Proprionibacteriaceae strains.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
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:OYO17711.1}.
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DR EMBL; NMVO01000001; OYO17711.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A255GQ54; -.
DR OrthoDB; 3734014at2; -.
DR Proteomes; UP000215896; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004040; F:amidase activity; IEA:InterPro.
DR Gene3D; 1.10.530.10; -; 1.
DR InterPro; IPR002901; MGlyc_endo_b_GlcNAc-like_dom.
DR PANTHER; PTHR33308; PEPTIDOGLYCAN HYDROLASE FLGJ; 1.
DR PANTHER; PTHR33308:SF9; PEPTIDOGLYCAN HYDROLASE FLGJ; 1.
DR Pfam; PF01832; Glucosaminidase; 1.
DR PRINTS; PR01002; FLGFLGJ.
DR SMART; SM00047; LYZ2; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000215896};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 94..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 121..275
FT /note="Mannosyl-glycoprotein endo-beta-N-
FT acetylglucosamidase-like"
FT /evidence="ECO:0000259|SMART:SM00047"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..380
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..425
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 470 AA; 50333 MW; C84F5C2CB40771C4 CRC64;
MIPPSTVTWT TSATEVPPGA KCCPASWSDR PPIARRSRKS LVNLRTRPRS PFPAVRERNL
PPPRTRLRPA SGPSVRAYPA EEPTMKPQRI DRRVLAIAIT VLTVASSLLL APWAMAAKGV
DTSSKQAYLK SVAPLAQASM KKYGVPASVA IAQSIQESSW GKSSLSLEGN AYFGIKCSSQ
SQYSNGCVTK QTWEVVNGKK IVIDAKFRRY PKPENSFLDH GLFLKSKDRY AAAFKYTKQP
KQFIREVHKA GYATDPNYTN AITKLMDQYN LYQYDKVTTT TSPTKKPTAT KSPTKKPTAK
PTATKSPTGK PTAKPTPKQT ASPKPTATRS PTDKPTGKPT PKQTATPKQT ATPKPTASPK
PTPKQTATPK ATPPVTSSPE PTTQPTSEPT SEPTTGPEPT TDPTSEPVPT EPTEPSDPTE
PVNPEQPADP EKELPPDVPA PAPVADSKSS GGYPTGGYPE TTGGLASTGV
//
