ID A0A0T0MFM9_9CELL Unreviewed; 683 AA.
AC A0A0T0MFM9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Bi-functional transferase/deacetylase {ECO:0000313|EMBL:KQS97699.1};
GN ORFNames=ASG23_17340 {ECO:0000313|EMBL:KQS97699.1};
OS Cellulomonas sp. Leaf395.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=1736362 {ECO:0000313|EMBL:KQS97699.1, ECO:0000313|Proteomes:UP000051971};
RN [1] {ECO:0000313|EMBL:KQS97699.1, ECO:0000313|Proteomes:UP000051971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf395 {ECO:0000313|EMBL:KQS97699.1,
RC ECO:0000313|Proteomes:UP000051971};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQS97699.1, ECO:0000313|Proteomes:UP000051971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf395 {ECO:0000313|EMBL:KQS97699.1,
RC ECO:0000313|Proteomes:UP000051971};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQS97699.1}.
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DR EMBL; LMQI01000005; KQS97699.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T0MFM9; -.
DR STRING; 1736362.ASG23_17340; -.
DR Proteomes; UP000051971; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd06423; CESA_like; 1.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR002509; NODB_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR43630; POLY-BETA-1,6-N-ACETYL-D-GLUCOSAMINE SYNTHASE; 1.
DR PANTHER; PTHR43630:SF1; POLY-BETA-1,6-N-ACETYL-D-GLUCOSAMINE SYNTHASE; 1.
DR Pfam; PF13641; Glyco_tranf_2_3; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR PROSITE; PS51677; NODB; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000051971};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:KQS97699.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..683
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006657771"
FT TRANSMEM 283..310
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 577..601
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 607..629
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 650..670
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 60..247
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 683 AA; 73060 MW; 5C4CC75DB3758425 CRC64;
MLVAVLAVLL LALGLQTITA SVWQAGTATT GERVPVATPP GGPVLVADGD TLVGVPLQER
TVALTFDDGP DPRWTPQILD VLARENVPAT FFVVGSHAVE EPELLRQVVA AGHELGGHTW
SHADLSAVPT WRANLELSLG QLGLAGGAGI STSLLRPPYS SSPGDLDAAE LTAVQRAADA
GYLVVLADRD TKDWSRPGVE QIVADGSPTG TEGQIVLLHD GGGDRSETLA ALPALIERYR
EAGYRFTTVS DGLGLAVGAT RPAEAIPAVQ GQVLDVAVRA SGWLVTAVSW AVLGFGVLSL
LRTVLVVGLA PRHGRVSKRR VARGQWLPPV TVLVPAYNEA VGIERAVRSL VASDHPELEV
VVIDDGSTDG TGDVVERLGL PGVRLVRQAN AGKAAALRTG TRVASHDVLV MLDGDTVFEP
DTIRQLVQPL RDLAVGAVSG NTKVGNRTGL LGRWQHLEYV SGFNLDRRLQ DLLGCITTVP
GAAGAFRRQA VEAAGGLSSE TLAEDTDITM GVLRAGYRVV HEERARAWTE APSSVNDLWR
QRYRWSYGTM QCIWKHRHAV RDSTDGGRRL GWVGIPYMLL FQVLLPLLAP AIDLFALYGL
FTGNARSVMT VWLAFALVQL ATTAYALRLD GESLKPLWSL PLQQVFYRQL IYLVVIQSIA
SAVAGARLPW HKLHRSGDVV VRA
//