ID A0A0M9XB04_9ACTN Unreviewed; 748 AA.
AC A0A0M9XB04;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Bi-functional transferase/deacetylase {ECO:0000313|EMBL:KOT45466.1};
GN ORFNames=ADK41_02810 {ECO:0000313|EMBL:KOT45466.1};
OS Streptomyces caelestis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=36816 {ECO:0000313|EMBL:KOT45466.1, ECO:0000313|Proteomes:UP000037773};
RN [1] {ECO:0000313|EMBL:KOT45466.1, ECO:0000313|Proteomes:UP000037773}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-24567 {ECO:0000313|EMBL:KOT45466.1,
RC ECO:0000313|Proteomes:UP000037773};
RA Noorani M.;
RL Submitted (JUL-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:KOT45466.1}.
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DR EMBL; LGCN01000017; KOT45466.1; -; Genomic_DNA.
DR RefSeq; WP_030823237.1; NZ_LGCN01000017.1.
DR AlphaFoldDB; A0A0M9XB04; -.
DR PATRIC; fig|36816.3.peg.597; -.
DR OrthoDB; 9763050at2; -.
DR Proteomes; UP000037773; 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:UP000037773};
KW Transferase {ECO:0000313|EMBL:KOT45466.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 348..371
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 638..662
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 668..690
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 96..283
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
FT REGION 287..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 748 AA; 81382 MW; 48F5276ECB8B3C48 CRC64;
MTTAPARGRR RAPTRMERAA GRAAALHRPR VLLALLLLLA LTCVMLLDGY LRAEVGDDQR
VRSGASSSEV PDEILDGGPI LGFPGGQAET VSVPDRTIVL TFDDGPDPTW TPKVMEVLEK
YDVPGTFFVV GSMVSRHPDI VEDLVEQGHE IGVHTFTHVD LSYQSASRVT REMEQTQLAL
AGAAGITTTL FRAPYSSGAD AVDNYSWQVY QQLGQEGYTS VFVDTDSEDW KEPGVAKIVE
GATPEDGEGA SVLFHDSGGD RTQTLAALSE YIEKMRAKGY SFTTVSGATA ERRQQQQSAG
GSGAGGPGAP SGTGDALQAS HRPATGTLRY EGKALLAAVA VAEWTVPALS AGLVIVGVAV
MGRFGLMLVL ARRHHRQRNG RRFGWGPPVT RPVSVIVPAY NEKECIENTL RSLAESTHPI
EIVVVDDGST DGTAELAEGL GLPGVRVIRQ ENAGKPAALN NGIRSARHDI VVMMDGDTVF
EPDTVGRLVQ PFADPSVGAV AGNAKVGNRS TLIGAWQHIE YVMGFNLDRR MYDLLRCMPT
IPGAIGAFRR EAVLQVGGMS EDTLAEDTDI TIALHRAGWR VVYEEHARAW TEAPRSLRQL
WSQRHRWSYG TMQALWKHRG SLMDKGPSGR FGRVGMPLVV LFQIVTPVFA PLIDVFTVYS
MLFVDFRAAL SAWFAVLGVQ LVCAAYAFRL DREKYRYLLM MPLQQFAYRQ MMYLVLIHSC
VTALTGGRLR WQKLKRTGEV GMPAGTGG
//
