ID A0A1C6V885_9ACTN Unreviewed; 731 AA.
AC A0A1C6V885;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase {ECO:0000313|EMBL:SCL62485.1};
GN ORFNames=GA0070603_3412 {ECO:0000313|EMBL:SCL62485.1};
OS Micromonospora chersina.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=47854 {ECO:0000313|EMBL:SCL62485.1, ECO:0000313|Proteomes:UP000198605};
RN [1] {ECO:0000313|EMBL:SCL62485.1, ECO:0000313|Proteomes:UP000198605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44151 {ECO:0000313|EMBL:SCL62485.1,
RC ECO:0000313|Proteomes:UP000198605};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FMIB01000002; SCL62485.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C6V885; -.
DR STRING; 47854.GA0070603_3412; -.
DR OrthoDB; 3864432at2; -.
DR Proteomes; UP000198605; 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 Transferase {ECO:0000313|EMBL:SCL62485.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 329..354
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 620..646
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 652..672
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 102..289
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 731 AA; 80468 MW; 38D5632BF3528EC5 CRC64;
MGVWRAGRRL DGTGDVPAPP GLTTWGRRQR RRDRRRWLLA AVATFILLNL LAIGAYANAR
FTPDHRAEGP AGTATVPKPV RDGGTVVDFP DGRLEARRMP PKTIALTFDD GPDPKWTPQV
LDVLARHHAP ATFFVVGSQV ARHPELAERM AREGHELGIH TFTHPQMADL PAWRRKLEYS
QTQAAIAHLT GVSTSLARLP YSSGVDSLDD ASWPVVRETG RWGYVSVFND TDSRDWARPG
VPAIVRNATP DGDRGAVVLM HDSGGDRSQT VAALDRFIPE MQARGYRFTT VSQGLGQPGA
GTARLDALDR ARGALLVWGV RAADGTIRLL WLLLIVVGLL TLARTLLLFG YAVAHARRRR
APTWSWGGVV TDPVTIIVPA YNERTTIAAA VRSLATGSHP GIEVLVVDDE SDDGTAEEVE
RLGLPNVRVA RVPGGGKAAA LNAGVALARH DLLVMVDADT VVDPDAIHRL VQPFADPRVG
AVAGNVKVGN RRRLLGRWQH IEYVIGFSLD RRLYDTLHCM PTIPGALGAF RREAVRAAGG
LSRATLAEDT DLTMGIHRAG WRVVYEETAV ARTEAPVTLP ELWRQRYRWS YGTMQALWRH
RRALVERGPS GRFGRRGLPF IALFSVLLPL LAPVVDIFAV YGLFFLDRYE TVAAWLAVLV
VQVVTAILAF RLDREPLRPL WALPLQQFVY RQVMYLVLLH SVITALSGGR LKWQKLRRTG
EVAAAHTQPV T
//
