ID A0A191UYP2_9ACTN Unreviewed; 734 AA.
AC A0A191UYP2;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Bi-functional transferase/deacetylase {ECO:0000313|EMBL:ANJ07793.1};
GN ORFNames=GCM10010220_24090 {ECO:0000313|EMBL:GGR71071.1},
GN Spa2297_12795 {ECO:0000313|EMBL:ANJ07793.1};
OS Streptomyces parvulus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=146923 {ECO:0000313|EMBL:ANJ07793.1, ECO:0000313|Proteomes:UP000078468};
RN [1] {ECO:0000313|EMBL:ANJ07793.1, ECO:0000313|Proteomes:UP000078468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2297 {ECO:0000313|EMBL:ANJ07793.1,
RC ECO:0000313|Proteomes:UP000078468};
RA Nishizawa T., Miura T., Harada C., Guo Y., Narisawa K., Ohta H.,
RA Takahashi H., Shirai M.;
RT "Non-Contiguous Finished Genome Sequence of Streptomyces parvulus 2297
RT Integrated Site-Specifically with Actinophage R4.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GGR71071.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 4068 {ECO:0000313|EMBL:GGR71071.1};
RX PubMed=30832757;
RA Wu L., Ma J.;
RT "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT project: providing services to taxonomists for standard genome sequencing
RT and annotation.";
RL Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN [3] {ECO:0000313|EMBL:GGR71071.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 4068 {ECO:0000313|EMBL:GGR71071.1};
RA Sun Q., Ohkuma M.;
RL Submitted (DEC-2022) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP015866; ANJ07793.1; -; Genomic_DNA.
DR EMBL; BMRX01000005; GGR71071.1; -; Genomic_DNA.
DR RefSeq; WP_064728172.1; NZ_CP015866.1.
DR AlphaFoldDB; A0A191UYP2; -.
DR KEGG; spav:Spa2297_12795; -.
DR Proteomes; UP000078468; Chromosome.
DR Proteomes; UP000645274; 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; cd10962; CE4_GT2-like; 1.
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:ANJ07793.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 317..339
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 607..633
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 639..659
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 680..700
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 91..278
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
FT REGION 705..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 734 AA; 80446 MW; 97D34A3A69E45EA3 CRC64;
MASRTRRHGA ARSARAVSRR RLPLRLLLPL LLLVALAAML MLRGYVHSEI LADHRVQAPA
PTTHVPEKIL EGGPVIDVRG GRTESLSVPD HRLVLTFDDG PDPTWTPRVL DVLKKHDAHA
VFFVTGTMAS RYPDLVQRMV DEGHEVGLHT FNHPDLSFQS KKRIDWELSQ NQLAITGAAG
VRTSLFRPPY SSFADAMDDK SWPVTEYIGS RGYITVVNNT DSEDWKKPGV GEIIRRATPE
GGKGAIVLMH DSGGDRHQTV QALDRFLPDL KEKGYRFANL TEALDAPSAM SPVTGAELWK
GKAWVFLVQA SEKLTDVLVV GLAIIGTLVI GRFVLMLLLS GVHARRVRRK GFGWGPAVTG
PVTVLVPAYN EAKCIENTVR SLMESDHPIE IIVIDDGSTD GTARIVEGLG LPGVRVIRQL
NAGKPAALNR GLANARYDIV VMMDGDTVFE PSTVRELVQP FGDPRVGAVA GNAKVGNKDS
LIGAWQHIEY VMGFNLDRRM YDILGCMPTI PGAVGAFRRS ALAPIGGMSD DTLAEDTDVT
MALHRAGWRV VYAENARAWT EAPESVSQLW SQRYRWSYGT MQAIWKHRRA VIEKGPSGRF
GRVGLPFVSL FMVLAPLLAP LIDVFLLYGI VFGPTQKTIV AWLGVLAIQA VCAAYAFRLD
RERLTPLISL PLQQILYRQI MYVVLLQSWI TALTGGRLRW QKLRRSGGVS APPGGGAPGV
PAPRSRAMDG RPVG
//
