ID A0A1J5FNQ8_9BACT Unreviewed; 376 AA.
AC A0A1J5FNQ8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Glycosyltransferase 2-like domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AUK12_00175 {ECO:0000313|EMBL:OIP58119.1};
OS Candidatus Levybacteria bacterium CG2_30_37_29.
OC Bacteria; Candidatus Levybacteria.
OX NCBI_TaxID=1805237 {ECO:0000313|EMBL:OIP58119.1, ECO:0000313|Proteomes:UP000182355};
RN [1] {ECO:0000313|EMBL:OIP58119.1, ECO:0000313|Proteomes:UP000182355}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG2_30_37_29 {ECO:0000313|EMBL:OIP58119.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(2016).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family.
CC {ECO:0000256|ARBA:ARBA00006739}.
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:OIP58119.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MNYS01000002; OIP58119.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J5FNQ8; -.
DR STRING; 1805237.AUK12_00175; -.
DR Proteomes; UP000182355; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004582; F:dolichyl-phosphate beta-D-mannosyltransferase activity; IEA:InterPro.
DR GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:InterPro.
DR CDD; cd06442; DPM1_like; 1.
DR InterPro; IPR039528; DPM1-like.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR007267; GtrA_DPMS_TM.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR43398:SF2; DOLICHOL-PHOSPHATE MANNOSYLTRANSFERASE; 1.
DR PANTHER; PTHR43398; DOLICHOL-PHOSPHATE MANNOSYLTRANSFERASE SUBUNIT 1; 1.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR Pfam; PF04138; GtrA; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 252..270
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 349..372
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 6..176
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF00535"
FT DOMAIN 251..372
FT /note="GtrA/DPMS transmembrane"
FT /evidence="ECO:0000259|Pfam:PF04138"
SQ SEQUENCE 376 AA; 42443 MW; A6FFFD1AA3CBD2B7 CRC64;
MKKVVIILPT YNESGNIDKV ITLLEEDIFP KIKNHDMNIL VADDNSPDGT ADEVRNLMKK
WKNIDLNLGE KKGLGAAYVR GMTYAVEKMG ADIMFEMDAD GQHDPQKITQ FLQKIDEGND
FVIGTRYSNG GSVPSNWPIQ RKAFSIVANL LVRTIFARFS IHDWTGGYRA LKKEVFLKEK
KELENFNGYI FQISFLHKVV RDKFKVAEVP FLMTDRTLGK SKIAPLGYIF DVLFYVITAR
IKELATGSFG KFLVVGGTGF VIQVVIYQIL VNATKLPLGI DTVLSAQMAI FSNYNLNNLW
TFKERKATNF GQYVLKMAGF FGTSNVGVIV IQSGIVQLGE ILYGRNYPLV YFVIGTGVLM
VWNFGTYSLV IWKKKK
//
