ID A0A1F6ASR8_9BACT Unreviewed; 368 AA.
AC A0A1F6ASR8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Dolichyl-phosphate beta-D-mannosyltransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A3A64_03220 {ECO:0000313|EMBL:OGG27739.1};
OS Candidatus Gottesmanbacteria bacterium RIFCSPLOWO2_01_FULL_48_11.
OC Bacteria; Candidatus Gottesmanbacteria.
OX NCBI_TaxID=1798395 {ECO:0000313|EMBL:OGG27739.1, ECO:0000313|Proteomes:UP000178305};
RN [1] {ECO:0000313|EMBL:OGG27739.1, ECO:0000313|Proteomes:UP000178305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(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:OGG27739.1}.
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DR EMBL; MFJY01000037; OGG27739.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6ASR8; -.
DR Proteomes; UP000178305; 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 250..270
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 276..297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 318..339
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 345..362
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 5..175
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF00535"
FT DOMAIN 249..367
FT /note="GtrA/DPMS transmembrane"
FT /evidence="ECO:0000259|Pfam:PF04138"
SQ SEQUENCE 368 AA; 40594 MW; 3AE4B3C820D747CF CRC64;
MKAVIILPTY NERENIVDIL TKLTRVTRTI SDFSFVFLVA DDASPDGTAQ AVEDYKKDRN
DIVIVSGKKE GLGKAILRGM IYAVEVLHAD IVAQIDADLS HDPEALPKFF EKITKGYDFV
VGSRYIPGGS IPDNWGIHRK IYSVIGNAIV RFGLGQTGVH DWTGGYRAYH KKYVELLREK
VKPYSGYVFQ IAFLHNAISS GARVAEVPIH FTDRRFGHSK IAPSEYIRNV LLYVAKERVA
SVIHGQLGKF FVVGAIGFVI NTIALELLVG TGAHPVAGSA IGAELAIISN FFLNNAWTFG
HKKIAKGSMF AKFFQFNGTS LGALFIQSGT VFVGTLLFGL GAYRLSYILG IGLGLIWNYT
MYSKVIWK
//
