ID A0A077M5S5_9MICO Unreviewed; 409 AA.
AC A0A077M5S5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Dolichol-phosphate mannosyltransferase, fused to C-terminaluncharacterized domain {ECO:0000313|EMBL:CCH79400.1};
GN ORFNames=BN12_4230001 {ECO:0000313|EMBL:CCH79400.1};
OS Tetrasphaera japonica T1-X7.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC Tetrasphaera.
OX NCBI_TaxID=1194083 {ECO:0000313|EMBL:CCH79400.1, ECO:0000313|Proteomes:UP000035721};
RN [1] {ECO:0000313|EMBL:CCH79400.1, ECO:0000313|Proteomes:UP000035721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T1-X7 {ECO:0000313|EMBL:CCH79400.1,
RC ECO:0000313|Proteomes:UP000035721};
RX PubMed=23178666; DOI=10.1038/ismej.2012.136;
RA Kristiansen R., Nguyen H.T.T., Saunders A.M., Nielsen J.L., Wimmer R.,
RA Le V.Q., McIlroy S.J., Petrovski S., Seviour R.J., Calteau A.,
RA Nielsen K.L., Nielsen P.H.;
RT "A metabolic model for members of the genus Tetrasphaera involved in
RT enhanced biological phosphorus removal.";
RL ISME J. 7:543-554(2013).
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:CCH79400.1}.
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DR EMBL; CAJB01000361; CCH79400.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077M5S5; -.
DR STRING; 1194083.BN12_4230001; -.
DR Proteomes; UP000035721; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd04179; DPM_DPG-synthase_like; 1.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR48090; UNDECAPRENYL-PHOSPHATE 4-DEOXY-4-FORMAMIDO-L-ARABINOSE TRANSFERASE-RELATED; 1.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000313|EMBL:CCH79400.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000035721};
KW Transferase {ECO:0000313|EMBL:CCH79400.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 351..369
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 376..398
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 119..281
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF00535"
FT REGION 1..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 409 AA; 45031 MW; C7470012CCB1A0A7 CRC64;
MSEHLTEPMT QGPTGPAADP TQPTAYTPTG LTSADLTEPM TQGPTGPAAD PTQPPACTPT
GLTSADLTEP MTQAPAGPAA DPTEPTAYTP TISRREDHGP RTGYVVEGDD PTLPDPYVTV
VLPCYNEGAH VLKEIDRISR VLDESEFGYE ILCIDDASTD DTLAVLRDAR ADYPSVKVLP
FRRNGGAGTA RRIGSQLARG EIVVWTDADM TYENERIPDL VRVLHDDPTY DQVVGARTTE
EGTHKWARVP AKWFIRKVAE HLTNQRIPDL NSGLRAFRRE VSLPYLRLLP AGFSCVTTIT
IAFLSNQHDV KYVETSYAKR EGTSKFHFVR DAYRYILQVL RMVMYFDPLK VLMPPALWLI
AIALVKGVVD MVRHPFYFPA STVLLFVSGM MIGSLALLSD LVVRSRDGA
//
