ID A0A136KKT0_9BACT Unreviewed; 331 AA.
AC A0A136KKT0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Putative undecaprenyl-phosphate N-acetylglucosaminyl 1-phosphate transferase {ECO:0000313|EMBL:KXK10032.1};
DE EC=2.7.8.33 {ECO:0000313|EMBL:KXK10032.1};
GN Name=tagO {ECO:0000313|EMBL:KXK10032.1};
GN ORFNames=UZ20_WS6002000113 {ECO:0000313|EMBL:KXK10032.1};
OS candidate division WS6 bacterium OLB21.
OC Bacteria; Candidatus Dojkabacteria.
OX NCBI_TaxID=1617427 {ECO:0000313|EMBL:KXK10032.1, ECO:0000313|Proteomes:UP000070449};
RN [1] {ECO:0000313|EMBL:KXK10032.1, ECO:0000313|Proteomes:UP000070449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB21 {ECO:0000313|EMBL:KXK10032.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Improved understanding of the partial-nitritation anammox process through
RT 23 genomes representing the majority of the microbial community.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR600715-1};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KXK10032.1}.
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DR EMBL; JYPD01000010; KXK10032.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136KKT0; -.
DR STRING; 1617427.UZ20_WS6002000113; -.
DR Proteomes; UP000070449; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0036380; F:UDP-N-acetylglucosamine-undecaprenyl-phosphate N-acetylglucosaminephosphotransferase activity; IEA:UniProtKB-EC.
DR CDD; cd06853; GT_WecA_like; 1.
DR InterPro; IPR000715; Glycosyl_transferase_4.
DR PANTHER; PTHR22926; PHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE; 1.
DR PANTHER; PTHR22926:SF3; UNDECAPRENYL-PHOSPHATE ALPHA-N-ACETYLGLUCOSAMINYL 1-PHOSPHATE TRANSFERASE; 1.
DR Pfam; PF00953; Glycos_transf_4; 1.
PE 4: Predicted;
KW Magnesium {ECO:0000256|PIRSR:PIRSR600715-1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR600715-1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KXK10032.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 42..63
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 115..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 170..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 195..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 252..269
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 311..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 107
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ SEQUENCE 331 AA; 35581 MW; 836BB134D37B6DCC CRC64;
MIIAAGTVHM STQMGGMFVG LAILTIVGIL DDKYELSGKV QLLFQLIAAV IVVITGSTIT
GISVAGLDLD FVASSTAINF GSLVYYMNLP ADIITVIWIL LIVNALNWVC GIDALGEGMA
IIAALVMSIL SVRFGALDLA FIPFVLAFGI LGFILYNYPP SKIIGGTVGH GYGFIIAVLS
IMISSVATAG NGPKLTTSII ILSIPILDMI WVLINRMKEN KTINIFKLLS ISGRVHLHHR
LMVAGLTTKQ TLYVETSAMA IIAVVAFYFG DFNNALTTGL IVIALILILF TFISIRNRAV
SRTKIVKRSK EPEDPPAIVD TGPSPEERYA Y
//
