ID A0A136K3I6_9BACT Unreviewed; 542 AA.
AC A0A136K3I6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Putative undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase {ECO:0000313|EMBL:KXK03972.1};
DE EC=2.7.8.- {ECO:0000313|EMBL:KXK03972.1};
GN ORFNames=UZ03_NOB001001455 {ECO:0000313|EMBL:KXK03972.1};
OS Nitrospira sp. OLB3.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Nitrospira.
OX NCBI_TaxID=1617410 {ECO:0000313|EMBL:KXK03972.1, ECO:0000313|Proteomes:UP000070691};
RN [1] {ECO:0000313|EMBL:KXK03972.1, ECO:0000313|Proteomes:UP000070691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB3 {ECO:0000313|EMBL:KXK03972.1};
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 (MAR-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:KXK03972.1}.
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DR EMBL; JZQY01000034; KXK03972.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136K3I6; -.
DR STRING; 1617410.UZ03_NOB001001455; -.
DR PATRIC; fig|1617410.3.peg.1477; -.
DR Proteomes; UP000070691; 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:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IEA:InterPro.
DR CDD; cd06853; GT_WecA_like; 1.
DR InterPro; IPR000715; Glycosyl_transferase_4.
DR InterPro; IPR018480; PNAcMuramoyl-5peptid_Trfase_CS.
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.
DR PROSITE; PS01348; MRAY_2; 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:KXK03972.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 46..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 71..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 100..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 181..199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 211..228
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 234..256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 277..305
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 311..330
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 362..383
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 389..407
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 414..430
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 442..460
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 472..488
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 494..515
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 522..541
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 150
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT BINDING 210
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ SEQUENCE 542 AA; 59103 MW; 2C81C92415A6A7E5 CRC64;
MTSAVFFSFI TSLFICMALI PPLQLNAGRW SFMDLPGGRK VHANPIPRIG GIAFGSAALL
SIFFWVPQDP AVGPVLLSAL VILAFGIWDD RANLNYKVKL IGQLVAVFAV VIVGDIRLEQ
VPFLYDENAP LWLALPLTVV FLVGAANAVN LSDGLDGLAG GLAFLSFAGI AYLAYLSHDT
TVLVLAAGFL GGLLGFLRYN TYPARIFMGD AGSQLLGFSM GVLVLLLSDP SRNPFPVTIG
LLVLGLPFLD TIAVMGQRLA KGRSPFIGDR NHVHHKLLAL GLSHYEAVIV IYGIQAVMVG
LAYLLRWQSD ALILTMYGTF AFAMFALFVA TERGGILLSE STDGRVLSDT KMARIGLWLS
DMAPRFLAVV VPLFLIANVF VPGHVPMDVG YAALGLFAVV LGGLWLMPEY RSHFVRGGLY
VGSAFLMYMG EQSGILDIWP IYVTQNTLLA VIAILVLLSM RFSRGNRFQT TPLDYLMVFF
ALIVPLLPEM RADMPTLSIL AAKLIVLYFS FELLLHTFAD RVKQFGLVSL WILFGLGVRA
WL
//
