ID A0A0S8AEA0_9BACT Unreviewed; 411 AA.
AC A0A0S8AEA0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Glycosyl transferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AMK71_12975 {ECO:0000313|EMBL:KPJ97638.1};
OS Nitrospira bacterium SG8_35_4.
OC Bacteria; Nitrospirota; Nitrospiria.
OX NCBI_TaxID=1704025 {ECO:0000313|EMBL:KPJ97638.1, ECO:0000313|Proteomes:UP000050997};
RN [1] {ECO:0000313|EMBL:KPJ97638.1, ECO:0000313|Proteomes:UP000050997}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_35_4 {ECO:0000313|EMBL:KPJ97638.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPJ97638.1}.
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DR EMBL; LJTM01000280; KPJ97638.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8AEA0; -.
DR Proteomes; UP000050997; 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 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};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 41..63
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 84..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 136..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 190..207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 213..229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 273..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 329..347
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 353..375
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 182
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ SEQUENCE 411 AA; 45217 MW; DB9F10E4DFCD4F35 CRC64;
MREKHFAINW TPLHTGGTML LLLLSLPLVR EFFHDRGGVR WVHVLLIASL VSYIITPIVK
YAAFKFNILD NPDARKVHNS PTPLMGGIGI YIAFLTAIMG NVIFSRELIA IVIGATIVFI
SGLLDDIMKL SSRVRLLLQL MAVMILMLNG ITISIFETTS LGVLLNSGIT CLWIIGLTNT
TNFFDGMDGL ATGLCILFSF FIGVVAFQTY QPFLGWLSVA VMGGCLGFLP SNFRSGKPAE
IFLGDSGSNF LGFTLASIAV MGEWSERSLV SSLITPVLIF SVMIYDMIYI TISRILTGKV
NTVKEWLDYV GKDHLHHRLA DLLHSRRKSV LFILLLSFTL GLNALLLRDS DAMTAVILLA
QALCILVVIT IMEIAGNKKA KSRSITNAIQ EAPEIYPINQ DTEEGSCTPQ P
//
