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Database: UniProt
Entry: A0A261GQ62_9GAMM
LinkDB: A0A261GQ62_9GAMM
Original site: A0A261GQ62_9GAMM 
ID   A0A261GQ62_9GAMM        Unreviewed;       357 AA.
AC   A0A261GQ62;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase {ECO:0000256|HAMAP-Rule:MF_02030};
DE            EC=2.7.8.33 {ECO:0000256|HAMAP-Rule:MF_02030};
DE   AltName: Full=UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase {ECO:0000256|HAMAP-Rule:MF_02030};
DE   AltName: Full=Undecaprenyl-phosphate GlcNAc-1-phosphate transferase {ECO:0000256|HAMAP-Rule:MF_02030};
GN   Name=wecA {ECO:0000256|HAMAP-Rule:MF_02030};
GN   ORFNames=BTA51_07640 {ECO:0000313|EMBL:OZG73679.1};
OS   Hahella sp. CCB-MM4.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Hahellaceae; Hahella.
OX   NCBI_TaxID=1926491 {ECO:0000313|EMBL:OZG73679.1, ECO:0000313|Proteomes:UP000215632};
RN   [1] {ECO:0000313|EMBL:OZG73679.1, ECO:0000313|Proteomes:UP000215632}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCB-MM4 {ECO:0000313|EMBL:OZG73679.1,
RC   ECO:0000313|Proteomes:UP000215632};
RA   Sam K.-K., Lau N.-S., Dinesh B., Go F., Amirul A.-A.A.;
RT   "Genome sequence of Hahella sp. CCB-MM4 and discovery of its potential
RT   applications.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the transfer of the GlcNAc-1-phosphate moiety from
CC       UDP-GlcNAc onto the carrier lipid undecaprenyl phosphate (C55-P),
CC       yielding GlcNAc-pyrophosphoryl-undecaprenyl (GlcNAc-PP-C55).
CC       {ECO:0000256|HAMAP-Rule:MF_02030}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-
CC         D-glucosamine = N-acetyl-alpha-D-glucosaminyl-di-trans,octa-cis-
CC         undecaprenyl diphosphate + UMP; Xref=Rhea:RHEA:28090,
CC         ChEBI:CHEBI:57705, ChEBI:CHEBI:57865, ChEBI:CHEBI:60392,
CC         ChEBI:CHEBI:62959; EC=2.7.8.33; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_02030};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02030,
CC         ECO:0000256|PIRSR:PIRSR600715-1};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02030};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC       biosynthesis. {ECO:0000256|HAMAP-Rule:MF_02030}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_02030}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_02030}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC       membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. WecA
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_02030}.
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:OZG73679.1}.
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DR   EMBL; MRYI01000003; OZG73679.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A261GQ62; -.
DR   OrthoDB; 9783652at2; -.
DR   UniPathway; UPA00281; -.
DR   Proteomes; UP000215632; Unassembled WGS sequence.
DR   GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0036380; F:UDP-N-acetylglucosamine-undecaprenyl-phosphate N-acetylglucosaminephosphotransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009243; P:O antigen biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd06853; GT_WecA_like; 1.
DR   HAMAP; MF_02030; WecA_Gammaproteo; 1.
DR   InterPro; IPR012750; ECA_WecA-rel.
DR   InterPro; IPR000715; Glycosyl_transferase_4.
DR   NCBIfam; TIGR02380; ECA_wecA; 1.
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   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_02030};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_02030};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW   Rule:MF_02030};
KW   Lipopolysaccharide biosynthesis {ECO:0000256|ARBA:ARBA00022985,
KW   ECO:0000256|HAMAP-Rule:MF_02030};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_02030, ECO:0000256|PIRSR:PIRSR600715-
KW   1};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_02030};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02030};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR600715-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215632};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_02030};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_02030};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_02030}.
FT   TRANSMEM        6..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT   TRANSMEM        42..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT   TRANSMEM        70..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT   TRANSMEM        98..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT   TRANSMEM        122..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT   TRANSMEM        155..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT   TRANSMEM        180..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT   TRANSMEM        210..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT   TRANSMEM        237..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT   TRANSMEM        291..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT   TRANSMEM        317..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02030"
FT   BINDING         150
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT   BINDING         214
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ   SEQUENCE   357 AA;  39236 MW;  26E339404057C06D CRC64;
     MDIFVAILIA FILSFIAVSA VNPIAVKVGL VDVPNARKRH SGNVPLVGGI AIFFAVIFEI
     VFYVDSGWQV DLYLLASTLV VTIGALDDRY DLKVSYRLLA QTLAALIMII GAGLYIDDLG
     DLLGFGIVEL GYGGVLFTIV AVMGGINAFN MVDGIDGLVG CLSLVSFSSL AFLLALVDSY
     WLFLPVFFMG AILAYLMFNL GWPSKKAKKI FMGDAGSMLI GFTVVWLLVV GTQEEEVAFH
     SVTALWIIAV PLMDMAAIMC RRMLKGESPF KPDRNHLHHI FIRAGFTSRQ ALLVITLTAS
     LLAMFGVAMQ LLEVKEWVSL SLFLSVFALY CWQLQYIWRA VSRIRRLLSR TGVQGAR
//
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