ID   WECA_AERHY              Reviewed;         423 AA.
AC   B3FN88;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 2.
DT   03-AUG-2022, entry version 22.
DE   RecName: Full=UDP-N-acetylgalactosamine-undecaprenyl-phosphate N-acetylgalactosaminephosphotransferase;
DE            EC=2.7.8.40;
GN   Name=wecA;
OS   Aeromonas hydrophila.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=644;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AH-3;
RX   PubMed=18408022; DOI=10.1128/jb.00153-08;
RA   Jimenez N., Canals R., Salo M.T., Vilches S., Merino S., Tomas J.M.;
RT   "The Aeromonas hydrophila wb*O34 gene cluster: genetics and temperature
RT   regulation.";
RL   J. Bacteriol. 190:4198-4209(2008).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC   STRAIN=AH-3;
RX   PubMed=21335454; DOI=10.1128/jb.01441-10;
RA   Merino S., Jimenez N., Molero R., Bouamama L., Regue M., Tomas J.M.;
RT   "A UDP-HexNAc:polyprenol-P GalNAc-1-P transferase (WecP) representing a new
RT   subgroup of the enzyme family.";
RL   J. Bacteriol. 193:1943-1952(2011).
CC   -!- FUNCTION: Transfers N-acetyl-galactosamine (GalNAc) to undecaprenyl
CC       phosphate, a step in the assembly of the repeating-unit of the O-
CC       antigen. Shows no activity with UDP-N-acetyl-alpha-D-glucosamine.
CC       {ECO:0000269|PubMed:21335454}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-
CC         D-galactosamine = N-acetyl-alpha-D-galactosaminyl-di-trans,octa-cis-
CC         undecaprenyl diphosphate + UMP; Xref=Rhea:RHEA:36787,
CC         ChEBI:CHEBI:57865, ChEBI:CHEBI:60392, ChEBI:CHEBI:67138,
CC         ChEBI:CHEBI:74214; EC=2.7.8.40;
CC         Evidence={ECO:0000269|PubMed:21335454};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; LPS O-antigen
CC       biosynthesis. {ECO:0000269|PubMed:21335454}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the bacterial sugar transferase family.
CC       {ECO:0000305}.
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DR   EMBL; EU274663; ABX39510.2; -; Genomic_DNA.
DR   AlphaFoldDB; B3FN88; -.
DR   SMR; B3FN88; -.
DR   STRING; 1448139.AI20_04960; -.
DR   KEGG; ag:ABX39510; -.
DR   eggNOG; COG2148; Bacteria.
DR   BioCyc; MetaCyc:MON-18064; -.
DR   BRENDA; 2.7.8.40; 164.
DR   UniPathway; UPA00281; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IDA:UniProtKB.
DR   GO; GO:0009243; P:O antigen biosynthetic process; IDA:UniProtKB.
DR   InterPro; IPR003362; Bact_transf.
DR   InterPro; IPR017475; EPS_sugar_tfrase.
DR   Pfam; PF02397; Bac_transf; 1.
DR   TIGRFAMs; TIGR03025; EPS_sugtrans; 1.
PE   1: Evidence at protein level;
KW   Lipopolysaccharide biosynthesis; Membrane; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..423
FT                   /note="UDP-N-acetylgalactosamine-undecaprenyl-phosphate N-
FT                   acetylgalactosaminephosphotransferase"
FT                   /id="PRO_0000424131"
FT   TOPO_DOM        1..13
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        35..47
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        69..79
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        80..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        101..107
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        129..239
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        261..423
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   423 AA;  48850 MW;  2630DE22EF70EF44 CRC64;
     MSYQRRHSRW YERVLFSPPS LFFLGAMLAV CLPALERWGW GFWEYFDAVR VNTLGGAFVA
     FLLTGIVLYR FLRYPGASPV AYMIPTVTTL YGSLVGALFF LRLPYSRQVL FESYVVALLC
     CWVVYFIGRR YRTPKYALLP FGDYQPLMHH TCVEWRLLDK PDLGAVRYDA VVADLRDDDL
     AGEWERFLAR CALAHIPVYH IKQISETLTG RVKIDHLHEN QLGSLLPSPI YAFIKRGMDI
     LAAVIAIPLF SPLMLATAVL IKLESPGPVM FLQNRVGKGN RDFRIYKFRS MCQNSEQHGA
     QFAQDGDMRV TRVGKVIRKL RIDELPQFFN VLKGDMSLIG PRPEQRTFVD QFDREIPFYM
     YRHIVRPGIS GWAQVVHGYA ADADDTRIKI EHDFYYIKNF SLWLDVLIVF KTIRTILTGF
     GAR