AMSG_ERWAM
ID AMSG_ERWAM Reviewed; 477 AA.
AC Q46628;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 2.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=UDP-galactose-lipid carrier transferase;
DE EC=2.-.-.-;
GN Name=amsG;
OS Erwinia amylovora (Fire blight bacteria).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=552;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=EA1/79;
RX PubMed=7596293; DOI=10.1111/j.1365-2958.1995.tb02361.x;
RA Bugert P., Geider K.;
RT "Molecular analysis of the ams operon required for exopolysaccharide
RT synthesis of Erwinia amylovora.";
RL Mol. Microbiol. 15:917-933(1995).
RN [2]
RP SEQUENCE REVISION TO 306 AND 333.
RA Geider K.K.;
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the biosynthesis of amylovoran which functions as
CC a virulence factor. May act as a sugar transferase and may be involved
CC in the export of the repeating unit by flipping the lipid carrier to
CC the periplasmic face of the inner membrane.
CC -!- PATHWAY: Glycan metabolism; exopolysaccharide biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the bacterial sugar transferase family.
CC {ECO:0000305}.
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DR EMBL; X77921; CAA54879.2; -; Genomic_DNA.
DR PIR; S61891; S61891.
DR RefSeq; WP_004158333.1; NZ_RQKG01000006.1.
DR AlphaFoldDB; Q46628; -.
DR SMR; Q46628; -.
DR GeneID; 8912412; -.
DR OMA; AGYINRY; -.
DR UniPathway; UPA00631; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR003362; Bact_transf.
DR InterPro; IPR017475; EPS_sugar_tfrase.
DR InterPro; IPR017472; Undecaprenyl-P_galact_Ptfrase.
DR Pfam; PF02397; Bac_transf; 1.
DR TIGRFAMs; TIGR03025; EPS_sugtrans; 1.
DR TIGRFAMs; TIGR03022; WbaP_sugtrans; 1.
PE 3: Inferred from homology;
KW Cell membrane; Exopolysaccharide synthesis; Membrane; Transferase;
KW Transmembrane; Transmembrane helix; Virulence.
FT CHAIN 1..477
FT /note="UDP-galactose-lipid carrier transferase"
FT /id="PRO_0000166462"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 305..477
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
SQ SEQUENCE 477 AA; 55074 MW; 8F86F82CD3B4E8B9 CRC64;
MREIEFTFKG LLIRLSLALS DLIFFNIALA LAIVLINGFP GEILTGIPQH ELDLKIATHI
LLSVICVGWF WVRLRHYTYR KPFWFELKEV FRTILIFSIV DLSVSALSKW ELSRWIWILT
WLLSMAMVPF GRACVKRLLN RKKLWKKQSI IIGSGKNAQE AWQALQSEEM MGFDVIAFYD
VDGSQTALEL FGVPVLKEEQ QLWSLVDSDT QFIVAVEYEQ SQSRDRWLKN LATHNCRSVS
VIPSLRGVPL YGTDMAYIFS HEVMILRVSN NLAKHSSRFL KRTFDLVGAL SIITLLLPAL
VILIFMVSRD GGAPIYGHER VGRDGRKFKC LKFRSMVVNS KEVLEEVLRT DPVARAEWDE
DFKLKNDPRI TRIGHFIRKT SLDELPQLWN VVRGEMSLVG PRPVIEAELE RYAGDVDYYF
MAKPGMTGLW QVSGRNDVSY ETRVYFDSWY VKNWSLWNDI AILFKTIGVV LKRDGAY
