ID RFAL_SALTY Reviewed; 404 AA. AC P26471; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 27-MAR-2024, entry version 113. DE RecName: Full=O-antigen ligase; GN Name=rfaL; Synonyms=rfbT, waaL; OrderedLocusNames=STM3713; OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=99287; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=LT2; RX PubMed=1657881; DOI=10.1128/jb.173.22.7151-7163.1991; RA Maclachlan P.R., Kadam S.K., Sanderson K.E.; RT "Cloning, characterization, and DNA sequence of the rfaLK region for RT lipopolysaccharide synthesis in Salmonella typhimurium LT2."; RL J. Bacteriol. 173:7151-7163(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LT2 / SGSC1412 / ATCC 700720; RX PubMed=11677609; DOI=10.1038/35101614; RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E., RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., RA Wilson R.K.; RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."; RL Nature 413:852-856(2001). CC -!- FUNCTION: Adds the O-antigen on the glucose(II) group of LPS. CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis. CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the O-antigen polymerase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M73826; AAA27206.1; -; Genomic_DNA. DR EMBL; AE006468; AAL22572.1; -; Genomic_DNA. DR PIR; B41317; B41317. DR RefSeq; NP_462613.1; NC_003197.2. DR RefSeq; WP_000958458.1; NC_003197.2. DR AlphaFoldDB; P26471; -. DR STRING; 99287.STM3713; -. DR PaxDb; 99287-STM3713; -. DR GeneID; 1255237; -. DR KEGG; stm:STM3713; -. DR PATRIC; fig|99287.12.peg.3927; -. DR HOGENOM; CLU_056701_0_0_6; -. DR BioCyc; MetaCyc:STM3713-MONOMER; -. DR BioCyc; SENT99287:STM3713-MONOMER; -. DR UniPathway; UPA00958; -. DR PHI-base; PHI:3726; -. DR PHI-base; PHI:6587; -. DR PHI-base; PHI:9592; -. DR Proteomes; UP000001014; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW. DR GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR007016; O-antigen_ligase-related. DR PANTHER; PTHR37422:SF16; O-ANTIGEN LIGASE; 1. DR PANTHER; PTHR37422; TEICHURONIC ACID BIOSYNTHESIS PROTEIN TUAE; 1. DR Pfam; PF04932; Wzy_C; 1. PE 3: Inferred from homology; KW Cell membrane; Ligase; Lipopolysaccharide biosynthesis; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1..404 FT /note="O-antigen ligase" FT /id="PRO_0000208067" FT TRANSMEM 66..84 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 184..203 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 227..244 FT /note="Helical" FT /evidence="ECO:0000255" SQ SEQUENCE 404 AA; 46034 MW; 1B84F7B3C757D2AB CRC64; MLTTSLTLNK EKWKPIWNKA LVFLFVATYF LDGITRYKHL IIILMVITAI YQVSRSPKSF PPLFKNSVFY SVAVLSLILV YSILISPDMK ESFKEFENTV LEGFLLYTLL IPVLLKDETK ETVAKIVLFS FLTSLGLRCL AESILYIEDY NKGIMPFISY AHRHMSDSMV FLFPALLNIW LFRKNAIKLV FLVLSAIYLF FILGTLSRGA WLAVLIVGVL WAILNRQWKL IGVGAILLAI IGALVITQHN NKPDPEHLLY KLQQTDSSYR YTNGTQGTAW ILIQENPIKG YGYGNDVYDG VYNKRVVDYP TWTFKESIGP HNTILYIWFS AGILGLASLV YLYGAIIRET ASSTLRKVEI SPYNAHLLLF LSFVGFYIVR GNFEQVDIAQ IGIITGFLLA LRNR //