RFAL_ECOLI
ID RFAL_ECOLI Reviewed; 419 AA.
AC P27243; Q2M7T6;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=O-antigen ligase;
GN Name=rfaL; Synonyms=waaL; OrderedLocusNames=b3622, JW3597;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1624462; DOI=10.1128/jb.174.14.4746-4752.1992;
RA Klena J.D., Pradel E., Schnaitman C.A.;
RT "Comparison of lipopolysaccharide biosynthesis genes rfaK, rfaL, rfaY, and
RT rfaZ of Escherichia coli K-12 and Salmonella typhimurium.";
RL J. Bacteriol. 174:4746-4752(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP SUBCELLULAR LOCATION, AND TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [6]
RP INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=30837344; DOI=10.1128/mbio.02819-18;
RA Weaver J., Mohammad F., Buskirk A.R., Storz G.;
RT "Identifying small proteins by ribosome profiling with stalled initiation
RT complexes.";
RL MBio 10:0-0(2019).
CC -!- FUNCTION: Adds the O-antigen on the glucose group of LPS.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:15919996}.
CC -!- INDUCTION: Expressed in both exponetial and stationary phase in rich
CC medium (at protein level). {ECO:0000269|PubMed:30837344}.
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; M95398; AAA24524.1; -; Genomic_DNA.
DR EMBL; U00039; AAB18599.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76646.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77670.1; -; Genomic_DNA.
DR PIR; S47843; S47843.
DR RefSeq; NP_418079.1; NC_000913.3.
DR RefSeq; WP_001395405.1; NZ_LN832404.1.
DR AlphaFoldDB; P27243; -.
DR BioGRID; 4263298; 155.
DR DIP; DIP-10673N; -.
DR IntAct; P27243; 1.
DR STRING; 511145.b3622; -.
DR TCDB; 9.B.67.5.1; the o-antigen polymerase (oap) family.
DR PaxDb; P27243; -.
DR PRIDE; P27243; -.
DR EnsemblBacteria; AAC76646; AAC76646; b3622.
DR EnsemblBacteria; BAE77670; BAE77670; BAE77670.
DR GeneID; 948148; -.
DR KEGG; ecj:JW3597; -.
DR KEGG; eco:b3622; -.
DR PATRIC; fig|1411691.4.peg.3084; -.
DR EchoBASE; EB1394; -.
DR eggNOG; COG3307; Bacteria.
DR HOGENOM; CLU_054167_0_0_6; -.
DR OMA; MLIAWLM; -.
DR BioCyc; EcoCyc:EG11424-MON; -.
DR BioCyc; MetaCyc:EG11424-MON; -.
DR UniPathway; UPA00958; -.
DR PHI-base; PHI:3106; -.
DR PRO; PR:P27243; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0016757; F:glycosyltransferase activity; IMP:EcoCyc.
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 Pfam; PF04932; Wzy_C; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Ligase;
KW Lipopolysaccharide biosynthesis; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..419
FT /note="O-antigen ligase"
FT /id="PRO_0000097284"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..105
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..168
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..193
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..241
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..346
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 368..369
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 412..419
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT CONFLICT 205..224
FT /note="VLYVLALTQTRATLLLFPII -> GTLCSGANTNQSNPTPVPYN (in
FT Ref. 1; AAA24524)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="R -> T (in Ref. 1; AAA24524)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="A -> R (in Ref. 1; AAA24524)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 419 AA; 46878 MW; E15382BD2CC70533 CRC64;
MLTSFKLHSL KPYTLKSSMI LEIITYILCF FSMIIAFVDN TFSIKIYNIT AIVCLLSLIL
RGRQENYNIK NLILPLSIFL IGLLDLIWYS AFKVDNSPFR ATYHSYLNTA KIFIFGSFIV
FLTLTSQLKS KKESVLYTLY SLSFLIAGYA MYINSIHEND RISFGVGTAT GAAYSTMLIG
IVSGVAILYT KKNHPFLFLL NSCAVLYVLA LTQTRATLLL FPIICVAALI AYYNKSPKKF
TSSIVLLIAI LASIVIIFNK PIQNRYNEAL NDLNSYTNAN SVTSLGARLA MYEIGLNIFI
KSPFSFRSAE SRAESMNLLV AEHNRLRGAL EFSNVHLHNE IIEAGSLKGL MGIFSTLFLY
FSLFYIAYKK RALGLLILTL GIVGIGLSDV IIWARSIPII IISAIVLLLV INNRNNTIN
