RFAC_ECOLI
ID RFAC_ECOLI Reviewed; 319 AA.
AC P24173; P27376; Q2M7T5;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Lipopolysaccharide heptosyltransferase 1;
DE EC=2.-.-.-;
GN Name=rfaC; Synonyms=rfa-2, waaC, yibC; OrderedLocusNames=b3621, JW3596;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-24.
RC STRAIN=K12;
RX PubMed=8478319; DOI=10.1128/jb.175.9.2534-2540.1993;
RA Chen L., Coleman W.G. Jr.;
RT "Cloning and characterization of the Escherichia coli K-12 rfa-2 (rfaC)
RT gene, a gene required for lipopolysaccharide inner core synthesis.";
RL J. Bacteriol. 175:2534-2540(1993).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 264-319.
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).
CC -!- FUNCTION: Heptose transfer to the lipopolysaccharide core. It transfers
CC the innermost heptose to [4'-P](3-deoxy-D-manno-octulosonic acid)2-IVA.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 9 family. {ECO:0000305}.
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DR EMBL; M95398; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X62530; CAA44391.1; -; Genomic_DNA.
DR EMBL; U00039; AAB18598.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76645.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77671.1; -; Genomic_DNA.
DR PIR; A40619; A40619.
DR RefSeq; NP_418078.1; NC_000913.3.
DR RefSeq; WP_001264584.1; NZ_LN832404.1.
DR PDB; 2H1H; X-ray; 2.40 A; A/B=1-300.
DR PDBsum; 2H1H; -.
DR AlphaFoldDB; P24173; -.
DR SMR; P24173; -.
DR BioGRID; 4263304; 500.
DR IntAct; P24173; 17.
DR STRING; 511145.b3621; -.
DR BindingDB; P24173; -.
DR ChEMBL; CHEMBL4295576; -.
DR CAZy; GT9; Glycosyltransferase Family 9.
DR jPOST; P24173; -.
DR PaxDb; P24173; -.
DR PRIDE; P24173; -.
DR EnsemblBacteria; AAC76645; AAC76645; b3621.
DR EnsemblBacteria; BAE77671; BAE77671; BAE77671.
DR GeneID; 948136; -.
DR KEGG; ecj:JW3596; -.
DR KEGG; eco:b3621; -.
DR PATRIC; fig|1411691.4.peg.3085; -.
DR EchoBASE; EB1175; -.
DR eggNOG; COG0859; Bacteria.
DR HOGENOM; CLU_038371_6_0_6; -.
DR InParanoid; P24173; -.
DR OMA; ITHLAWA; -.
DR PhylomeDB; P24173; -.
DR BioCyc; EcoCyc:EG11189-MON; -.
DR BioCyc; MetaCyc:EG11189-MON; -.
DR BRENDA; 2.4.99.B6; 2026.
DR UniPathway; UPA00958; -.
DR EvolutionaryTrace; P24173; -.
DR PRO; PR:P24173; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008713; F:ADP-heptose-lipopolysaccharide heptosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008920; F:lipopolysaccharide heptosyltransferase activity; IDA:CACAO.
DR GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IMP:EcoCyc.
DR CDD; cd03789; GT9_LPS_heptosyltransferase; 1.
DR InterPro; IPR002201; Glyco_trans_9.
DR InterPro; IPR011908; LipoPS_heptosylTferase-I.
DR Pfam; PF01075; Glyco_transf_9; 1.
DR TIGRFAMs; TIGR02193; heptsyl_trn_I; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Glycosyltransferase;
KW Lipopolysaccharide biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..319
FT /note="Lipopolysaccharide heptosyltransferase 1"
FT /id="PRO_0000207260"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:2H1H"
FT HELIX 11..15
FT /evidence="ECO:0007829|PDB:2H1H"
FT HELIX 18..27
FT /evidence="ECO:0007829|PDB:2H1H"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:2H1H"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:2H1H"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:2H1H"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:2H1H"
FT HELIX 59..63
FT /evidence="ECO:0007829|PDB:2H1H"
FT TURN 64..67
FT /evidence="ECO:0007829|PDB:2H1H"
FT HELIX 69..83
FT /evidence="ECO:0007829|PDB:2H1H"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:2H1H"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:2H1H"
FT HELIX 97..102
FT /evidence="ECO:0007829|PDB:2H1H"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:2H1H"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:2H1H"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:2H1H"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:2H1H"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:2H1H"
FT HELIX 122..127
FT /evidence="ECO:0007829|PDB:2H1H"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:2H1H"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:2H1H"
FT HELIX 140..152
FT /evidence="ECO:0007829|PDB:2H1H"
FT HELIX 167..170
FT /evidence="ECO:0007829|PDB:2H1H"
FT TURN 175..178
FT /evidence="ECO:0007829|PDB:2H1H"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:2H1H"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:2H1H"
FT HELIX 196..206
FT /evidence="ECO:0007829|PDB:2H1H"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:2H1H"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:2H1H"
FT HELIX 220..230
FT /evidence="ECO:0007829|PDB:2H1H"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:2H1H"
FT HELIX 244..252
FT /evidence="ECO:0007829|PDB:2H1H"
FT STRAND 257..262
FT /evidence="ECO:0007829|PDB:2H1H"
FT HELIX 263..270
FT /evidence="ECO:0007829|PDB:2H1H"
FT STRAND 275..282
FT /evidence="ECO:0007829|PDB:2H1H"
FT HELIX 284..287
FT /evidence="ECO:0007829|PDB:2H1H"
FT STRAND 294..298
FT /evidence="ECO:0007829|PDB:2H1H"
SQ SEQUENCE 319 AA; 35544 MW; 31463CB533F33D33 CRC64;
MRVLIVKTSS MGDVLHTLPA LTDAQQAIPG IKFDWVVEEG FAQIPSWHAA VERVIPVAIR
RWRKAWFSAP IKAERKAFRE ALQAENYDAV IDAQGLVKSA ALVTRLAHGV KHGMDWQTAR
EPLASLFYNR KHHIAKQQHA VERTRELFAK SLGYSKPQTQ GDYAIAQHFL TNLPTDAGEY
AVFLHATTRD DKHWPEEHWR ELIGLLADSG IRIKLPWGAP HEEERAKRLA EGFAYVEVLP
KMSLEGVARV LAGAKFVVSV DTGLSHLTAA LDRPNITVYG PTDPGLIGGY GKNQMVCRAP
RENLINLNSQ AVLEKLSSL