ARNC_PSEPF
ID ARNC_PSEPF Reviewed; 340 AA.
AC Q3KCC2;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase {ECO:0000255|HAMAP-Rule:MF_01164};
DE EC=2.4.2.53 {ECO:0000255|HAMAP-Rule:MF_01164};
DE AltName: Full=Undecaprenyl-phosphate Ara4FN transferase {ECO:0000255|HAMAP-Rule:MF_01164};
DE Short=Ara4FN transferase {ECO:0000255|HAMAP-Rule:MF_01164};
GN Name=arnC {ECO:0000255|HAMAP-Rule:MF_01164}; OrderedLocusNames=Pfl01_2842;
OS Pseudomonas fluorescens (strain Pf0-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=205922;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pf0-1;
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(2009).
CC -!- FUNCTION: Catalyzes the transfer of 4-deoxy-4-formamido-L-arabinose
CC from UDP to undecaprenyl phosphate. The modified arabinose is attached
CC to lipid A and is required for resistance to polymyxin and cationic
CC antimicrobial peptides. {ECO:0000255|HAMAP-Rule:MF_01164}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=di-trans,octa-cis-undecaprenyl phosphate + UDP-4-deoxy-4-
CC formamido-beta-L-arabinose = 4-deoxy-4-formamido-alpha-L-
CC arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + UDP;
CC Xref=Rhea:RHEA:27722, ChEBI:CHEBI:58223, ChEBI:CHEBI:58709,
CC ChEBI:CHEBI:58909, ChEBI:CHEBI:60392; EC=2.4.2.53;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01164};
CC -!- PATHWAY: Glycolipid biosynthesis; 4-amino-4-deoxy-alpha-L-arabinose
CC undecaprenyl phosphate biosynthesis; 4-amino-4-deoxy-alpha-L-arabinose
CC undecaprenyl phosphate from UDP-4-deoxy-4-formamido-beta-L-arabinose
CC and undecaprenyl phosphate: step 1/2. {ECO:0000255|HAMAP-
CC Rule:MF_01164}.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01164}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01164}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01164}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family.
CC {ECO:0000255|HAMAP-Rule:MF_01164}.
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DR EMBL; CP000094; ABA74583.1; -; Genomic_DNA.
DR RefSeq; WP_011334254.1; NC_007492.2.
DR AlphaFoldDB; Q3KCC2; -.
DR SMR; Q3KCC2; -.
DR STRING; 205922.Pfl01_2842; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR EnsemblBacteria; ABA74583; ABA74583; Pfl01_2842.
DR KEGG; pfo:Pfl01_2842; -.
DR eggNOG; COG0463; Bacteria.
DR HOGENOM; CLU_033536_0_0_6; -.
DR OMA; DLVSGWK; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00036; UER00495.
DR Proteomes; UP000002704; Chromosome.
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:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IEA:UniProtKB-UniRule.
DR GO; GO:0099621; F:undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0036108; P:4-amino-4-deoxy-alpha-L-arabinopyranosyl undecaprenyl phosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 3.90.550.10; -; 1.
DR HAMAP; MF_01164; ArnC_transfer; 1.
DR InterPro; IPR022857; ArnC_tfrase.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance; Cell inner membrane; Cell membrane;
KW Glycosyltransferase; Lipid A biosynthesis; Lipid biosynthesis;
KW Lipid metabolism; Lipopolysaccharide biosynthesis; Membrane; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..340
FT /note="Undecaprenyl-phosphate 4-deoxy-4-formamido-L-
FT arabinose transferase"
FT /id="PRO_0000380268"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01164"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01164"
SQ SEQUENCE 340 AA; 37391 MW; 022F9F62FC37648C CRC64;
MRPYPIHCVS IVIPVYNEED SLPELLRRTE AACKQLRHDY EIVLVDDGSR DASAQLLEEA
ASVVDSPFVA VILNRNYGQH AAIMAGFEQC KGDVVITLDA DLQNPPEEIP RLVAEAEKGF
DVVGTVRGNR QDSALRRYPS KLINLAVQRS TGVAMSDYGC MLRAYRRTII DAMLACRERS
TFIPILANSF ARHTTEIPVA HAEREHGDSK YSPMRLINLM FDLITCMTTT PLRLLSIVGF
AMAGLGVLFA AALIFMRLAF GAGWAGDGLF VLFAVLFVFT GGQFIGMGLL GEYLGRMYSD
VRARPRFFIE KVLRGHPATP APAITVDGLT SNSTSDQVLS
