ARNC_PSEFS
ID ARNC_PSEFS Reviewed; 341 AA.
AC C3KAD3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 25-MAY-2022, entry version 89.
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=PFLU_3042;
OS Pseudomonas fluorescens (strain SBW25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=216595;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SBW25;
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; AM181176; CAY49271.1; -; Genomic_DNA.
DR RefSeq; WP_012724222.1; NC_012660.1.
DR AlphaFoldDB; C3KAD3; -.
DR SMR; C3KAD3; -.
DR STRING; 216595.PFLU_3042; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR EnsemblBacteria; CAY49271; CAY49271; PFLU_3042.
DR KEGG; pfs:PFLU_3042; -.
DR eggNOG; COG0463; Bacteria.
DR HOGENOM; CLU_033536_0_0_6; -.
DR OMA; NKNYGQT; -.
DR OrthoDB; 1064289at2; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00036; UER00495.
DR Proteomes; UP000002332; 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;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..341
FT /note="Undecaprenyl-phosphate 4-deoxy-4-formamido-L-
FT arabinose transferase"
FT /id="PRO_0000380269"
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 341 AA; 37725 MW; 1B70A9DA71EF1114 CRC64;
MKPYPIHCVS IVIPVYNEQE SLPELLRRTT AACKQLAYEY EIILVDDGSR DNSAQLLEDA
AAEDGSNVVA VILNRNYGQH AAIMAGFEQC RGDVVITLDA DLQNPPEEIP RLVEQAALGY
DVVATVRNNR QDSAFRRWPS RLINLAVQRS TGVAMTDYGC MLRAYRRTIV DAMLACRERS
TFIPILANGF ARHTTEILVH HAEREHGESK YSAMRLISLM FDLLTCMTTT PLRLLSIVGF
SLAALGMLFA FALIVMRLAF GADWAGDGLF VLFAVLFVFT GGQFIGMGLL GEYLGRMYSD
VRARPRFFIE KVLRNQPAAP APVVVVDGLV SSHTSTSADQ V
