ARNC_PSEA8
ID ARNC_PSEA8 Reviewed; 339 AA.
AC B7VBN3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 80.
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=PLES_14801;
OS Pseudomonas aeruginosa (strain LESB58).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=557722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LESB58;
RX PubMed=19047519; DOI=10.1101/gr.086082.108;
RA Winstanley C., Langille M.G.I., Fothergill J.L., Kukavica-Ibrulj I.,
RA Paradis-Bleau C., Sanschagrin F., Thomson N.R., Winsor G.L., Quail M.A.,
RA Lennard N., Bignell A., Clarke L., Seeger K., Saunders D., Harris D.,
RA Parkhill J., Hancock R.E.W., Brinkman F.S.L., Levesque R.C.;
RT "Newly introduced genomic prophage islands are critical determinants of in
RT vivo competitiveness in the Liverpool epidemic strain of Pseudomonas
RT aeruginosa.";
RL Genome Res. 19:12-23(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; FM209186; CAW26208.1; -; Genomic_DNA.
DR RefSeq; WP_003112880.1; NC_011770.1.
DR AlphaFoldDB; B7VBN3; -.
DR SMR; B7VBN3; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR KEGG; pag:PLES_14801; -.
DR HOGENOM; CLU_033536_0_0_6; -.
DR OMA; DLVSGWK; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00036; UER00495.
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..339
FT /note="Undecaprenyl-phosphate 4-deoxy-4-formamido-L-
FT arabinose transferase"
FT /id="PRO_0000380264"
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 339 AA; 37296 MW; B045790966F26AC9 CRC64;
MKPYPIDLVS VVIPVYNEEA SLPELLRRTE AACLELGRAF EIVLVDDGSR DRSAELLQAA
AERDGSAVVA VILNRNYGQH AAILAGFEQS RGDLVITLDA DLQNPPEEIP RLVERAAQGY
DVVGSIRAER QDSAWRRWPS RLVNLAVQRS TGVAMHDYGC MLRAYRRSIV EAMLACRERS
TFIPILANGF ARHTCEIRVA HAERAHGESK YSAMRLLNLM FDLVTCMTTT PLRLLSLVGG
GMALAGFLFA LFLLVLRLAF GAAWAGNGLF VLFAVLFMFS GVQLLGMGLL GEYLGRMYSD
VRARPRFFIE RVVRATPSAL PSALQRAGFT SSSSEPSTP
