ID   ARNC_WIGBR              Reviewed;         323 AA.
AC   Q8D342;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 99.
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=WIGBR1590;
OS   Wigglesworthia glossinidia brevipalpis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Wigglesworthia.
OX   NCBI_TaxID=36870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12219091; DOI=10.1038/ng986;
RA   Akman L., Yamashita A., Watanabe H., Oshima K., Shiba T., Hattori M.,
RA   Aksoy S.;
RT   "Genome sequence of the endocellular obligate symbiont of tsetse flies,
RT   Wigglesworthia glossinidia.";
RL   Nat. Genet. 32:402-407(2002).
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.
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 membrane {ECO:0000255|HAMAP-Rule:MF_01164};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01164}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01164}.
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DR   EMBL; BA000021; BAC24305.1; -; Genomic_DNA.
DR   RefSeq; WP_011069963.1; NC_004344.2.
DR   AlphaFoldDB; Q8D342; -.
DR   SMR; Q8D342; -.
DR   STRING; 36870.25166114; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   PRIDE; Q8D342; -.
DR   EnsemblBacteria; BAC24305; BAC24305; BAC24305.
DR   KEGG; wbr:b2254; -.
DR   eggNOG; COG0463; Bacteria.
DR   HOGENOM; CLU_033536_0_0_6; -.
DR   OMA; FCIAGYR; -.
DR   OrthoDB; 1064289at2; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00036; UER00495.
DR   Proteomes; UP000000562; 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 membrane; Glycosyltransferase;
KW   Lipid A biosynthesis; Lipid biosynthesis; Lipid metabolism;
KW   Lipopolysaccharide biosynthesis; Membrane; Reference proteome; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..323
FT                   /note="Undecaprenyl-phosphate 4-deoxy-4-formamido-L-
FT                   arabinose transferase"
FT                   /id="PRO_0000059205"
FT   TRANSMEM        238..258
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   323 AA;  37795 MW;  45E8E6D3A179F766 CRC64;
     MLNFKKLSII IPVYNEQDSL IELIKRTVNT CSKLKIKYEI IIIDDGSNDK SINILEKEAL
     KQNSKIVAIF LKKNYGQHSA IMAGFKHSSG DLVITMDADL QNPPEEIPKL ILNAEKGYDV
     IGTFRQNRKD NWFRKISSRL INIIIQIVIG KSMKDYGCML RAYNRNIINS ILEYNKKNIF
     IPILANTLSK NIIEIPVLHY EREFGCSKYN LIKLIKLIYD LFFCISFNLI KKNKMFNIFI
     ILIFLAVLMS IVFFFIFFLK IKLNIFYKIL FIPIIITLFL IKSFIIIILK ILIDIFFVKA
     KKNSIYYINK IIKNNFSKKK DVT