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ARNC_ENT38
ID   ARNC_ENT38              Reviewed;         327 AA.
AC   A4WAM4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   25-MAY-2022, entry version 96.
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=Ent638_2078;
OS   Enterobacter sp. (strain 638).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=399742;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=638;
RX   PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA   Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA   Vangronsveld J., Newman L., Monchy S.;
RT   "Genome sequence of the plant growth promoting endophytic bacterium
RT   Enterobacter sp. 638.";
RL   PLoS Genet. 6:E1000943-E1000943(2010).
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; CP000653; ABP60754.1; -; Genomic_DNA.
DR   RefSeq; WP_012017469.1; NC_009436.1.
DR   AlphaFoldDB; A4WAM4; -.
DR   SMR; A4WAM4; -.
DR   STRING; 399742.Ent638_2078; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   EnsemblBacteria; ABP60754; ABP60754; Ent638_2078.
DR   KEGG; ent:Ent638_2078; -.
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; UP000000230; 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..327
FT                   /note="Undecaprenyl-phosphate 4-deoxy-4-formamido-L-
FT                   arabinose transferase"
FT                   /id="PRO_1000065654"
FT   TRANSMEM        236..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01164"
FT   TRANSMEM        270..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01164"
SQ   SEQUENCE   327 AA;  36648 MW;  08860041D9C984FB CRC64;
     MTKVEAIHKV SVVIPVYNEQ ESLPELIRRT TAACELLGKD YEILLVDDGS SDESASMLSD
     AAEEPGSHIV AVLLNRNYGQ HNAIMAGFSH VTGDLIVTLD ADLQNPPEEI PRLVAKADEG
     YDVVGTVRQN RQDTWFRKRA SRLINRLIQS TTGKAMGDYG CMLRAYRRHI IDAMLHCHER
     STFIPILANT FARKAIEIPV HHAEREFGES KYSFMRLINL MYDLVTCLTT TPLRMLSVFG
     SIIAVLGFTL SVLLVVLRIA FGPQWAADGV FMLFAVLFMF IGAQFVAMGL LGEYIGRIYT
     DVRARPRYFI QRVVSRGSVS TSKENQQ
 
 
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