ID   ARNC_KLEP3              Reviewed;         327 AA.
AC   B5XTK8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 78.
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=KPK_0267;
OS   Klebsiella pneumoniae (strain 342).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=507522;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=342;
RX   PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA   Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA   Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA   Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA   Methe B.A.;
RT   "Complete genome sequence of the N2-fixing broad host range endophyte
RT   Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL   PLoS Genet. 4:E1000141-E1000141(2008).
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; CP000964; ACI11621.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5XTK8; -.
DR   SMR; B5XTK8; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   EnsemblBacteria; ACI11621; ACI11621; KPK_0267.
DR   KEGG; kpe:KPK_0267; -.
DR   HOGENOM; CLU_033536_0_0_6; -.
DR   OMA; NKNYGQT; -.
DR   OrthoDB; 1064289at2; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00036; UER00495.
DR   Proteomes; UP000001734; 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_1000137916"
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;  36782 MW;  224C45BC559F18A0 CRC64;
     MLTYPPVKKV SVVIPVYNEQ DSLPELLRRT DTACATLGRQ YEILLIDDGS SDDSARMLTE
     AAEAEGSHVV AVLLNRNYGQ HSAIMAGFSH VTGDLIITLD ADLQNPPEEI PRLVEKADEG
     YDVVGTVRQN RQDSIFRKSA SKMINRLIQR TTGKAMGDYG CMLRAYRRHI IDAMLNCHER
     STFIPILANT FARRAVEIPV MHAEREFGDS KYSFMRLINL MYDLVTCLTT TPLRLLSIFG
     SVIALLGFAF GLLLVVLRLA FGPQWAAEGV FMLFAVLFMF IGAQFIGMGL LGEYIGRIYN
     DVRARPRYFI QRVVRQPETA SKEEDRS