ARNC_PROMH
ID ARNC_PROMH Reviewed; 326 AA.
AC B4ETL6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, 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=PMI1044;
OS Proteus mirabilis (strain HI4320).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=529507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI4320;
RX PubMed=18375554; DOI=10.1128/jb.01981-07;
RA Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA Parkhill J., Mobley H.L.T.;
RT "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT both adherence and motility.";
RL J. Bacteriol. 190:4027-4037(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; AM942759; CAR42270.1; -; Genomic_DNA.
DR RefSeq; WP_004242618.1; NC_010554.1.
DR AlphaFoldDB; B4ETL6; -.
DR SMR; B4ETL6; -.
DR STRING; 529507.PMI1044; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR EnsemblBacteria; CAR42270; CAR42270; PMI1044.
DR GeneID; 6799908; -.
DR KEGG; pmr:PMI1044; -.
DR eggNOG; COG0463; Bacteria.
DR HOGENOM; CLU_033536_0_0_6; -.
DR OMA; NKNYGQT; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00036; UER00495.
DR Proteomes; UP000008319; 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..326
FT /note="Undecaprenyl-phosphate 4-deoxy-4-formamido-L-
FT arabinose transferase"
FT /id="PRO_0000380262"
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 326 AA; 36752 MW; CF364F3917EAE364 CRC64;
MSTFEKINKV SVVIPVYNEE ESLPQLLERT IKSCKQLEQE YELILVDDGS SDNSAKMLEE
AANIEDNHVI AIILNRNYGQ HSAIMAGFNQ ADGDLVITLD ADLQNPPEEI PRLVATAEEG
YDVVGTRRRN RQDSWFRKTA SKMINAMITK ATGRSMGDYG CMLRAYRRHI IDAMLQCHER
STFIPILANT FARRTIEIEV AHAEREYGDS KYSFLKLINL MYDLLTCLTT APLRLLSVVG
SVIAVAGFLL AVLLIVLRLI FGAIWAADGV FTLFAILFMF IGAQFVAMGL LGEYIGRIYN
DVRARPRYFI QKVVGVKKPN KNQEED
