ID   ARNC_SERP5              Reviewed;         326 AA.
AC   A8GDR6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   25-MAY-2022, entry version 86.
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=Spro_2155;
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=399741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA   Vangronsveld J., van der Lelie D., Richardson P.;
RT   "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000826; ABV41256.1; -; Genomic_DNA.
DR   RefSeq; WP_012144887.1; NC_009832.1.
DR   AlphaFoldDB; A8GDR6; -.
DR   SMR; A8GDR6; -.
DR   STRING; 399741.Spro_2155; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   EnsemblBacteria; ABV41256; ABV41256; Spro_2155.
DR   KEGG; spe:Spro_2155; -.
DR   eggNOG; COG1215; Bacteria.
DR   HOGENOM; CLU_033536_0_0_6; -.
DR   OMA; NKNYGQT; -.
DR   OrthoDB; 1064289at2; -.
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..326
FT                   /note="Undecaprenyl-phosphate 4-deoxy-4-formamido-L-
FT                   arabinose transferase"
FT                   /id="PRO_1000065656"
FT   TRANSMEM        235..255
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;  36227 MW;  0FBAAE0E5976A69B CRC64;
     MSRVEPIKKV SVVIPVYNEQ ESLPALLERT TAACKQLTQP YEIILVDDGS SDNSADMLTA
     AAEQPGSCVI AVLLNRNYGQ HSAIMAGFNQ VSGDLVITLD ADLQNPPEEI PRLVKVAEEG
     YDVVGTVRAN RQDSWFRKSA SRIINMMIQR ATGKSMGDYG CMLRAYRRHI IEAMLNCHER
     STFIPILANT FARRTTEIEV LHAEREFGDS KYSLMKLINL MYDLITCLTT TPLRLLSVVG
     SVVALSGFLL AVLLIALRLI MGPEWSGGGV FTLFAVLFTF IGAQFVGMGL LGEYIGRIYT
     DVRARPRYFV QKVVGEQPNH NTQEEE