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ARNC_AERHH
ID   ARNC_AERHH              Reviewed;         326 AA.
AC   A0KGY7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=AHA_0991;
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC
OS   13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 / KCTC
RC   2358 / NCIMB 9240 / NCTC 8049;
RX   PubMed=16980456; DOI=10.1128/jb.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H.,
RA   Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA   Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
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; CP000462; ABK39590.1; -; Genomic_DNA.
DR   RefSeq; WP_011704926.1; NC_008570.1.
DR   RefSeq; YP_855537.1; NC_008570.1.
DR   AlphaFoldDB; A0KGY7; -.
DR   SMR; A0KGY7; -.
DR   STRING; 380703.AHA_0991; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   EnsemblBacteria; ABK39590; ABK39590; AHA_0991.
DR   KEGG; aha:AHA_0991; -.
DR   PATRIC; fig|380703.7.peg.995; -.
DR   eggNOG; COG0463; Bacteria.
DR   HOGENOM; CLU_033536_0_0_6; -.
DR   OMA; DLVSGWK; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00036; UER00495.
DR   Proteomes; UP000000756; 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_0000380259"
FT   TRANSMEM        234..254
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   326 AA;  36090 MW;  B467D2BE5078C6F8 CRC64;
     MNNTDIKLVS VVIPVYNEEA SLPALLSRVT AACDQLSQNY EVILIDDGSH DGSTELIRDA
     AAVEGSKLVG VLLNRNYGQH AAIMAGFETA KGDLVITLDA DLQNPPEEIP RLVEAAMQGY
     DVVGTMRRNR QDSWFRKTAS KLINKSVQKA TGVHMSDYGC MLRAYRRHII DAMLCCQERS
     TFIPILANSF ARRTIELEVG HAERAHGESK YGLMHLINLM YDLVTCMTTT PLRLLSIVGS
     VVAGIGFTFS ILLILMRLIL GADWAADGVF TLFAILFTFV GVQLLGMGLL GEYIGRMYTD
     VRARPRYFIH QIVRSATTPS QQEAEQ
 
 
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