ID E6WIX3_PANSA Unreviewed; 327 AA.
AC E6WIX3;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase {ECO:0000256|HAMAP-Rule:MF_01164};
DE EC=2.4.2.53 {ECO:0000256|HAMAP-Rule:MF_01164};
DE AltName: Full=Undecaprenyl-phosphate Ara4FN transferase {ECO:0000256|HAMAP-Rule:MF_01164};
DE Short=Ara4FN transferase {ECO:0000256|HAMAP-Rule:MF_01164};
GN Name=arnC {ECO:0000256|HAMAP-Rule:MF_01164};
GN OrderedLocusNames=Pat9b_5647 {ECO:0000313|EMBL:ADU71803.1};
OS Pantoea sp. (strain At-9b).
OG Plasmid pPAT9B01 {ECO:0000313|EMBL:ADU71803.1,
OG ECO:0000313|Proteomes:UP000001624}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=592316 {ECO:0000313|EMBL:ADU71803.1, ECO:0000313|Proteomes:UP000001624};
RN [1] {ECO:0000313|EMBL:ADU71803.1, ECO:0000313|Proteomes:UP000001624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=At-9b {ECO:0000313|Proteomes:UP000001624};
RC PLASMID=Plasmid pPAT9B01 {ECO:0000313|Proteomes:UP000001624};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pinto A., Currie C., Woyke T.;
RT "Complete sequence plasmid1 of Pantoea sp. At-9b.";
RL Submitted (DEC-2010) 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:0000256|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:0000256|HAMAP-Rule:MF_01164};
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis. {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_01164}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_01164}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01164}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family.
CC {ECO:0000256|HAMAP-Rule:MF_01164}.
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DR EMBL; CP002434; ADU71803.1; -; Genomic_DNA.
DR RefSeq; WP_013511632.1; NC_014838.1.
DR AlphaFoldDB; E6WIX3; -.
DR KEGG; pao:Pat9b_5647; -.
DR HOGENOM; CLU_033536_0_0_6; -.
DR OrthoDB; 9811884at2; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00036; UER00495.
DR Proteomes; UP000001624; Plasmid pPAT9B01.
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 CDD; cd04187; DPM1_like_bac; 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 PANTHER; PTHR48090:SF3; UNDECAPRENYL-PHOSPHATE 4-DEOXY-4-FORMAMIDO-L-ARABINOSE TRANSFERASE; 1.
DR PANTHER; PTHR48090; UNDECAPRENYL-PHOSPHATE 4-DEOXY-4-FORMAMIDO-L-ARABINOSE TRANSFERASE-RELATED; 1.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251, ECO:0000256|HAMAP-
KW Rule:MF_01164}; Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01164};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01164};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP-
KW Rule:MF_01164};
KW Lipid A biosynthesis {ECO:0000256|ARBA:ARBA00022556, ECO:0000256|HAMAP-
KW Rule:MF_01164};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_01164};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_01164};
KW Lipopolysaccharide biosynthesis {ECO:0000256|HAMAP-Rule:MF_01164};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_01164};
KW Plasmid {ECO:0000313|EMBL:ADU71803.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01164}; Transmembrane {ECO:0000256|HAMAP-Rule:MF_01164};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01164}.
FT TRANSMEM 242..265
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01164"
FT TRANSMEM 271..295
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01164"
FT DOMAIN 11..172
FT /note="Glycosyltransferase 2-like"
FT /evidence="ECO:0000259|Pfam:PF00535"
SQ SEQUENCE 327 AA; 36699 MW; C0F6E9D31AB286E0 CRC64;
MLEETPIRKV SVVIPVYNEE ESLPELVRRT HTACDLLNLE YEILLVDDGS SDRSGEMIAD
AADMPGSHVV GVLLNRNYGQ HSAIMAGFSH VSGDLIITLD ADLQNPPEEI PNLVAAAQQG
YDVVGTVRQN RQDSWFRRRA SRLINKLIQR VTGKAMGDYG CMLRAYRRHI VDAMLNCHER
STFIPILANT FARRTIELPV KHAEREFGDS KYSFMRLINL MYDLVTCLTT TPLRLLSVVG
SVIALAGFAF SLILIVLRLF LGAAWAGDGV FVLFAVLFMF IGAQFVGMGL LGEYIGRIYN
DVRARPRYFI QRVIHPHKNA SVQEIEQ
//
