ARNT_SALSV
ID ARNT_SALSV Reviewed; 548 AA.
AC B4TPI4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase {ECO:0000255|HAMAP-Rule:MF_01165};
DE EC=2.4.2.43 {ECO:0000255|HAMAP-Rule:MF_01165};
DE AltName: Full=4-amino-4-deoxy-L-arabinose lipid A transferase {ECO:0000255|HAMAP-Rule:MF_01165};
DE AltName: Full=Lipid IV(A) 4-amino-4-deoxy-L-arabinosyltransferase {ECO:0000255|HAMAP-Rule:MF_01165};
DE AltName: Full=Undecaprenyl phosphate-alpha-L-Ara4N transferase {ECO:0000255|HAMAP-Rule:MF_01165};
GN Name=arnT {ECO:0000255|HAMAP-Rule:MF_01165}; OrderedLocusNames=SeSA_A2529;
OS Salmonella schwarzengrund (strain CVM19633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=439843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CVM19633;
RX PubMed=21602358; DOI=10.1128/jb.00297-11;
RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA Leclerc J.E., Ravel J., Cebula T.A.;
RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT CRISPR-mediated adaptive sublineage evolution.";
RL J. Bacteriol. 193:3556-3568(2011).
CC -!- FUNCTION: Catalyzes the transfer of the L-Ara4N moiety of the
CC glycolipid undecaprenyl phosphate-alpha-L-Ara4N to lipid A. The
CC modified arabinose is attached to lipid A and is required for
CC resistance to polymyxin and cationic antimicrobial peptides.
CC {ECO:0000255|HAMAP-Rule:MF_01165}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,octa-cis-
CC undecaprenyl phosphate + lipid IVA = lipid IIA + di-trans,octa-cis-
CC undecaprenyl phosphate.; EC=2.4.2.43; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01165};
CC -!- PATHWAY: Lipopolysaccharide metabolism; 4-amino-4-deoxy-beta-L-
CC arabinose-lipid A biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01165}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01165}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01165}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 83 family.
CC {ECO:0000255|HAMAP-Rule:MF_01165}.
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DR EMBL; CP001127; ACF88928.1; -; Genomic_DNA.
DR RefSeq; WP_000978056.1; NC_011094.1.
DR AlphaFoldDB; B4TPI4; -.
DR SMR; B4TPI4; -.
DR CAZy; GT83; Glycosyltransferase Family 83.
DR EnsemblBacteria; ACF88928; ACF88928; SeSA_A2529.
DR KEGG; sew:SeSA_A2529; -.
DR HOGENOM; CLU_019200_2_1_6; -.
DR OMA; TFWPGAP; -.
DR UniPathway; UPA00037; -.
DR Proteomes; UP000001865; 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:0103015; F:4-amino-4-deoxy-L-arabinose transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000030; F:mannosyltransferase activity; IEA:InterPro.
DR GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006493; P:protein O-linked glycosylation; IEA:InterPro.
DR HAMAP; MF_01165; ArnT_transfer; 1.
DR InterPro; IPR022839; ArnT_tfrase.
DR InterPro; IPR003342; Glyco_trans_39/83.
DR Pfam; PF02366; PMT; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Glycosyltransferase;
KW Lipid A biosynthesis; Lipid biosynthesis; Lipid metabolism;
KW Lipopolysaccharide biosynthesis; Membrane; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..548
FT /note="Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-
FT arabinose arabinosyl transferase"
FT /id="PRO_0000380034"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 163..185
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 289..309
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
SQ SEQUENCE 548 AA; 61805 MW; 8FEA3F83ADFD8397 CRC64;
MMKSIRYYLA FAAFIALYYV IPVNSRLLWQ PDETRYAEIS REMLASGDWI VPHFLGLRYF
EKPIAGYWIN SLGQWLFGAT NFGVRAGAIL TTLLAAALVA WLTFRLWRDK RTALLASVIF
LSLFAVYSIG TYAVLDPMIA LWLTAGMCCF WQGMQATTRT GKIGMFLLLG ATCGLGVLTK
GFLALAVPVV SVLPWVIVQK RWKDFLLYGW LAVLSCFVVV LPWAIAIARR EADFWHYFFW
VEHIQRFAMS DAQHKAPFWY YLPVLLAGSL PWLGLLPGAL KLGWRERNGA FYLLGWTIMP
LLFFSIAKGK LPTYVLSCFA PIAILMARFV LHNVKEGVAA LRVNGGINLV FGLVGIVAAF
VVSSWGPLKS PVWTHIETYK VFCVWGVFTV WAFVGWYSLC HSQKYLLPAF CPLGLALLFG
FSVPDRVMES KQPQFFVEMT QAPLASSRYI LVDNVGVAAG LAWSLKRDDI MLYGHAGELR
YGLSYPDVQD KFVKADDFNA WLNQHRQEGI ITLVLSIAKD EDISALSLPP ADNIDYQGRL
VLIQYRPK
