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ARNT_SALEP
ID   ARNT_SALEP              Reviewed;         548 AA.
AC   B5R274;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=SEN2283;
OS   Salmonella enteritidis PT4 (strain P125109).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=550537;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P125109;
RX   PubMed=18583645; DOI=10.1101/gr.077404.108;
RA   Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA   Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA   Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA   Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA   Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA   Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA   Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT   "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT   gallinarum 287/91 provides insights into evolutionary and host adaptation
RT   pathways.";
RL   Genome Res. 18:1624-1637(2008).
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; AM933172; CAR33867.1; -; Genomic_DNA.
DR   RefSeq; WP_000978052.1; NC_011294.1.
DR   AlphaFoldDB; B5R274; -.
DR   SMR; B5R274; -.
DR   CAZy; GT83; Glycosyltransferase Family 83.
DR   KEGG; set:SEN2283; -.
DR   HOGENOM; CLU_019200_2_1_6; -.
DR   OMA; TFWPGAP; -.
DR   UniPathway; UPA00037; -.
DR   Proteomes; UP000000613; 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_0000380027"
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        404..424
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
SQ   SEQUENCE   548 AA;  61791 MW;  309656D80FA66992 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 FGIIGIVAAF
     VVSSWGPLKS PVWTHIETYK VFCVWGVFTV WAFVGWYSLC HSQQYLLPAF CPLGLALLFG
     FSIPDRVMES KQPQFFVEMT QAPLASSRYI LADNVGVAAG LAWSLKRDDI MLYGHAGELR
     YGLSYPDVQD KFVKADDFNA WLNQHRQEGI ITLVLSIAKD EDISALSLPP ADNVDYQGRL
     VLIQYRPK
 
 
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