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ARNT_ECO27
ID   ARNT_ECO27              Reviewed;         550 AA.
AC   B7UFR9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 64.
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=E2348C_2401;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/jb.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA   Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA   Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
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; FM180568; CAS09949.1; -; Genomic_DNA.
DR   RefSeq; WP_000844015.1; NC_011601.1.
DR   AlphaFoldDB; B7UFR9; -.
DR   SMR; B7UFR9; -.
DR   CAZy; GT83; Glycosyltransferase Family 83.
DR   EnsemblBacteria; CAS09949; CAS09949; E2348C_2401.
DR   KEGG; ecg:E2348C_2401; -.
DR   HOGENOM; CLU_019200_2_1_6; -.
DR   OMA; TFWPGAP; -.
DR   UniPathway; UPA00037; -.
DR   Proteomes; UP000008205; 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..550
FT                   /note="Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-
FT                   arabinose arabinosyl transferase"
FT                   /id="PRO_0000379995"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT   TRANSMEM        81..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT   TRANSMEM        113..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT   TRANSMEM        134..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT   TRANSMEM        165..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT   TRANSMEM        204..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT   TRANSMEM        263..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT   TRANSMEM        288..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT   TRANSMEM        315..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT   TRANSMEM        346..366
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT   TRANSMEM        382..402
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT   TRANSMEM        406..426
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
SQ   SEQUENCE   550 AA;  62558 MW;  08F13317CEBD51A9 CRC64;
     MKSVRYLIGL FAFIACYYLL PISTRLLWQP DETRYAEISR EMLASGDWIV PHLLGLRYFE
     KPIAGYWINS IGQWLFGANN FGVRAGVIFA TLLTAALVTW FTLRLWRDKR LALLAAVIYL
     SLFIVYAIGT YAVLDPFIAF WLVAGMCSFW LAMQAQTWKG KSAGFLLLGI TCGMGVMTKG
     FLALAVPVLS VLPWVATQKR WKDLFIYGWL AVISCILTVL PWGLAIAQRE PDFWHYFFWV
     EHIQRFAMDD AQHRAPFWYY LPVIIAGSLP WLGLLPGALY AGWQNRKHSA TVYLLSWTIM
     PLLFFSVAKG KLPTYILSCF APLAMLMAHY ALLAAKNNPL ALRINGWINI AFGVTGIIAT
     FVVSPWGPMN TPVWQTFESY KVFCAWSIFS LWAFFGWYTL TNVEKTWPFA ALCPLGLALL
     VGFSIPDRVM EGKHPQFFVE MTQESLQPSR YILTDSVGVA AGLAWSLQRD DIIMYRQTGE
     LKYGLNYPDA KGRFVSGDEF ANWLNQHRQE GIITLVLSVD RDEDINSLAI PSADVIDRQE
     RLVLIQYRPK
 
 
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