ARNT_PHOLL
ID ARNT_PHOLL Reviewed; 553 AA.
AC Q7N3Q9;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase;
DE EC=2.4.2.43;
DE AltName: Full=4-amino-4-deoxy-L-arabinose lipid A transferase;
DE AltName: Full=Lipid IV(A) 4-amino-4-deoxy-L-arabinosyltransferase;
DE AltName: Full=Polymyxin resistance protein PmrK;
DE AltName: Full=Undecaprenyl phosphate-alpha-L-Ara4N transferase;
GN Name=arnT; Synonyms=pbgE, pmrK; OrderedLocusNames=plu2656;
OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS TT01).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=243265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15139 / CIP 105565 / TT01;
RX PubMed=14528314; DOI=10.1038/nbt886;
RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA Glaser P., Boemare N., Danchin A., Kunst F.;
RT "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT luminescens.";
RL Nat. Biotechnol. 21:1307-1313(2003).
RN [2]
RP REGULATION BY PHOP AND PHOQ.
RX PubMed=14973084; DOI=10.1128/jb.186.5.1270-1279.2004;
RA Derzelle S., Turlin E., Duchaud E., Pages S., Kunst F., Givaudan A.,
RA Danchin A.;
RT "The PhoP-PhoQ two-component regulatory system of Photorhabdus luminescens
RT is essential for virulence in insects.";
RL J. Bacteriol. 186:1270-1279(2004).
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 (By
CC similarity). {ECO:0000250}.
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;
CC -!- PATHWAY: Lipopolysaccharide metabolism; 4-amino-4-deoxy-beta-L-
CC arabinose-lipid A biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- INDUCTION: Activated by low magnesium concentrations, via the two-
CC component regulatory system PhoP/PhoQ.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 83 family.
CC {ECO:0000305}.
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DR EMBL; BX571867; CAE15030.1; -; Genomic_DNA.
DR RefSeq; WP_011146878.1; NC_005126.1.
DR AlphaFoldDB; Q7N3Q9; -.
DR SMR; Q7N3Q9; -.
DR STRING; 243265.plu2656; -.
DR CAZy; GT83; Glycosyltransferase Family 83.
DR PRIDE; Q7N3Q9; -.
DR EnsemblBacteria; CAE15030; CAE15030; plu2656.
DR GeneID; 24166002; -.
DR KEGG; plu:plu2656; -.
DR eggNOG; COG1807; Bacteria.
DR HOGENOM; CLU_019200_2_1_6; -.
DR OMA; TFWPGAP; -.
DR OrthoDB; 854536at2; -.
DR BioCyc; PLUM243265:PLU_RS13165-MON; -.
DR UniPathway; UPA00037; -.
DR Proteomes; UP000002514; 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 2: Evidence at transcript level;
KW Cell inner membrane; Cell membrane; Glycosyltransferase;
KW Lipid A biosynthesis; Lipid biosynthesis; Lipid metabolism;
KW Lipopolysaccharide biosynthesis; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..553
FT /note="Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-
FT arabinose arabinosyl transferase"
FT /id="PRO_0000121508"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 553 AA; 63917 MW; BF97A58E78A1A701 CRC64;
MLNNRACKVG AFLMALFFVI TYLLPLNGRL LWQPDETRYA EISREMLQRG DWIVPYLLDI
RYFEKPVAGY WINNISQWIF GDNNFAVRFG SVFCIFISAI LLYRLAMMMW HNRHIAFATS
LIYISMFLVF AIGTYSVLDP MFSLWVTAAM MCSFWGLKTD CTRRRIMAYL VLGLCCGMGF
MTKGFLALAV PVIVMLPIVI YQKRVLQIVC FGPLAIISAI AISLPWVIAI ALREPDYWHY
FFWVEHIKRF SSDDAQHIAP FWYYIPILIL GVIPWLGLLP GAVMKSWKER KSNPEMFFLL
CWFVVPLLFF SIAKGKLPTY ILPCMAPLAM MMAKFGVDCV KNGKMELLKI NGMVNVFLGL
LAVIVLFAME VVTKHALYQP SEWLKWVLAI VAFGIWGIIG YLCFALNGKY WLLAAFCSIV
VSLVIGHALP ENTVNSKLPQ NFIKLHHQEL AGSRYILSES VGLATSVAWE MKRSDIYMFE
RWGELEYGLN YPDSRYRYIS YKDFPQWLAK ARKEGRVSVL FHLYKDEKLP DLPKADQISR
NYRFAILVYE KQP
