ARNT1_PROMH
ID ARNT1_PROMH Reviewed; 548 AA.
AC B4EUL1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase 1 {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 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_01165};
GN Name=arnT1 {ECO:0000255|HAMAP-Rule:MF_01165}; OrderedLocusNames=PMI0275;
OS Proteus mirabilis (strain HI4320).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=529507;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI4320;
RX PubMed=18375554; DOI=10.1128/jb.01981-07;
RA Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA Parkhill J., Mobley H.L.T.;
RT "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT both adherence and motility.";
RL J. Bacteriol. 190:4027-4037(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; AM942759; CAR40745.1; -; Genomic_DNA.
DR RefSeq; WP_012367533.1; NC_010554.1.
DR AlphaFoldDB; B4EUL1; -.
DR SMR; B4EUL1; -.
DR STRING; 529507.PMI0275; -.
DR CAZy; GT83; Glycosyltransferase Family 83.
DR EnsemblBacteria; CAR40745; CAR40745; PMI0275.
DR GeneID; 6802481; -.
DR KEGG; pmr:PMI0275; -.
DR PATRIC; fig|529507.6.peg.265; -.
DR eggNOG; COG1807; Bacteria.
DR HOGENOM; CLU_019200_2_1_6; -.
DR OMA; DWITPWY; -.
DR UniPathway; UPA00037; -.
DR Proteomes; UP000008319; 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; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..548
FT /note="Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-
FT arabinose arabinosyl transferase 1"
FT /id="PRO_0000380013"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 89..109
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 180..200
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 214..234
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 292..312
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT TRANSMEM 347..367
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 405..425
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
SQ SEQUENCE 548 AA; 62263 MW; B7084221A0FD460C CRC64;
MNIAMTERYK WLLFFLFILL TYFIPLETRL LWQPDEIRYA EISREMLVSG NWSVPYLLDI
RYFEKPVLGY WINCIAQWLF GESHFAVRIV VVTSTLLTGW LIYKAAMVVW RNSALAFNAM
TVFLSSFLVL AIGTYNILDP IVTLFVTAAM YSFLVALSTP NKKGKIIAYM GIGFFCALGF
LTKGFIAVVL PALVFLVMAI SQARFKEVVC YSSIALLALA ITAGPWVITV ALQAPDYWNY
FFWVEHVQRF IAKESARSQP TWFYIPIVIL GVLPWLGFLF GALKSAFSLK KGTLYFLLWF
TLFFAFFSAS KGKLLTYMLP CFVPLSILIA HYIEELKDRP DEKISKVNAS INIAFGLMGI
SAVIYSLYSA KFALYDTNET LKIVLAISGF LFWSVIGAGA LFRQTQFLTM FCSIGLSLVI
GYAIPEKIES RSTPENIIQR YYEPLSNKSY LLTDEVGIGT SLAWGLKRTD IRLTETKGEL
AYGLNYPDVK NKYYSLEQLL ALIEANQYKG VAIVLVRPDR KQILTKLTTL KEKPIVEKEG
DLTLVFFN
