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Database: UniProt
Entry: B2TW40
LinkDB: B2TW40
Original site: B2TW40 
ID   ARNT_SHIB3              Reviewed;         550 AA.
AC   B2TW40;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   29-OCT-2014, entry version 45.
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};
GN   OrderedLocusNames=SbBS512_E2633;
OS   Shigella boydii serotype 18 (strain CDC 3083-94 / BS512).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=344609;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 3083-94 / BS512;
RA   Rasko D.A., Rosovitz M., Maurelli A.T., Myers G., Seshadri R., Cer R.,
RA   Jiang L., Ravel J., Sebastian Y.;
RT   "Complete sequence of Shigella boydii serotype 18 strain BS512.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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: 4-amino-4-deoxy-alpha-L-arabinopyranosyl di-
CC       trans,octa-cis-undecaprenyl phosphate + lipid IV(A) = lipid II(A)
CC       + di-trans,octa-cis-undecaprenyl phosphate. {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; CP001063; ACD10073.1; -; Genomic_DNA.
DR   RefSeq; WP_000844032.1; NC_010658.1.
DR   RefSeq; YP_001881080.1; NC_010658.1.
DR   STRING; 344609.SbBS512_E2633; -.
DR   CAZy; GT83; Glycosyltransferase Family 83.
DR   EnsemblBacteria; ACD10073; ACD10073; SbBS512_E2633.
DR   GeneID; 6268944; -.
DR   KEGG; sbc:SbBS512_E2633; -.
DR   PATRIC; 18672313; VBIShiBoy129590_2916.
DR   eggNOG; COG1807; -.
DR   HOGENOM; HOG000273002; -.
DR   KO; K07264; -.
DR   OMA; GNWIAPH; -.
DR   OrthoDB; EOG6NKQWN; -.
DR   BioCyc; SBOY344609:GI0O-2632-MONOMER; -.
DR   UniPathway; UPA00037; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000030; F:mannosyltransferase activity; IEA:InterPro.
DR   GO; GO:0016763; F:transferase activity, transferring pentosyl groups; IEA:InterPro.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-HAMAP.
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.
DR   Pfam; PF02366; PMT; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Complete proteome;
KW   Glycosyltransferase; Lipid A biosynthesis; Lipid biosynthesis;
KW   Lipid metabolism; Lipopolysaccharide biosynthesis; Membrane;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN         1    550       Undecaprenyl phosphate-alpha-4-amino-4-
FT                                deoxy-L-arabinose arabinosyl transferase.
FT                                /FTId=PRO_0000380036.
FT   TRANSMEM      7     27       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01165}.
FT   TRANSMEM     81    101       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01165}.
FT   TRANSMEM    111    133       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01165}.
FT   TRANSMEM    137    154       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01165}.
FT   TRANSMEM    165    185       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01165}.
FT   TRANSMEM    204    224       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01165}.
FT   TRANSMEM    255    275       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01165}.
FT   TRANSMEM    288    308       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01165}.
FT   TRANSMEM    315    335       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01165}.
FT   TRANSMEM    346    366       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01165}.
FT   TRANSMEM    382    402       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01165}.
FT   TRANSMEM    406    426       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01165}.
SQ   SEQUENCE   550 AA;  62548 MW;  5A77BDADB66E981C CRC64;
     MKSVRYLIGL FAFIACYYLL PISTRLLWQP DETRYAEISR EMLASGDWIV PHLLGLRYFE
     KPIAGYWINS IGQWLFGANN FGVRAGVIFA TLLTAALVTW FTLRLWRDKR LALLATVIYL
     SLFIVYAIGT YAVLDPFIAF WLVAGMCSFW LAMQAQTWKG KSAGFLLLGI TCGMGVMTKG
     FLALAVPVLS VLPWVATQKR WKDLFIYGWL AVISCVLTVL PWGLAIAQRE PDFWHYFFWI
     EHIQRFALDD AQHRAPFWYY VPVIIAGSLP WLGLLPGALY TGWKNRKHSA TVYLLSWTIM
     PLLFFSVAKG KLPTYILSCF ASLAMLMAHY ALLAAKNNPL ALRINGWINI AFGVTGIIAT
     FVVSPWGPMN TPVWQTFESY KVFCAWSIFS LWAFFGWYTL TNVEKTWSFA ALCPLGLALL
     VGFSIPDRVM EGKHPQFFVE MTQESLQPSR YILTDSVGVA AGLAWSLQRD DIIMYRQTGE
     LKYGLNYPDA KGRFVSGDEF ANWLNQHRQE GIITLVLSVD RDEDINSLAI PPADAIDRQE
     RLVLIQYRPK
//
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