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ARNT_SHIFL
ID   ARNT_SHIFL              Reviewed;         550 AA.
AC   Q83KB6; Q7UC62;
DT   02-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 4.
DT   03-AUG-2022, entry version 111.
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=SF2336, S2469;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN43850.2; -; Genomic_DNA.
DR   EMBL; AE014073; AAP17669.1; -; Genomic_DNA.
DR   RefSeq; NP_708143.2; NC_004337.2.
DR   RefSeq; WP_000844002.1; NZ_WPGW01000032.1.
DR   AlphaFoldDB; Q83KB6; -.
DR   SMR; Q83KB6; -.
DR   STRING; 198214.SF2336; -.
DR   EnsemblBacteria; AAN43850; AAN43850; SF2336.
DR   EnsemblBacteria; AAP17669; AAP17669; S2469.
DR   GeneID; 1027765; -.
DR   GeneID; 58389478; -.
DR   KEGG; sfl:SF2336; -.
DR   KEGG; sfx:S2469; -.
DR   PATRIC; fig|198214.7.peg.2799; -.
DR   HOGENOM; CLU_019200_2_1_6; -.
DR   OMA; TFWPGAP; -.
DR   OrthoDB; 854536at2; -.
DR   UniPathway; UPA00037; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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..550
FT                   /note="Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-
FT                   arabinose arabinosyl transferase"
FT                   /id="PRO_0000121513"
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        111..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT   TRANSMEM        137..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        255..275
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;  62524 MW;  B32C3767EED556E6 CRC64;
     MKSVRYLIGI FAFIACYYLL PISTRLLWQP DETRYAEISR EMLASGDWIV PHLLGLRYFE
     KPIAGYWINS IGQWLFGANN FGVRAGVIFA TLLTAALVTW FTLRLWRDKR LALLATVIYL
     SLFIVYAIGT YAVLDPFIAF WLVAGMCSFW LAMQAQTWKG KSAGFLLLGI TCGMGVMTKG
     FLALAVPVLS VLPWVATQKR WKDLFIYGWL AVISCVLTVL PWGLAIAQRE PDFWHYFFWV
     EHIQRFALDD AQHRAPFWYY VPVIIAGSLP WLGLLPGALY TGWKNRKHSA TVYLLSWTIM
     PLLFFSVAKG KLPTYILSCF APLAMLLAHY ALLAAKNNPL ALRINGWINI AFGVTGIIAT
     FVISPWGPMN TPVWQTFESY KVFCAWSIFS LWAFFGWYTL TNVEKTWSFA ALCPLGLALL
     VGFSIPDRVM EGKHPQFFVE MTQESLQPSR YILTDSVGVA AGLAWSLQRD DIIMYRQTGE
     LKYGLNYPDA KGRFVSGDEF ANWLNQHRQE GIITLVLSVD RDEDINSLAI PPADAIVRQE
     RLVLIQYRPK
 
 
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