(data stored in ACNUC7421 zone)

SWISSPROT: ARNT2_PROMH

ID   ARNT2_PROMH             Reviewed;         553 AA.
AC   B4ETL9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   11-DEC-2019, entry version 73.
DE   RecName: Full=Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase 2 {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 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01165};
GN   Name=arnT2 {ECO:0000255|HAMAP-Rule:MF_01165}; OrderedLocusNames=PMI1047;
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 IV(A) = lipid II(A) + di-trans,octa-
CC         cis-undecaprenyl phosphate.; EC=2.4.2.43;
CC         Evidence={ECO:0000255|HAMAP-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}.
DR   EMBL; AM942759; CAR42273.1; -; Genomic_DNA.
DR   RefSeq; WP_012367836.1; NC_010554.1.
DR   STRING; 529507.PMI1047; -.
DR   CAZy; GT83; Glycosyltransferase Family 83.
DR   EnsemblBacteria; CAR42273; CAR42273; PMI1047.
DR   GeneID; 6802570; -.
DR   KEGG; pmr:PMI1047; -.
DR   PATRIC; fig|529507.6.peg.1013; -.
DR   eggNOG; ENOG4105SA9; Bacteria.
DR   eggNOG; COG1807; LUCA.
DR   HOGENOM; HOG000273002; -.
DR   KO; K07264; -.
DR   OMA; TFWPGAP; -.
DR   BioCyc; PMIR529507:G1GJY-1070-MONOMER; -.
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;
DR   PRODOM; B4ETL9.
DR   SWISS-2DPAGE; B4ETL9.
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..553
FT                   /note="Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-
FT                   arabinose arabinosyl transferase 2"
FT                   /id="PRO_1000137929"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT   TRANSMEM        115..135
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        178..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT   TRANSMEM        208..228
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT   TRANSMEM        261..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT   TRANSMEM        295..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT   TRANSMEM        317..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT   TRANSMEM        352..372
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT   TRANSMEM        386..406
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
FT   TRANSMEM        410..430
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01165"
SQ   SEQUENCE   553 AA;  63064 MW;  EA9B64AAE4EC1533 CRC64;
     MLNNRASKIG AILLALFFVL TYLFPLNSRL LWQPDETRYA EISREMVVSG NWIVPHMLDI
     RYFEKPIAGY WINNISQLIF GHTNFAVRFG SVISILLSAL LIYLLARMMW RNRQVAFVAS
     LIYLSMFLVF SVGTYSVLDP MLALWVTASM VCCFWALKAT TAKTRILAWI TLGLACGMAF
     MTKGFLALAI PVIVMIPVTL YQKQFTRMLL YGVLAVLSAA LISLPWVLAV AKAEPDYWHY
     FFWVEHIQRF SGDDAQHSSP FWYYIPIILL GVIPWLGLLP GALTSAWKKR RKRPELFFLL
     CWFVVPFLFF SIAKGKLPTY MLPFMGPLAM LMAKYGVDCA RKFKMKALRI NGYINIFIGV
     AAVVAILIIQ LVSSKPIYMP YEWSKWVLAI VAFSLWGIIG YLCSTLNGKH WLWAASCSLG
     VSLCIGQAIP NSSIDGKLPQ EFIRQNIDTL NASKYIVSNS VGVGAGLAWE LQRSDIYLYE
     RTGELTYGIE YPDSQHRLLK PESFEQWLEN ARKEGNVSVV ITYKDPKKLA QMPRPEELVT
     NRRMAILTYE KRK
//

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