EMBB_MYCLE
ID EMBB_MYCLE Reviewed; 1083 AA.
AC Q9CDA9;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Probable arabinosyltransferase B;
DE EC=2.4.2.-;
GN Name=embB; OrderedLocusNames=ML0104;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
CC -!- FUNCTION: Arabinosyl transferase responsible for the polymerization of
CC arabinose into the arabinan of arabinogalactan. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the emb family. {ECO:0000305}.
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DR EMBL; AL583917; CAC29612.1; -; Genomic_DNA.
DR PIR; H86921; H86921.
DR RefSeq; NP_301201.1; NC_002677.1.
DR RefSeq; WP_010907526.1; NC_002677.1.
DR AlphaFoldDB; Q9CDA9; -.
DR SMR; Q9CDA9; -.
DR STRING; 272631.ML0104; -.
DR CAZy; GT53; Glycosyltransferase Family 53.
DR PRIDE; Q9CDA9; -.
DR EnsemblBacteria; CAC29612; CAC29612; CAC29612.
DR KEGG; mle:ML0104; -.
DR PATRIC; fig|272631.5.peg.165; -.
DR Leproma; ML0104; -.
DR eggNOG; COG1807; Bacteria.
DR HOGENOM; CLU_010182_0_0_11; -.
DR OMA; TPDYNAK; -.
DR Proteomes; UP000000806; 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:0052636; F:arabinosyltransferase activity; IEA:InterPro.
DR GO; GO:0071766; P:Actinobacterium-type cell wall biogenesis; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.610; -; 1.
DR Gene3D; 2.60.120.940; -; 1.
DR InterPro; IPR032731; Arabino_trans_C.
DR InterPro; IPR042486; Arabino_trans_C_2.
DR InterPro; IPR007680; Arabino_trans_central.
DR InterPro; IPR040920; Arabino_trans_N.
DR InterPro; IPR027451; EmbABC_dom1.
DR Pfam; PF14896; Arabino_trans_C; 1.
DR Pfam; PF17689; Arabino_trans_N; 1.
DR Pfam; PF04602; Arabinose_trans; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cell wall biogenesis/degradation; Glycosyltransferase;
KW Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1083
FT /note="Probable arabinosyltransferase B"
FT /id="PRO_0000220567"
FT TRANSMEM 23..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 421..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 456..478
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 525..542
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 555..572
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 576..598
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 611..633
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 648..670
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 690..712
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1083 AA; 117158 MW; 391009AF336F0DCF CRC64;
MSVIYRAHRV AIANRTASRN VRVARWVAAI AGLIGFVSSV VTPLLPVVQT TATLNWPQNG
QLNSVTAPLI SLTPVDITAT VPCAVVAALP PSGGVVLGTA PKQGKDANLN ALFIDVNSQR
VDVTDRNVVI LSVPRNQVAG DAGAPGCSSI EVTSTHAGTF ATFVGVTDSA GNPLRGGFPD
PNLRPQIVGV FTDLTGGAPS GLRLSATIDT RFSSTPTTLK RFAMMLAIIT TVGALVALWR
LDQLDGRRMR RLIPARWSMF TLVDVAVIFG FLLWHVIGAN SSDDGYQMQM ARTADHSGYM
ANYFRWFGSP EDPFGWYYNL LALMIHVSDA SMWIRLPDLI CGVACWLLLS REVLPRLGPA
IVGFKPALWA AGLVLLAAWM PFNNGLRPEG QIALGALITY VLIERAITYG RMTPVALATL
TAAFTIGIQP TGLIAVAALL AGGRPMLYIL VRRHRAVGAW PLVAPLLAAG TVVLTVVFAE
QTLSTVLEAT KVRTAIGPAQ AWYTENLRYY YLILPTVDGS LSRRFGFLIT ALCLFTAVLI
TLRRKQIPGV ARGPAWRLIG TILGTMFFLT FAPTKWVHHF GLFAALGAAV AALTTVLVSH
EVLRWSRNRM AFLAALLFVM TLCFATTNGW WYVSSYGVPF NSAMPRIDGI TFSTIFFILF
AIVALYAYYL HFTNTGHGEG RLIRTLTVSF WAPIPFAAGL MTLVFIGSMV AGIVRQYPTY
SNGWANIRAL TGGCGLADDV LVEPDSNAGY MTALPSNYGP LGPLGGVNAI GFTANGVPEH
TVAEAIRITP NQPGTDYDWE APTKLKAPGI NGSVVPLPYG LNPNKVPIAG TYTTGAQQQS
RLTSAWYQLP KPDDRHPLVV VTAAGKITGN SVLHGHTYGQ TVVLEYGDPG PNGGLVPAGR
LVPDDLYGEQ PKAWRNLRFA RSQMPFDAVA VRVVAENLSL TPEDWIAVTP PRVPELRSLQ
EYVGSSQPVL LDWEVGLAFP CQQPMLHANG VTDIPKFRIT PDYSAKKIDT DTWEDGANGG
LLGITDLLLR AHVMSTYLAR DWGRDWGSLR KFDPLVDTHP AQLDLDTATR SGWWSPGKIR
IKP
