EMBA_MYCLE
ID EMBA_MYCLE Reviewed; 1111 AA.
AC Q9CDA8;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Probable arabinosyltransferase A;
DE EC=2.4.2.-;
GN Name=embA; OrderedLocusNames=ML0105;
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; CAC29613.1; -; Genomic_DNA.
DR PIR; A86922; A86922.
DR RefSeq; NP_301202.1; NC_002677.1.
DR RefSeq; WP_010907527.1; NC_002677.1.
DR AlphaFoldDB; Q9CDA8; -.
DR SMR; Q9CDA8; -.
DR STRING; 272631.ML0105; -.
DR CAZy; GT53; Glycosyltransferase Family 53.
DR PRIDE; Q9CDA8; -.
DR EnsemblBacteria; CAC29613; CAC29613; CAC29613.
DR KEGG; mle:ML0105; -.
DR PATRIC; fig|272631.5.peg.166; -.
DR Leproma; ML0105; -.
DR eggNOG; COG1807; Bacteria.
DR HOGENOM; CLU_010182_0_0_11; -.
DR OMA; GWLHFRM; -.
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..1111
FT /note="Probable arabinosyltransferase A"
FT /id="PRO_0000220562"
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 205..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 333..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 370..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 394..413
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 462..484
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 530..547
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 554..576
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 581..603
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 615..637
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 652..674
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 695..717
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 804..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1111 AA; 118489 MW; 221AE71109D1FA08 CRC64;
MPHDGHEPPQ RIIRLIAVGA GITGLLLCAV VPLLPVKQTT ATIRWPQSAT RDGWVTQITA
PLVSGTPRAL DISIPCSAMA TLPDSVGLVV STLPSGGVDT GKSGLFVRAN KNAVVVAFRD
SVAAVAPRPA VAAGNCSVLH IWANTRGAGA NFVGIPGAAG ILTAEKKPQV GGIFTDLKVP
VQPGLSAHID IDTRFITAPT AIKKIAVGVG AAAVLIAILA LSALDRRNRN GHRLINWRVS
MAWLAQWRVI LATPPRAGGA SRIADGGVLA TLLLWHIIGA TSSDDGYNLT VARVSSEAGY
LANYYRYFGA TEAPFDWYFT VLAKLASVST AGVWMRIPAT LAGIACWLII NHWVLRRLGP
GTGGLSTNRV AVLTAGAMFL AAWLPFNNGL RPEPLIALGV LFTWVLVERA IALRRLASAA
TAAVVAILTA TLAPQGLIAI AALLTGARAI TQTIRRRRTT DGLLAPLLVL AASLSLITLV
VFHSQTLATV GESARIKYKV GPTIACYQDF LRYYFLTVES NADGSMTRRF PVLVLLLCMF
GVLVVLLRRS RVPGLASGPT WRLIGTTATS LLLLTFTPTK WAIQFGALAG LTGTFGAIAA
FAFARISLHT RRNLTVYITA LLFVLAWATA GINGWFGVSN YGVPWFDIQP VIAGHPVTSI
FLTLSILTGL LAGGQHFRLD YAKHTEVKDT RRNRFLATTP LVVVATTMVL CEVGSLAKGA
VARYPLYTTA KANLAALRSG LAPSVCAMAD DVLTEPDPNA GMLQPVPGQI FGPTGPLGGM
NPIGFKPEGV NDDLKSDPVV SKPGLVNSDA SPNKPNVTFS DSAGTAGGKG PVGVNGSHVA
LPFGLDPDRT PVMGSYGENT LAASATSAWY QLPLHWKESI ADRPLVVVSA AGAIWSYKED
GNFIYGQSLK LQWGVTRPDG IIQPLAQVMP IDIGPQPAWR NLRFPLTWAP PEANVARVVA
YDPNLSPDQW LAFTPPRVPV LQTLQQLLGS QTPVLMDIAT AANFPCQRPF SEHLGIAELP
QYRILPDHKQ TAASSNLWQS SEAGGPFLFL QALLRTSTIS TYLRDDWYRD WGSVEQYYRL
VPADQAPEAV VKQGMITVPG WIRRGPIRAL P
