ID   EMBC_MYCLE              Reviewed;        1070 AA.
AC   Q9CDA7;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Probable arabinosyltransferase C;
DE            EC=2.4.2.-;
GN   Name=embC; OrderedLocusNames=ML0106;
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; CAC29614.1; -; Genomic_DNA.
DR   PIR; B86922; B86922.
DR   RefSeq; NP_301203.1; NC_002677.1.
DR   RefSeq; WP_010907528.1; NC_002677.1.
DR   AlphaFoldDB; Q9CDA7; -.
DR   SMR; Q9CDA7; -.
DR   STRING; 272631.ML0106; -.
DR   CAZy; GT53; Glycosyltransferase Family 53.
DR   EnsemblBacteria; CAC29614; CAC29614; CAC29614.
DR   KEGG; mle:ML0106; -.
DR   PATRIC; fig|272631.5.peg.169; -.
DR   Leproma; ML0106; -.
DR   eggNOG; COG1807; Bacteria.
DR   HOGENOM; CLU_010182_0_0_11; -.
DR   OMA; RPFGHQN; -.
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..1070
FT                   /note="Probable arabinosyltransferase C"
FT                   /id="PRO_0000220571"
FT   TRANSMEM        10..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        210..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        247..269
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        399..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        425..442
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        449..471
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        512..534
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        547..564
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        574..596
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        603..625
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        645..664
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        685..707
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1070 AA;  114755 MW;  46E10F02D49A93A3 CRC64;
     MSGAGANYWI ARLLAVIAGL LGALLAMATP FLPVNQNTAQ LNWPQNSTFE SVEAPLIGYV
     ATGLNVTVPC AAAAGLTGPQ SAGQTVLLST VPKQAPKAVD RGLLIQRAND DLVLVVRNVP
     VVSAPMSQVL SPACQRLTFA AYFDKITAEF VGLTYGPNAE HPGVPLRGER SGYDFRPQIV
     GVFTDLSGPI PTGLNFSATI DTRYSSSPTL LKTIAMILGV VLTIVALVAL HLLDTADGTQ
     HRRLLPSRWW SIGCLDGLVI TILAWWHFVG ANTSDDGYIL TMARVSEHAG YMANYYRWFG
     TPEAPFGWYY DLLALWAHVT TTSAWMRVPT LAMALTCWWL ISREVIPRLG HAAKASRAAA
     WTAAGMFLAV WLPLDNGLRP EPIIALGILL TWCSVERAVA TSRLLPVAVA CIVGALTLFS
     GPTGIASIGA LLVAVGPLLT ILQRRSKQFG AVPLVAPILA ASTVTAILIF RDQTFAGESQ
     ASLLKRAVGP SLKWFDEHIR YERLFMASPD GSVARRFAVL ALLVALSVAV AMSLRKGRIP
     GLAAGPSRRI IGITVTSFLA MMFTPTKWTH HFGVFAGLAG SLGALAAVAV ASAALRSRRN
     RTVFAAVVLF VVALSFASVN GWWYVSNFGV PWSNSFPKLR WSLTTALLEL TVIVLLLAAW
     FHFVATTNGS AKTRFGVRID RIVQSPIAIA TWSLVIFEVA SLTMAMIGQY PAWTVGKSNL
     QALTGQTCGL AEEVLVEQDP NAGMLLPVST PVADALGSSL AEAFTANGIP ADVSADPVME
     PPGDRSFVKE NGMTTGGEAG NEGGTNATPG INGSRAQLPY NLDPARTPVL GSWQSGIQVV
     ARLRSGWYRL PARDKAGPLL VVSAAGRFDH HEVKLQWATD SGAASGQPGG AFQFSDVGAS
     PAWRNLRLPL SAIPSMATQI RLVADDEDLA PQHWIALTPP RIPQLRTLQD VVGYQDPVFL
     DWLVGLAFPC QRPFDHQYGV DETPKWRILP DRFGAEANSP VMDNNGGGPL GVTELLLKAT
     TVASYLKDDW SRDWGALQRL TPYYPNAQPA RLSLGTTTRS GLWNPAPLRH