ID   EMBB_MYCTO              Reviewed;        1098 AA.
AC   P9WNL6; L0TDT8; P72030; P72061;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 38.
DE   RecName: Full=Probable arabinosyltransferase B;
DE            EC=2.4.2.-;
GN   Name=embB; OrderedLocusNames=MT3902;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Arabinosyl transferase responsible for the polymerization of
CC       arabinose into the arabinan of arabinogalactan. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the emb family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK48268.1; -; Genomic_DNA.
DR   PIR; G70697; G70697.
DR   RefSeq; WP_003901728.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WNL6; -.
DR   SMR; P9WNL6; -.
DR   DrugCentral; P9WNL6; -.
DR   CAZy; GT53; Glycosyltransferase Family 53.
DR   EnsemblBacteria; AAK48268; AAK48268; MT3902.
DR   KEGG; mtc:MT3902; -.
DR   PATRIC; fig|83331.31.peg.4199; -.
DR   HOGENOM; CLU_010182_0_0_11; -.
DR   Proteomes; UP000001020; 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   GO; GO:0046677; P:response to antibiotic; 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   Antibiotic resistance; Cell membrane; Cell wall biogenesis/degradation;
KW   Glycosyltransferase; Membrane; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..1098
FT                   /note="Probable arabinosyltransferase B"
FT                   /id="PRO_0000427105"
FT   TRANSMEM        28..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        217..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        271..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        402..419
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        434..456
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        472..494
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        541..558
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        570..587
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        597..619
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        626..648
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        663..685
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        698..720
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1098 AA;  118021 MW;  DD7D7025DC803833 CRC64;
     MTQCASRRKS TPNRAILGAF ASARGTRWVA TIAGLIGFVL SVATPLLPVV QTTAMLDWPQ
     RGQLGSVTAP LISLTPVDFT ATVPCDVVRA MPPAGGVVLG TAPKQGKDAN LQALFVVVSA
     QRVDVTDRNV VILSVPREQV TSPQCQRIEV TSTHAGTFAN FVGLKDPSGA PLRSGFPDPN
     LRPQIVGVFT DLTGPAPPGL AVSATIDTRF STRPTTLKLL AIIGAIVATV VALIALWRLD
     QLDGRGSIAQ LLLRPFRPAS SPGGMRRLIP ASWRTFTLTD AVVIFGFLLW HVIGANSSDD
     GYILGMARVA DHAGYMSNYF RWFGSPEDPF GWYYNLLALM THVSDASLWM RLPDLAAGLV
     CWLLLSREVL PRLGPAVEAS KPAYWAAAMV LLTAWMPFNN GLRPEGIIAL GSLVTYVLIE
     RSMRYSRLTP AALAVVTAAF TLGVQPTGLI AVAALVAGGR PMLRILVRRH RLVGTLPLVS
     PMLAAGTVIL TVVFADQTLS TVLEATRVRA KIGPSQAWYT ENLRYYYLIL PTVDGSLSRR
     FGFLITALCL FTAVFIMLRR KRIPSVARGP AWRLMGVIFG TMFFLMFTPT KWVHHFGLFA
     AVGAAMAALT TVLVSPSVLR WSRNRMAFLA ALFFLLALCW ATTNGWWYVS SYGVPFNSAM
     PKIDGITVST IFFALFAIAA GYAAWLHFAP RGAGEGRLIR ALTTAPVPIV AGFMAAVFVA
     SMVAGIVRQY PTYSNGWSNV RAFVGGCGLA DDVLVEPDTN AGFMKPLDGD SGSWGPLGPL
     GGVNPVGFTP NGVPEHTVAE AIVMKPNQPG TDYDWDAPTK LTSPGINGST VPLPYGLDPA
     RVPLAGTYTT GAQQQSTLVS AWYLLPKPDD GHPLVVVTAA GKIAGNSVLH GYTPGQTVVL
     EYAMPGPGAL VPAGRMVPDD LYGEQPKAWR NLRFARAKMP ADAVAVRVVA EDLSLTPEDW
     IAVTPPRVPD LRSLQEYVGS TQPVLLDWAV GLAFPCQQPM LHANGIAEIP KFRITPDYSA
     KKLDTDTWED GTNGGLLGIT DLLLRAHVMA TYLSRDWARD WGSLRKFDTL VDAPPAQLEL
     GTATRSGLWS PGKIRIGP