EMBC_MYCTO
ID EMBC_MYCTO Reviewed; 1094 AA.
AC P9WNL4; L0TF98; O08116; P72059;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 42.
DE RecName: Full=Probable arabinosyltransferase C;
DE EC=2.4.2.-;
GN Name=embC; OrderedLocusNames=MT3900;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000516; AAK48266.1; -; Genomic_DNA.
DR PIR; E70697; E70697.
DR RefSeq; WP_003917841.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WNL4; -.
DR SMR; P9WNL4; -.
DR CAZy; GT53; Glycosyltransferase Family 53.
DR EnsemblBacteria; AAK48266; AAK48266; MT3900.
DR KEGG; mtc:MT3900; -.
DR PATRIC; fig|83331.31.peg.4197; -.
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..1094
FT /note="Probable arabinosyltransferase C"
FT /id="PRO_0000427106"
FT TRANSMEM 28..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 431..453
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 466..488
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 530..552
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 565..582
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 586..608
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 620..642
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 657..679
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 700..722
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 817..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1094 AA; 117504 MW; BF8A57B3BCC5CDF9 CRC64;
MATEAAPPRI AVRLPSTSVR DAGANYRIAR YVAVVAGLLG AVLAIATPLL PVNQTTAQLN
WPQNGTFASV EAPLIGYVAT DLNITVPCQA AAGLAGSQNT GKTVLLSTVP KQAPKAVDRG
LLLQRANDDL VLVVRNVPLV TAPLSQVLGP TCQRLTFTAH ADRVAAEFVG LVQGPNAEHP
GAPLRGERSG YDFRPQIVGV FTDLAGPAPP GLSFSASVDT RYSSSPTPLK MAAMILGVAL
TGAALVALHI LDTADGMRHR RFLPARWWST GGLDTLVIAV LVWWHFVGAN TSDDGYILTM
ARVSEHAGYM ANYYRWFGTP EAPFGWYYDL LALWAHVSTA SIWMRLPTLA MALTCWWVIS
REVIPRLGHA VKTSRAAAWT AAGMFLAVWL PLDNGLRPEP IIALGILLTW CSVERAVATS
RLLPVAIACI IGALTLFSGP TGIASIGALL VAIGPLRTIL HRRSRRFGVL PLVAPILAAA
TVTAIPIFRD QTFAGEIQAN LLKRAVGPSL KWFDEHIRYE RLFMASPDGS IARRFAVLAL
VLALAVSVAM SLRKGRIPGT AAGPSRRIIG ITIISFLAMM FTPTKWTHHF GVFAGLAGSL
GALAAVAVTG AAMRSRRNRT VFAAVVVFVL ALSFASVNGW WYVSNFGVPW SNSFPKWRWS
LTTALLELTV LVLLLAAWFH FVANGDGRRT ARPTRFRARL AGIVQSPLAI ATWLLVLFEV
VSLTQAMISQ YPAWSVGRSN LQALAGKTCG LAEDVLVELD PNAGMLAPVT APLADALGAG
LSEAFTPNGI PADVTADPVM ERPGDRSFLN DDGLITGSEP GTEGGTTAAP GINGSRARLP
YNLDPARTPV LGSWRAGVQV PAMLRSGWYR LPTNEQRDRA PLLVVTAAGR FDSREVRLQW
ATDEQAAAGH HGGSMEFADV GAAPAWRNLR APLSAIPSTA TQVRLVADDQ DLAPQHWIAL
TPPRIPRVRT LQNVVGAADP LFLDWLVGLA FPCQRPFGHQ YGVDETPKWR ILPDRFGAEA
NSPVMDHNGG GPLGITELLM RATTVASYLK DDWFRDWGAL QRLTPYYPDA QPADLNLGTV
TRSGLWSPAP LRRG
