EMBC_MYCTU
ID EMBC_MYCTU Reviewed; 1094 AA.
AC P9WNL5; L0TF98; O08116; P72059;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Probable arabinosyltransferase C;
DE EC=2.4.2.-;
GN Name=embC; OrderedLocusNames=Rv3793; ORFNames=MTCY13D12.27;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9142129; DOI=10.1038/nm0597-567;
RA Telenti A., Philipp W.J., Sreevatsan S., Bernasconi C., Stockbauer K.E.,
RA Wieles B., Musser J.M., Jacobs W.R. Jr.;
RT "The emb operon, a gene cluster of Mycobacterium tuberculosis involved in
RT resistance to ethambutol.";
RL Nat. Med. 3:567-570(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [3]
RP INDUCTION.
RX PubMed=16585755; DOI=10.1128/jb.188.8.2936-2944.2006;
RA Sharma K., Gupta M., Pathak M., Gupta N., Koul A., Sarangi S., Baweja R.,
RA Singh Y.;
RT "Transcriptional control of the mycobacterial embCAB operon by PknH through
RT a regulatory protein, EmbR, in vivo.";
RL J. Bacteriol. 188:2936-2944(2006).
RN [4]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [6]
RP VARIANTS EMB RESISTANT ASP-394 AND GLN-738.
RX PubMed=10639358; DOI=10.1128/aac.44.2.326-336.2000;
RA Ramaswamy S.V., Amin A.G., Goeksel S., Stager C.E., Dou S.-J., El Sahly H.,
RA Moghazeh S.L., Kreiswirth B.N., Musser J.M.;
RT "Molecular genetic analysis of nucleotide polymorphisms associated with
RT ethambutol resistance in human isolates of Mycobacterium tuberculosis.";
RL Antimicrob. Agents Chemother. 44:326-336(2000).
CC -!- FUNCTION: Arabinosyl transferase responsible for the polymerization of
CC arabinose into the arabinan of arabinogalactan.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Positively regulated by the transcriptional regulatory
CC protein EmbR. {ECO:0000269|PubMed:16585755}.
CC -!- MISCELLANEOUS: This is one of the targets of the anti-tuberculosis drug
CC ethambutol [(S,S')-2,2'-(ethylenediimino)di-1-butanol; EMB]. EMB is a
CC first-line drug used to treat tuberculosis. EMB inhibits the transfer
CC of arabinogalactan into the cell wall.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
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; U68480; AAC45279.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP46622.1; -; Genomic_DNA.
DR PIR; E70697; E70697.
DR RefSeq; NP_218310.1; NC_000962.3.
DR RefSeq; WP_003901726.1; NZ_NVQJ01000009.1.
DR PDB; 3PTY; X-ray; 2.00 A; A=719-1094.
DR PDBsum; 3PTY; -.
DR AlphaFoldDB; P9WNL5; -.
DR SMR; P9WNL5; -.
DR STRING; 83332.Rv3793; -.
DR DrugBank; DB00330; Ethambutol.
DR DrugCentral; P9WNL5; -.
DR CAZy; GT53; Glycosyltransferase Family 53.
DR TCDB; 9.B.364.1.5; the putative arabinosyltransferase b (aratb) family.
DR PaxDb; P9WNL5; -.
DR GeneID; 886112; -.
DR KEGG; mtu:Rv3793; -.
DR TubercuList; Rv3793; -.
DR eggNOG; COG1807; Bacteria.
DR OMA; RPFGHQN; -.
DR PhylomeDB; P9WNL5; -.
DR BioCyc; MetaCyc:G185E-8089-MON; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
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; IMP:MTBBASE.
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:0009247; P:glycolipid biosynthetic process; IMP:MTBBASE.
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 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Cell membrane;
KW Cell wall biogenesis/degradation; Glycosyltransferase; Membrane;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..1094
FT /note="Probable arabinosyltransferase C"
FT /id="PRO_0000220573"
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"
FT VARIANT 394
FT /note="N -> D (resistance to EMB)"
FT /evidence="ECO:0000269|PubMed:10639358"
FT VARIANT 738
FT /note="R -> Q (resistance to EMB)"
FT /evidence="ECO:0000269|PubMed:10639358"
FT HELIX 736..746
FT /evidence="ECO:0007829|PDB:3PTY"
FT HELIX 750..753
FT /evidence="ECO:0007829|PDB:3PTY"
FT STRAND 755..759
FT /evidence="ECO:0007829|PDB:3PTY"
FT HELIX 761..764
FT /evidence="ECO:0007829|PDB:3PTY"
FT STRAND 768..771
FT /evidence="ECO:0007829|PDB:3PTY"
FT HELIX 773..776
FT /evidence="ECO:0007829|PDB:3PTY"
FT STRAND 779..784
FT /evidence="ECO:0007829|PDB:3PTY"
FT HELIX 845..847
FT /evidence="ECO:0007829|PDB:3PTY"
FT STRAND 856..858
FT /evidence="ECO:0007829|PDB:3PTY"
FT STRAND 862..865
FT /evidence="ECO:0007829|PDB:3PTY"
FT STRAND 881..889
FT /evidence="ECO:0007829|PDB:3PTY"
FT HELIX 893..895
FT /evidence="ECO:0007829|PDB:3PTY"
FT STRAND 896..901
FT /evidence="ECO:0007829|PDB:3PTY"
FT HELIX 903..907
FT /evidence="ECO:0007829|PDB:3PTY"
FT STRAND 912..916
FT /evidence="ECO:0007829|PDB:3PTY"
FT STRAND 918..921
FT /evidence="ECO:0007829|PDB:3PTY"
FT STRAND 923..925
FT /evidence="ECO:0007829|PDB:3PTY"
FT STRAND 927..932
FT /evidence="ECO:0007829|PDB:3PTY"
FT HELIX 933..935
FT /evidence="ECO:0007829|PDB:3PTY"
FT STRAND 942..949
FT /evidence="ECO:0007829|PDB:3PTY"
FT STRAND 958..960
FT /evidence="ECO:0007829|PDB:3PTY"
FT HELIX 971..975
FT /evidence="ECO:0007829|PDB:3PTY"
FT TURN 976..978
FT /evidence="ECO:0007829|PDB:3PTY"
FT STRAND 979..982
FT /evidence="ECO:0007829|PDB:3PTY"
FT HELIX 985..988
FT /evidence="ECO:0007829|PDB:3PTY"
FT STRAND 994..996
FT /evidence="ECO:0007829|PDB:3PTY"
FT HELIX 1000..1002
FT /evidence="ECO:0007829|PDB:3PTY"
FT STRAND 1009..1012
FT /evidence="ECO:0007829|PDB:3PTY"
FT TURN 1036..1039
FT /evidence="ECO:0007829|PDB:3PTY"
FT STRAND 1040..1049
FT /evidence="ECO:0007829|PDB:3PTY"
FT STRAND 1059..1065
FT /evidence="ECO:0007829|PDB:3PTY"
SQ SEQUENCE 1094 AA; 117490 MW; AF8190BE0A1EA05E 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 VFLDWLVGLA FPCQRPFGHQ YGVDETPKWR ILPDRFGAEA
NSPVMDHNGG GPLGITELLM RATTVASYLK DDWFRDWGAL QRLTPYYPDA QPADLNLGTV
TRSGLWSPAP LRRG