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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}.
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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
 
 
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