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Y1459_MYCTU
ID   Y1459_MYCTU             Reviewed;         591 AA.
AC   O53150; L0T9P4;
DT   09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Alpha-(1->6)-mannopyranosyltransferase Rv1459c;
DE            EC=2.4.1.-;
GN   OrderedLocusNames=Rv1459c;
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 [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   [2]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=18452585; DOI=10.1111/j.1365-2958.2008.06265.x;
RA   Mishra A.K., Alderwick L.J., Rittmann D., Wang C., Bhatt A.,
RA   Jacobs W.R. Jr., Takayama K., Eggeling L., Besra G.S.;
RT   "Identification of a novel alpha(1-->6) mannopyranosyltransferase MptB from
RT   Corynebacterium glutamicum by deletion of a conserved gene, NCgl1505,
RT   affords a lipomannan- and lipoarabinomannan-deficient mutant.";
RL   Mol. Microbiol. 68:1595-1613(2008).
RN   [3]
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).
CC   -!- FUNCTION: Catalyzes the addition of alpha-(1->6)-mannose residue.
CC       {ECO:0000269|PubMed:18452585}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:18452585}; Multi-
CC       pass membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the MptA/B family. {ECO:0000305}.
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DR   EMBL; AL123456; CCP44218.1; -; Genomic_DNA.
DR   PIR; F70871; F70871.
DR   RefSeq; NP_215975.1; NC_000962.3.
DR   AlphaFoldDB; O53150; -.
DR   STRING; 83332.Rv1459c; -.
DR   PaxDb; O53150; -.
DR   DNASU; 886585; -.
DR   GeneID; 886585; -.
DR   KEGG; mtu:Rv1459c; -.
DR   TubercuList; Rv1459c; -.
DR   eggNOG; ENOG5032QSS; Bacteria.
DR   OMA; MIVWALP; -.
DR   PhylomeDB; O53150; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Glycosyltransferase; Membrane; Reference proteome; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..591
FT                   /note="Alpha-(1->6)-mannopyranosyltransferase Rv1459c"
FT                   /id="PRO_0000420594"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        80..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        201..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        235..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        259..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        321..341
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        367..387
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        408..428
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        441..461
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        473..493
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        502..522
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        527..547
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          569..591
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   591 AA;  62693 MW;  B78B1B819529C57C CRC64;
     MAARHHTLSW SIASLHGDEQ AVGAPLTTTE LTALARTRLF GATGTVLMAI GALGAGARPV
     VQDPTFGVRL LNLPSRIQTV SLTMTTTGAV MMALAWLMLG RFTLGRRRMS RGKLDRTLLL
     WMLPLLIAPP MYSKDVYSYL AQSEIGRDGL DPYRVGPASG LGLGHVFTLS VPSLWRETPA
     PYGPLFLWIG RGISSLTGEN IVAAVLCHRL VVLIGVTLIV WATPRLAQRC GVAEVSALWL
     GAANPLLIMH LVAGIHNEAL MLGLMLTGVE FALRGLDMAN TPRPSPETWR LGPATIRASR
     RPELGASPRA GASRAVKPRP EWGPLAMLLA GSILITLSSQ VKLPSLLAMG FVTTVLAYRW
     GGNLRALLLA AAVMASLTLA IMAILGWASG LGFGWINTLG TANVVRSWMS PPTLLALGTG
     HVGILLGLGD HTTAVLSLTR AIGVLIITVM VCWLLLAVLR GRLHPIGGLG VALAVTVLLF
     PVVQPWYLLW AIIPLAAWAT RPGFRVAAIL ATLIVGIFGP TANGDRFALF QIVDATAASA
     IIVILLIALT YTRLPWRPLA AEQVVTAAES ASKTPATRRP TAAPDAYADS T
 
 
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