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SUGC_MYCTU
ID   SUGC_MYCTU              Reviewed;         393 AA.
AC   P9WQI3; F2GFS4; L0T8T0; O50454; Q7D8J6;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=Trehalose import ATP-binding protein SugC;
DE            EC=7.5.2.-;
GN   Name=sugC; OrderedLocusNames=Rv1238;
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 IN TREHALOSE IMPORT, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21118978; DOI=10.1073/pnas.1014642108;
RA   Kalscheuer R., Weinrick B., Veeraraghavan U., Besra G.S., Jacobs W.R. Jr.;
RT   "Trehalose-recycling ABC transporter LpqY-SugA-SugB-SugC is essential for
RT   virulence of Mycobacterium tuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:21761-21766(2010).
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: Part of the ABC transporter complex LpqY-SugA-SugB-SugC,
CC       which is highly specific for uptake of trehalose. Involved in the
CC       recycling of extracellular trehalose released from trehalose-containing
CC       molecules synthesized by M.tuberculosis. Trehalose uptake is essential
CC       for virulence. Probably responsible for energy coupling to the
CC       transport system. {ECO:0000269|PubMed:21118978}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (SugC),
CC       two transmembrane proteins (Suga and SugB) and a solute-binding protein
CC       (LpqY). {ECO:0000305|PubMed:21118978}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC       protein {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Mutants show no growth on trehalose as the sole
CC       carbon and energy source, but grow normally on glucose. They secrete
CC       substantial amounts of trehalose during growth on glycerol.
CC       {ECO:0000269|PubMed:21118978}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; AL123456; CCP43994.1; -; Genomic_DNA.
DR   PIR; E70952; E70952.
DR   RefSeq; NP_215754.1; NC_000962.3.
DR   RefSeq; WP_003406299.1; NZ_NVQJ01000039.1.
DR   AlphaFoldDB; P9WQI3; -.
DR   SMR; P9WQI3; -.
DR   STRING; 83332.Rv1238; -.
DR   PaxDb; P9WQI3; -.
DR   DNASU; 887104; -.
DR   GeneID; 887104; -.
DR   KEGG; mtu:Rv1238; -.
DR   TubercuList; Rv1238; -.
DR   eggNOG; COG3842; Bacteria.
DR   OMA; SPKAFLM; -.
DR   PhylomeDB; P9WQI3; -.
DR   BioCyc; MetaCyc:G185E-5409-MON; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IBA:GO_Central.
DR   GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0051701; P:biological process involved in interaction with host; IMP:MTBBASE.
DR   GO; GO:0015771; P:trehalose transport; IDA:MTBBASE.
DR   CDD; cd03301; ABC_MalK_N; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR015855; ABC_transpr_MalK-like.
DR   InterPro; IPR008995; Mo/tungstate-bd_C_term_dom.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR040582; OB_MalK.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF17912; OB_MalK; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF50331; SSF50331; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW   Reference proteome; Sugar transport; Translocase; Transport.
FT   CHAIN           1..393
FT                   /note="Trehalose import ATP-binding protein SugC"
FT                   /id="PRO_0000419314"
FT   DOMAIN          4..235
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         37..44
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   393 AA;  42915 MW;  0152AA1F79F5A9D5 CRC64;
     MAEIVLDHVN KSYPDGHTAV RDLNLTIADG EFLILVGPSG CGKTTTLNMI AGLEDISSGE
     LRIAGERVNE KAPKDRDIAM VFQSYALYPH MTVRQNIAFP LTLAKMRKAD IAQKVSETAK
     ILDLTNLLDR KPSQLSGGQR QRVAMGRAIV RHPKAFLMDE PLSNLDAKLR VQMRGEIAQL
     QRRLGTTTVY VTHDQTEAMT LGDRVVVMYG GIAQQIGTPE ELYERPANLF VAGFIGSPAM
     NFFPARLTAI GLTLPFGEVT LAPEVQGVIA AHPKPENVIV GVRPEHIQDA ALIDAYQRIR
     ALTFQVKVNL VESLGADKYL YFTTESPAVH SVQLDELAEV EGESALHENQ FVARVPAESK
     VAIGQSVELA FDTARLAVFD ADSGANLTIP HRA
 
 
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