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RGMG_RHIL3
ID   RGMG_RHIL3              Reviewed;         513 AA.
AC   Q1MAA2;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Putative ribose/galactose/methyl galactoside import ATP-binding protein {ECO:0000255|HAMAP-Rule:MF_01717};
DE            EC=7.5.2.11 {ECO:0000255|HAMAP-Rule:MF_01717};
DE            EC=7.5.2.7 {ECO:0000255|HAMAP-Rule:MF_01717};
GN   OrderedLocusNames=RL4654;
OS   Rhizobium leguminosarum bv. viciae (strain 3841).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=216596;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3841;
RX   PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA   Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F.,
RA   Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H.,
RA   East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach I.,
RA   Chillingworth T., Clarke K., Cronin A., Davis P., Fraser A., Hance Z.,
RA   Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA   Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.;
RT   "The genome of Rhizobium leguminosarum has recognizable core and accessory
RT   components.";
RL   Genome Biol. 7:R34.1-R34.20(2006).
CC   -!- FUNCTION: Part of an ABC transporter complex involved in carbohydrate
CC       import. Could be involved in ribose, galactose and/or methyl
CC       galactoside import. Responsible for energy coupling to the transport
CC       system. {ECO:0000255|HAMAP-Rule:MF_01717}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-ribose(out) + H2O = ADP + D-ribose(in) + H(+) +
CC         phosphate; Xref=Rhea:RHEA:29903, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:47013, ChEBI:CHEBI:456216; EC=7.5.2.7;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01717};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-galactose(out) + H2O = ADP + D-galactose(in) + H(+) +
CC         phosphate; Xref=Rhea:RHEA:60156, ChEBI:CHEBI:4139, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; EC=7.5.2.11; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01717};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01717}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01717}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Carbohydrate
CC       importer 2 (CUT2) (TC 3.A.1.2) family. {ECO:0000255|HAMAP-
CC       Rule:MF_01717}.
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DR   EMBL; AM236080; CAK10137.1; -; Genomic_DNA.
DR   RefSeq; WP_011653997.1; NC_008380.1.
DR   AlphaFoldDB; Q1MAA2; -.
DR   SMR; Q1MAA2; -.
DR   STRING; 216596.RL4654; -.
DR   EnsemblBacteria; CAK10137; CAK10137; RL4654.
DR   KEGG; rle:RL4654; -.
DR   eggNOG; COG1129; Bacteria.
DR   HOGENOM; CLU_000604_92_3_5; -.
DR   OMA; EGMAVIM; -.
DR   OrthoDB; 551294at2; -.
DR   Proteomes; UP000006575; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015611; F:ABC-type D-ribose transporter activity; IEA:RHEA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
DR   PROSITE; PS51260; MGLA; 1.
DR   PROSITE; PS51254; RBSA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Repeat; Sugar transport; Translocase; Transport.
FT   CHAIN           1..513
FT                   /note="Putative ribose/galactose/methyl galactoside import
FT                   ATP-binding protein"
FT                   /id="PRO_0000262989"
FT   DOMAIN          24..260
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01717"
FT   DOMAIN          270..510
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01717"
FT   BINDING         56..63
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01717"
SQ   SEQUENCE   513 AA;  56826 MW;  433EDD0B99D0300A CRC64;
     MAVSPTTMAA VRASGAVPNA EYLLSAEGVR KEFPGVVALD DVQFRLKRAS VHALMGENGA
     GKSTLMKILA GIYTPDKGDI RLKGIEIQLK SPLDALENGI AMIHQELNLM PFMTVAENIW
     IRREPKNRLG FIDHGVMHRM TEELFTRLNI AIDPDIEVRF LSVANRQMVE IAKAVSYNSD
     VLIMDEPTSA LTEREVEHLF RIIRDLKAQG IGIVYITHKM NELFEIADEF SVFRDGRYIG
     THASTDVTRD DIIRMMVGRE ITQMFPKEEV PIGEVMLSVK DLCLNGVFKN VSFEVRAGEI
     LGVAGLVGSG RSNVAETLFG VTPASSGSIE LYGKPVAISS PTEAIRNRMA FLTEDRKDTG
     CLLILDILEN MQIAVLQDRY VKGGFVQQGA VEATCEDMAK KLRVKTPNLY ERVENLSGGN
     QQKVLIGRWL LTNPRILILD EPTRGIDVGA KAEIHRLVTE MARDGVAVVM ISSEMPEVLG
     MSDRIMVMHE GRVTGFLNRD EATQIKVMEL AAQ
 
 
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