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NDVA_RHOP5
ID   NDVA_RHOP5              Reviewed;         602 AA.
AC   Q07QX6;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Beta-(1-->2)glucan export ATP-binding/permease protein NdvA {ECO:0000255|HAMAP-Rule:MF_01728};
DE            EC=7.5.2.3 {ECO:0000255|HAMAP-Rule:MF_01728};
GN   Name=ndvA {ECO:0000255|HAMAP-Rule:MF_01728}; OrderedLocusNames=RPE_1709;
OS   Rhodopseudomonas palustris (strain BisA53).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisA53;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Kim E., Harwood C.S., Oda Y.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisA53.";
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in Beta-(1-->2)glucan export. Transmembrane domains
CC       (TMD) form a pore in the inner membrane and the ATP-binding domain
CC       (NBD) is responsible for energy generation. {ECO:0000255|HAMAP-
CC       Rule:MF_01728}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->2)-beta-D-glucosyl](n)(in) + ATP + H2O = [(1->2)-beta-D-
CC         glucosyl](n)(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:18453,
CC         Rhea:RHEA-COMP:11881, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:27517, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; EC=7.5.2.3; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01728};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01728}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01728}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01728}.
CC   -!- DOMAIN: In NdvA the ATP-binding domain (NBD) and the transmembrane
CC       domain (TMD) are fused.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Beta-
CC       (1-->2)glucan exporter (TC 3.A.1.108.1) family. {ECO:0000255|HAMAP-
CC       Rule:MF_01728}.
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DR   EMBL; CP000463; ABJ05658.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q07QX6; -.
DR   SMR; Q07QX6; -.
DR   STRING; 316055.RPE_1709; -.
DR   EnsemblBacteria; ABJ05658; ABJ05658; RPE_1709.
DR   KEGG; rpe:RPE_1709; -.
DR   eggNOG; COG1132; Bacteria.
DR   HOGENOM; CLU_000604_84_1_5; -.
DR   OMA; MPVLSWW; -.
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:0015441; F:ABC-type beta-glucan transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.1560.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011527; ABC1_TM_dom.
DR   InterPro; IPR036640; ABC1_TM_sf.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00664; ABC_membrane; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF90123; SSF90123; 1.
DR   PROSITE; PS50929; ABC_TM1F; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS51317; NDVA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Sugar transport; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..602
FT                   /note="Beta-(1-->2)glucan export ATP-binding/permease
FT                   protein NdvA"
FT                   /id="PRO_0000290253"
FT   TRANSMEM        22..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01728"
FT   TRANSMEM        68..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01728"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01728"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01728"
FT   TRANSMEM        238..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01728"
FT   TRANSMEM        285..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01728"
FT   DOMAIN          21..311
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01728"
FT   DOMAIN          345..579
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01728"
FT   BINDING         378..385
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01728"
SQ   SEQUENCE   602 AA;  65944 MW;  D57760C14851C6A8 CRC64;
     MPMLRLYARV LQLLGKEAML GWVLAGANLL LAAAQFAEPV LFGRIVDVLS GNLSTGAMAQ
     PAQSPWPLLL AWAVFGLFTI GCGAAVALHA DRLAHRQRQA ILTDYFEHVL QLPLTYHTGT
     HSGRLMKVML NGTDALWRLW LGFFREHFAA LMSLVVLLPL SIYINWRLAL LLFALCVVFT
     VLTTLVVRKT YAMQGEVEES YSDLSARASD ALGNIALVQS FVRIDAEVQG LRFVADRLLA
     MQMPVLSWWA LVTVITRAST TITVLAIFTV GIALHEQGLT SVGEIVMFVS FATMLIQKLE
     QVVGFVNSVF MEAPRLQEFV NVLDAVPAVR DRLDAIDPGR LSGLVEFDNV SFSYDGKRPA
     IEDLSFTALP GQTIALVGAT GAGKSTAIAL LHRAFDPQSG VIKIDGMDVR GLTLAGLRRN
     IGVVFQEALL FDRTIADNLR VGKPDATEEE MRIAASRAQA LDFIERSELK FDTNAGERGR
     MLSGGERQRL SIARALLKDP PILILDEATS ALDAVTEAKV NLALDEVMKG RTTFVIAHRL
     STIRHATRIL VFDNGRVIES GSFDELLARR GYFAELAHAQ FMVQDSARSA MPAAQPEGIP
     EF
 
 
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