BZTD_RHOCB
ID BZTD_RHOCB Reviewed; 263 AA.
AC Q52666; D5AM33;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Glutamate/glutamine/aspartate/asparagine transport ATP-binding protein BztD;
GN Name=bztD; OrderedLocusNames=RCAP_rcc00338;
OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=272942;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=8809753; DOI=10.1111/j.1365-2958.1996.tb02541.x;
RA Zheng S., Haselkorn R.;
RT "A glutamate/glutamine/aspartate/asparagine transport operon in Rhodobacter
RT capsulatus.";
RL Mol. Microbiol. 20:1001-1011(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=20418398; DOI=10.1128/jb.00366-10;
RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA Haselkorn R.;
RT "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT Rhodobacter capsulatus SB 1003.";
RL J. Bacteriol. 192:3545-3546(2010).
CC -!- FUNCTION: Part of a binding-protein-dependent transport system for
CC glutamate, glutamine, aspartate, asparagine. Probably responsible for
CC energy coupling to the transport system.
CC -!- SUBUNIT: BztB and BztC form a heterodimer which can form a membrane
CC complex with a homodimer of BztD. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; U37407; AAB17889.1; -; Genomic_DNA.
DR EMBL; CP001312; ADE84103.1; -; Genomic_DNA.
DR PIR; S77604; S77604.
DR RefSeq; WP_013066083.1; NC_014034.1.
DR AlphaFoldDB; Q52666; -.
DR SMR; Q52666; -.
DR STRING; 272942.RCAP_rcc00338; -.
DR TCDB; 3.A.1.3.7; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; ADE84103; ADE84103; RCAP_rcc00338.
DR KEGG; rcp:RCAP_rcc00338; -.
DR eggNOG; COG1126; Bacteria.
DR HOGENOM; CLU_000604_1_22_5; -.
DR OMA; APIWVRR; -.
DR OrthoDB; 1191583at2; -.
DR Proteomes; UP000002361; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015424; F:ABC-type amino acid transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR030679; ABC_ATPase_HisP-typ.
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; 1.
DR PIRSF; PIRSF039085; ABC_ATPase_HisP; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 3: Inferred from homology;
KW Amino-acid transport; ATP-binding; Cell membrane; Membrane;
KW Nucleotide-binding; Reference proteome; Transport.
FT CHAIN 1..263
FT /note="Glutamate/glutamine/aspartate/asparagine transport
FT ATP-binding protein BztD"
FT /id="PRO_0000091967"
FT DOMAIN 23..257
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 55..62
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CONFLICT 214
FT /note="A -> T (in Ref. 1; AAB17889)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="R -> H (in Ref. 1; AAB17889)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 263 AA; 30002 MW; A0879FCEAC14498D CRC64;
MSEPSYDHQV DRSHMQVSDE IAIQISQMNK WYGQFHVLRD INLTVHRGER IVIAGPSGSG
KSTMIRCINR LEEHQSGKII VDGIELTSDL KNIDKVRSEV GMVFQHFNLF PHLTILENLT
LAPIWVRKVP KREAEETAMY YLEKVKIPEQ AQKYPGQLSG GQQQRVAIAR SLCMKPKIML
FDEPTSALDP EMIKEVLDTM IQLAEEGMTM LCVAHEMGFA QAVANRVIFM ADGQIVEQNN
PHDFFRNPQS ERTKQFLSQI LGH