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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
 
 
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