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Y1052_BRUA2
ID   Y1052_BRUA2             Reviewed;         332 AA.
AC   Q2YJJ9;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Putative peptide import ATP-binding protein BAB2_1052;
DE            EC=3.6.3.-;
GN   OrderedLocusNames=BAB2_1052;
OS   Brucella abortus (strain 2308).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=359391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308;
RX   PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA   Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(2005).
CC   -!- FUNCTION: Probably part of an ABC transporter complex that could be
CC       involved in peptide import. Probably responsible for energy coupling to
CC       the transport system (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (BAB2_1052
CC       and BAB2_1053), two transmembrane proteins (BAB2_1050 and BAB2_1051)
CC       and a solute-binding protein (BAB2_1049). {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Peripheral
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; AM040265; CAJ13218.1; -; Genomic_DNA.
DR   RefSeq; WP_002965564.1; NZ_KN046823.1.
DR   AlphaFoldDB; Q2YJJ9; -.
DR   SMR; Q2YJJ9; -.
DR   STRING; 359391.BAB2_1052; -.
DR   EnsemblBacteria; CAJ13218; CAJ13218; BAB2_1052.
DR   GeneID; 45054075; -.
DR   KEGG; bmf:BAB2_1052; -.
DR   PATRIC; fig|359391.11.peg.1839; -.
DR   HOGENOM; CLU_000604_1_23_5; -.
DR   OMA; LDPINTI; -.
DR   PhylomeDB; Q2YJJ9; -.
DR   Proteomes; UP000002719; Chromosome II.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015833; P:peptide transport; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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; IPR013563; Oligopep_ABC_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF08352; oligo_HPY; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01727; oligo_HPY; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Hydrolase; Membrane;
KW   Nucleotide-binding; Peptide transport; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..332
FT                   /note="Putative peptide import ATP-binding protein
FT                   BAB2_1052"
FT                   /id="PRO_0000290154"
FT   DOMAIN          11..261
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         47..54
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   332 AA;  36610 MW;  C67DF5FFDEEECAAE CRC64;
     MTISLKTAPL LEVSNLSVDF RTDGGWINAV DDVNFTLAPR ETLGLVGESG SGKSVTALSL
     LRLHDQRNSR LGGSVRYKGE DLFTLATSRL RQIRGHEIAM VFQDPIHTLN PVLTIGRQIE
     EGLRLHHGLQ GREARKRAIE LLDRVRIPDA ARRIDEYPHR MSGGQRQRVM IAIAIAGDPK
     ILIADEPTTA LDVTVQAQIM ELLRNLRDEL SMSVILISHD LGLVSEFADR AMVMYAGQPV
     ETGPIDKIFD EPLHPYTEGL LSAIPDLDDD LDRLPTIPGS IPEPSRRPPG CRFAPRCTFA
     QASCVKPQPI MSLTGGRASR CPPRLPTEEC VL
 
 
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