AAPJ_RHIL3
ID AAPJ_RHIL3 Reviewed; 341 AA.
AC Q52812; Q1MH71;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=General L-amino acid-binding periplasmic protein AapJ;
DE Flags: Precursor;
GN Name=aapJ; OrderedLocusNames=RL2204;
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 [GENOMIC DNA], FUNCTION, AND SUBUNIT.
RX PubMed=8898392; DOI=10.1046/j.1365-2958.1996.00078.x;
RA Walshaw D.L., Poole P.S.;
RT "The general L-amino acid permease of Rhizobium leguminosarum is an ABC
RT uptake system that also influences efflux of solutes.";
RL Mol. Microbiol. 21:1239-1252(1996).
RN [2]
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).
RN [3]
RP FUNCTION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=3841 {ECO:0000303|PubMed:19597156};
RX PubMed=19597156; DOI=10.1073/pnas.0903653106;
RA Prell J., White J.P., Bourdes A., Bunnewell S., Bongaerts R.J., Poole P.S.;
RT "Legumes regulate Rhizobium bacteroid development and persistence by the
RT supply of branched-chain amino acids.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:12477-12482(2009).
CC -!- FUNCTION: Part of the ABC transporter complex AapJQMP involved in
CC uptake of L-amino acids (PubMed:8898392, PubMed:19597156). Affects the
CC efflux of these amino acids as well (PubMed:8898392). Essential for the
CC development of bacteroids, the differentiated legume-symbiotic forms of
CC this bacterium, and for the effective N(2) fixation by them
CC (PubMed:19597156). {ECO:0000269|PubMed:19597156,
CC ECO:0000269|PubMed:8898392}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (AapP),
CC two transmembrane proteins (AapM and AapQ) and a solute-binding protein
CC (AapJ). {ECO:0000305|PubMed:19597156, ECO:0000305|PubMed:8898392}.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- DISRUPTION PHENOTYPE: Reduced uptake of amino acids Glu, Asp, Ala, Leu,
CC Ile and Val by bacteroids that lack this gene and the genes braC and
CC braC3 or braE and braF from another ABC uptake system of branched-chain
CC amino acids. Pea plants inoculated with bacteroids of either triple
CC mutant are defective in symbiosis; the plants are yellow, have
CC increased numbers of small pale pink root nodules, dry weights similar
CC to uninoculated control plants and 30% acetylene reduction compared to
CC plants inoculated with wild-type bacteroids. AapJ/braE/braF triple
CC mutant bacteroids are smaller, have reduced bacteroid protein and cell
CC number per plant compared to wild-type, and have a lower chromosome
CC number of 5 compared with 8 of the wild-type.
CC {ECO:0000269|PubMed:19597156}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 3 family.
CC {ECO:0000305}.
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DR EMBL; X82596; CAA57933.1; -; Genomic_DNA.
DR EMBL; AM236080; CAK07696.1; -; Genomic_DNA.
DR RefSeq; WP_011651801.1; NC_008380.1.
DR AlphaFoldDB; Q52812; -.
DR SMR; Q52812; -.
DR STRING; 216596.RL2204; -.
DR TCDB; 3.A.1.3.8; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; CAK07696; CAK07696; RL2204.
DR KEGG; rle:RL2204; -.
DR eggNOG; COG0834; Bacteria.
DR HOGENOM; CLU_019602_3_2_5; -.
DR OMA; RNTTWTF; -.
DR OrthoDB; 685252at2; -.
DR Proteomes; UP000006575; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IMP:UniProtKB.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0016595; F:glutamate binding; IC:UniProtKB.
DR GO; GO:0070728; F:leucine binding; IC:UniProtKB.
DR GO; GO:0043090; P:amino acid import; IMP:UniProtKB.
DR GO; GO:0015818; P:isoleucine transport; IMP:UniProtKB.
DR GO; GO:0051938; P:L-glutamate import; IMP:UniProtKB.
DR GO; GO:0015820; P:leucine transport; IMP:UniProtKB.
DR GO; GO:0015829; P:valine transport; IMP:UniProtKB.
DR InterPro; IPR005768; Lys_Arg_Orn-bd.
DR InterPro; IPR018313; SBP_3_CS.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR Pfam; PF00497; SBP_bac_3; 1.
DR SMART; SM00062; PBPb; 1.
DR TIGRFAMs; TIGR01096; 3A0103s03R; 1.
DR PROSITE; PS01039; SBP_BACTERIAL_3; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Periplasm; Signal; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..341
FT /note="General L-amino acid-binding periplasmic protein
FT AapJ"
FT /id="PRO_0000031748"
SQ SEQUENCE 341 AA; 36699 MW; 60E2E7678B08488D CRC64;
MKNKLLSAAI GAAVLAVGAS AASATTLSDV KAKGFVQCGV NTGLTGFAAP DASGNWAGFD
VDFCKAVASA VFGDPTKVKY TPTNAKERFT ALQSGEIDVL SRNTTWTINR DTALGFNFRP
VTYYDGQGFM VRKGLNVKSA LELSGAAICV QSGTTTELNL ADYFKTNNLQ YNPVVFENLP
EVNAAYDAGR CDVYTTDQSG LYSLRLTLKN PDEHIILPEI ISKEPLGPAV RQGDDQWFDI
VSWTAYALIN AEEFGITQAN VDEMKNSPNP DIKRFLGSET DTKIGTDLGL TNDWAANVIK
GVGNYGEIFE RNIGQGSPLK IARGLNALWN KGGIQYAPPV R
