ID   AGPA_RHIME              Reviewed;         693 AA.
AC   Q9X4Y1;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2001, sequence version 2.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Periplasmic alpha-galactoside-binding protein {ECO:0000305};
DE   AltName: Full=Alpha-galactoside permease {ECO:0000303|PubMed:9791127};
DE   Flags: Precursor;
GN   Name=agpA {ECO:0000303|PubMed:9791127}; OrderedLocusNames=RB1567;
GN   ORFNames=SMb21647;
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OG   Plasmid pSymB (megaplasmid 2).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION,
RP   INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=1021;
RX   PubMed=9791127; DOI=10.1128/jb.180.21.5739-5748.1998;
RA   Gage D.J., Long S.R.;
RT   "Alpha-galactoside uptake in Rhizobium meliloti: isolation and
RT   characterization of agpA, a gene encoding a periplasmic binding protein
RT   required for melibiose and raffinose utilization.";
RL   J. Bacteriol. 180:5739-5748(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11481431; DOI=10.1073/pnas.161294698;
RA   Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorhoelter F.J.,
RA   Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puehler A.;
RT   "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing
RT   endosymbiont Sinorhizobium meliloti.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11474104; DOI=10.1126/science.1060966;
RA   Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA   Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA   Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA   Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA   Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA   Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA   Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA   Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA   Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA   Wong K., Yeh K.-C., Batut J.;
RT   "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL   Science 293:668-672(2001).
RN   [4]
RP   INDUCTION.
RX   PubMed=17101990; DOI=10.1073/pnas.0606673103;
RA   Mauchline T.H., Fowler J.E., East A.K., Sartor A.L., Zaheer R., Hosie A.H.,
RA   Poole P.S., Finan T.M.;
RT   "Mapping the Sinorhizobium meliloti 1021 solute-binding protein-dependent
RT   transportome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:17933-17938(2006).
CC   -!- FUNCTION: Involved in the transport of alpha-galactosides. Required for
CC       the utilization of raffinose and melibiose. Probably acts as a
CC       periplasmic substrate-binding protein for a transport system.
CC       {ECO:0000269|PubMed:9791127}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:9791127}.
CC   -!- INDUCTION: Induced by melibiose, raffinose, galactose, galactosamine,
CC       dulcitol and stachyose (PubMed:9791127, PubMed:17101990). Expression is
CC       down-regulated by succinate and glucose, and by SyrA (PubMed:9791127).
CC       {ECO:0000269|PubMed:17101990, ECO:0000269|PubMed:9791127}.
CC   -!- DISRUPTION PHENOTYPE: Disruption mutant is unable to use melibiose and
CC       raffinose as carbon sources but it can use glucose and galactose.
CC       {ECO:0000269|PubMed:9791127}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 5 family.
CC       {ECO:0000305}.
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DR   EMBL; AF119834; AAD26274.1; -; Genomic_DNA.
DR   EMBL; AL591985; CAC49966.1; -; Genomic_DNA.
DR   PIR; F96037; F96037.
DR   RefSeq; NP_438106.1; NC_003078.1.
DR   RefSeq; WP_010976339.1; NC_003078.1.
DR   AlphaFoldDB; Q9X4Y1; -.
DR   SMR; Q9X4Y1; -.
DR   STRING; 266834.SM_b21647; -.
DR   TCDB; 3.A.1.5.7; the atp-binding cassette (abc) superfamily.
DR   EnsemblBacteria; CAC49966; CAC49966; SM_b21647.
DR   GeneID; 61601470; -.
DR   KEGG; sme:SM_b21647; -.
DR   PATRIC; fig|266834.11.peg.6492; -.
DR   eggNOG; COG0747; Bacteria.
DR   HOGENOM; CLU_017028_8_2_5; -.
DR   OMA; SECLTRT; -.
DR   Proteomes; UP000001976; Plasmid pSymB.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:UniProt.
DR   GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   InterPro; IPR030678; Peptide/Ni-bd.
DR   InterPro; IPR039424; SBP_5.
DR   InterPro; IPR000914; SBP_5_dom.
DR   PANTHER; PTHR30290; PTHR30290; 1.
DR   Pfam; PF00496; SBP_bac_5; 1.
DR   PIRSF; PIRSF002741; MppA; 1.
PE   2: Evidence at transcript level;
KW   Periplasm; Plasmid; Reference proteome; Signal; Sugar transport; Transport.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..693
FT                   /note="Periplasmic alpha-galactoside-binding protein"
FT                   /id="PRO_0000031783"
FT   CONFLICT        397
FT                   /note="E -> K (in Ref. 1; AAD26274)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   693 AA;  77407 MW;  76F9B95708C2DF9F CRC64;
     MKTHRLNMTA SLLIGISAFA VQAFASEPTV VPEQPPFPAQ GKITYVSRDS ILEFKALREY
     REPEWVTEKF VKAGKLPPVA ERLPKEPMVF KAGNMPDGMG VYGDVMRHVI GGRPEGWNYS
     AGQTQGWGGI DIGMFECLTR TAPLFQVEAD DMEPLPNLAK SWDWSEDGRK LTMHLIEGAK
     WSDGDPFDAD DVMFYWEDNV LDSSVSPLNG ATPETFGEGT TLKKIDQYTV EWTFKEAFPR
     QHLFAMAYGT FCPGPSHILK TKHPKYAGTT YNEYKNGFPA EYMNLPVMGA WVPVAYRPDD
     IIVLRRNPYY WKVDEAGNQL PYLNELHYKL STWADRDVQA IAGSGDISNL EQPENFVESL
     KRAANESAPA RLAFGPRVIG YNMHMNFSGN GWGDPDERAK AVRELNRNLD FRKAVTMAVD
     RKKLGEALVK GPFTAIYPGG LSSGTSFYDR NSTIYYPHDL EGAKVLLEKV GLKDTDGNGF
     VNFPAGKLGG RDVEIVLLVN SDYSTDRNLA EGMVGQMEKL GLRVVLNALD GKQRDAANYA
     GRFDWMIHRN TAEFASVVQN TPQLAPTGPR TSWHHRAPEG GEVDVMPHEQ ELVDIVNKFI
     ASNDNDERTE LMKQYQKVAT TNVDTVGLTE YPGALIINKR FSNIPPGAPI FMFNWAEDTI
     IRERVFVAAD KQGDYELYPE QLPGKPGESG PIN