GLUD_CORGL
ID GLUD_CORGL Reviewed; 273 AA.
AC P48245;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Glutamate transport system permease protein GluD {ECO:0000305};
DE AltName: Full=Glutamate uptake system protein GluD {ECO:0000305};
GN Name=gluD {ECO:0000303|PubMed:7868586}; OrderedLocusNames=Cgl1953, cg2139;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=7868586; DOI=10.1128/jb.177.5.1152-1158.1995;
RA Kronemeyer W., Peekhaus N., Kraemer R., Sahm H., Eggeling L.;
RT "Structure of the gluABCD cluster encoding the glutamate uptake system of
RT Corynebacterium glutamicum.";
RL J. Bacteriol. 177:1152-1158(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
CC -!- FUNCTION: Part of the ABC transporter complex GluABCD involved in
CC glutamate uptake. Probably responsible for the translocation of the
CC substrate across the membrane. {ECO:0000269|PubMed:7868586}.
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (GluA),
CC two transmembrane proteins (GluC and GluD) and a solute-binding protein
CC (GluB). {ECO:0000305|PubMed:7868586}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gluABCD cluster almost abolishes
CC glutamate uptake activity. {ECO:0000269|PubMed:7868586}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. HisMQ subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAF20294.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X81191; CAA57063.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB99346.1; -; Genomic_DNA.
DR EMBL; BX927153; CAF20294.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_601160.2; NC_003450.3.
DR RefSeq; WP_011014781.1; NC_006958.1.
DR AlphaFoldDB; P48245; -.
DR SMR; P48245; -.
DR STRING; 196627.cg2139; -.
DR TCDB; 3.A.1.3.9; the atp-binding cassette (abc) superfamily.
DR KEGG; cgb:cg2139; -.
DR KEGG; cgl:Cgl1953; -.
DR PATRIC; fig|196627.13.peg.1891; -.
DR eggNOG; COG0765; Bacteria.
DR HOGENOM; CLU_019602_1_3_11; -.
DR OMA; EPFMVYG; -.
DR Proteomes; UP000000582; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; -; 1.
DR InterPro; IPR010065; AA_ABC_transptr_permease_3TM.
DR InterPro; IPR043429; ArtM/GltK/GlnP/TcyL/YhdX-like.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR PANTHER; PTHR30614; PTHR30614; 1.
DR Pfam; PF00528; BPD_transp_1; 1.
DR SUPFAM; SSF161098; SSF161098; 1.
DR TIGRFAMs; TIGR01726; HEQRo_perm_3TM; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..273
FT /note="Glutamate transport system permease protein GluD"
FT /id="PRO_0000060043"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 30..221
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT REGION 242..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 101
FT /note="A -> V (in Ref. 1; CAA57063)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="R -> C (in Ref. 1; CAA57063)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 273 AA; 29866 MW; 601CB9F525C781B9 CRC64;
MLSGNGQLDA NKWTPFINSQ TWTTYILPGL WGTLKSAVFS VILALVMGTA LGLGRISEIR
ILRWFCAVII ETFRAIPVLI LMIFAYQMFA QYNIVPSSQL AFAAVVFGLT MYNGSVIAEI
LRSGIASLPK GQKEAAIALG MSSRQTTWSI LLPQAVAAML PALISQMVIA LKDSALGYQI
GYIEVVRSGI QSASVNRNYL AALFVVALIM IVLNFSLTAL ASRIERQLRA GRARKNIVAK
VPEQPDQGLE TKDNVNVDWQ DPDYKDLKTP GVQ
