ID   UGPC_BURCM              Reviewed;         361 AA.
AC   Q0BIZ6;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=sn-glycerol-3-phosphate import ATP-binding protein UgpC {ECO:0000255|HAMAP-Rule:MF_01727};
DE            EC=7.6.2.10 {ECO:0000255|HAMAP-Rule:MF_01727};
GN   Name=ugpC {ECO:0000255|HAMAP-Rule:MF_01727}; OrderedLocusNames=Bamb_0317;
OS   Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS   (strain AMMD)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=339670;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-244 / AMMD;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA   Ramette A., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Part of the ABC transporter complex UgpABCE involved in sn-
CC       glycerol-3-phosphate import. Responsible for energy coupling to the
CC       transport system. {ECO:0000255|HAMAP-Rule:MF_01727}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + sn-glycerol 3-phosphate(out) = ADP + H(+) +
CC         phosphate + sn-glycerol 3-phosphate(in); Xref=Rhea:RHEA:21668,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57597, ChEBI:CHEBI:456216;
CC         EC=7.6.2.10; Evidence={ECO:0000255|HAMAP-Rule:MF_01727};
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (UgpC),
CC       two transmembrane proteins (UgpA and UgpE) and a solute-binding protein
CC       (UgpB). {ECO:0000255|HAMAP-Rule:MF_01727}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01727}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01727}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. sn-glycerol-3-
CC       phosphate importer (TC 3.A.1.1.3) family. {ECO:0000255|HAMAP-
CC       Rule:MF_01727}.
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DR   EMBL; CP000440; ABI85877.1; -; Genomic_DNA.
DR   RefSeq; WP_011655782.1; NZ_CP009798.1.
DR   AlphaFoldDB; Q0BIZ6; -.
DR   SMR; Q0BIZ6; -.
DR   STRING; 339670.Bamb_0317; -.
DR   EnsemblBacteria; ABI85877; ABI85877; Bamb_0317.
DR   GeneID; 44691007; -.
DR   KEGG; bam:Bamb_0317; -.
DR   PATRIC; fig|339670.21.peg.1302; -.
DR   eggNOG; COG3842; Bacteria.
DR   OMA; APPMNLM; -.
DR   Proteomes; UP000000662; Chromosome 1.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015430; F:ABC-type glycerol-3-phosphate transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR   GO; GO:0001407; P:glycerophosphodiester transmembrane transport; IEA:InterPro.
DR   CDD; cd03301; ABC_MalK_N; 1.
DR   Gene3D; 2.40.50.140; -; 1.
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; IPR015855; ABC_transpr_MalK-like.
DR   InterPro; IPR008995; Mo/tungstate-bd_C_term_dom.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR040582; OB_MalK.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR017922; UgpC.
DR   PANTHER; PTHR43875:SF12; PTHR43875:SF12; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF17912; OB_MalK; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF50331; SSF50331; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS51315; UGPC; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Sugar transport; Translocase; Transport.
FT   CHAIN           1..361
FT                   /note="sn-glycerol-3-phosphate import ATP-binding protein
FT                   UgpC"
FT                   /id="PRO_0000289740"
FT   DOMAIN          4..235
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01727"
FT   BINDING         37..44
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01727"
SQ   SEQUENCE   361 AA;  38783 MW;  9474F516BF757725 CRC64;
     MAALSLKGIR KSYDGKQHVL HGIDVEIADG EFVVLVGPSG CGKSTLLRMI AGLETVTDGE
     IAIGDRVVNA LEPKDRDIAM VFQNYALYPH MTVAQNMGYG LKIRGIERAT IDSRVAAAAK
     ILELEPLLAR RPRELSGGQR QRVAMGRAIV REPSVFLFDE PLSNLDAKLR VQMRLEIQRL
     HARLATTSVY VTHDQIEAMT LAQRVIVMNR GYAEQIGAPV DVYEKPETVF VAGFIGSPAM
     NLMHGRLSED GATFAVAGGG PALPVAGAPG IGTTIATGRD WVLGVRPEHM TPQPGVAQAS
     LPVDSCELLG ADNLAHGRWG NHDVVVRLPH ADRPARGTAL GAALPAHRLH FFDPETGKRA
     G