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Database: UniProt
Entry: Q46ZM0
LinkDB: Q46ZM0
Original site: Q46ZM0 
ID   UGPC_CUPPJ              Reviewed;         369 AA.
AC   Q46ZM0;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 130.
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=Reut_A2049;
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 / LMG 1197;
RX   PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA   Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA   Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA   Kyrpides N.C.;
RT   "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT   versatile pollutant degrader.";
RL   PLoS ONE 5:E9729-E9729(2010).
CC   -!- FUNCTION: Part of the ABC transporter complex UgpBAEC involved in sn-
CC       glycerol-3-phosphate (G3P) import. Responsible for energy coupling to
CC       the 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; CP000090; AAZ61413.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q46ZM0; -.
DR   SMR; Q46ZM0; -.
DR   STRING; 264198.Reut_A2049; -.
DR   KEGG; reu:Reut_A2049; -.
DR   eggNOG; COG3842; Bacteria.
DR   HOGENOM; CLU_000604_1_1_4; -.
DR   OrthoDB; 5298774at2; -.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR   CDD; cd03301; ABC_MalK_N; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR047641; ABC_transpr_MalK/UgpC-like.
DR   InterPro; IPR008995; Mo/tungstate-bd_C_term_dom.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR013611; Transp-assoc_OB_typ2.
DR   PANTHER; PTHR43875; MALTODEXTRIN IMPORT ATP-BINDING PROTEIN MSMX; 1.
DR   PANTHER; PTHR43875:SF12; SN-GLYCEROL-3-PHOSPHATE IMPORT ATP-BINDING PROTEIN UGPC; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF08402; TOBE_2; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF50331; MOP-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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..369
FT                   /note="sn-glycerol-3-phosphate import ATP-binding protein
FT                   UgpC"
FT                   /id="PRO_0000289759"
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   369 AA;  39783 MW;  83D69F6E0F5BCFDC CRC64;
     MAKLSLRNVQ KTYAGNVKVV HGIDMEIADG EFIVIVGPSG CGKSTLLRMV AGLETITGGD
     IHIGDRVVNN LEPAERDIAM VFQNYALYPH MSVYDNMAYG LKIRGMAKAE IEQRVKHAAG
     ILELAPLLDR KPRQLSGGQR QRVAMGRAIV REPSVFLFDE PLSNLDAKLR VQMRLELKEL
     HRRLGTTSLY VTHDQVEAMT LADRMMVLNG GRVEQIGTPL EVYTRPASTF VAGFIGSPPM
     NLVPVARNGG MAGAGGVAQM RVLGKEGGAS DATLGHLPMG LHLPAEALLG LRPEHIEPCA
     AHDAIAEVDV RVVEALGADS FAYGSLGGQP IVVRLDSHAR VRAGDKLPVT SSPDHLHFFD
     AQSGKRIEA
//
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