ID   UGPC_BORA1              Reviewed;         361 AA.
AC   Q2L0H5;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=BAV1902;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=197N;
RX   PubMed=16885469; DOI=10.1128/jb.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA   Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA   Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA   Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT   with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT   extensive diversity in surface structures associated with host
RT   interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
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; AM167904; CAJ49511.1; -; Genomic_DNA.
DR   RefSeq; WP_012417570.1; NC_010645.1.
DR   AlphaFoldDB; Q2L0H5; -.
DR   SMR; Q2L0H5; -.
DR   STRING; 360910.BAV1902; -.
DR   EnsemblBacteria; CAJ49511; CAJ49511; BAV1902.
DR   GeneID; 41393743; -.
DR   KEGG; bav:BAV1902; -.
DR   eggNOG; COG3842; Bacteria.
DR   HOGENOM; CLU_000604_1_1_4; -.
DR   OMA; APPMNLM; -.
DR   OrthoDB; 1200451at2; -.
DR   Proteomes; UP000001977; Chromosome.
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; Reference proteome; Sugar transport; Translocase;
KW   Transport.
FT   CHAIN           1..361
FT                   /note="sn-glycerol-3-phosphate import ATP-binding protein
FT                   UgpC"
FT                   /id="PRO_0000289729"
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;  40232 MW;  EFE08007BFC44C98 CRC64;
     MATLSFRNLK KTYAGNVPVI HGIDMEIKDG EFIVIVGPSG CGKSTLMRMV AGLETVTSGE
     ILIDDKPVND LEPAERDIAM VFQNYALYPH MSVFENMAYG LKIRKVPKAE IQKRVEEAAQ
     ILELGKLLDR RPRQLSGGQR QRVAMGRAIV REPKVFLFDE PLSNLDAKLR VAMRLEILKL
     HRRLHTTSLY VTHDQVEAMT LAHRMVVMYQ GVPEQIGTPM EVFEKPASTF VAGFIGSPPM
     NLIEVDVAGD GTMTAEGMPL QISPLQVPSA VRGRKIIMGL RPEHMLLNAE GIPVEIEMIE
     TLGSEQLVHG RRGKHMLVVR CTTRQLSEST VKVGDTMNIG PDGRHDLHWF EPDTGRRVQG
     L