UGPC_BORPA
ID UGPC_BORPA Reviewed; 362 AA.
AC Q7W6G5;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 131.
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=BPP2947;
OS Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257311;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12822 / ATCC BAA-587 / NCTC 13253;
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
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; BX640432; CAE38239.1; -; Genomic_DNA.
DR RefSeq; WP_010928814.1; NC_002928.3.
DR AlphaFoldDB; Q7W6G5; -.
DR SMR; Q7W6G5; -.
DR EnsemblBacteria; CAE38239; CAE38239; BPP2947.
DR KEGG; bpa:BPP2947; -.
DR HOGENOM; CLU_000604_1_1_4; -.
DR OMA; APPMNLM; -.
DR Proteomes; UP000001421; 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; Sugar transport; Translocase; Transport.
FT CHAIN 1..362
FT /note="sn-glycerol-3-phosphate import ATP-binding protein
FT UgpC"
FT /id="PRO_0000289731"
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 362 AA; 39949 MW; A581089A1FDF5658 CRC64;
MATLSFRNVK KTYAGNVPVI HGSDMDVADG EFIVIVGPSG CGKSTLMRMV AGLETVTEGE
ILIDDKVVNT LEPAERDIAM VFQNYALYPH MSVFDNMAYG LKIRRLPKDE IRKRVEAAAQ
ILELGKLLDR RPRALSGGQR QRVAMGRAIV REPKVFLFDE PLSNLDAKLR VAMRLEILKL
HRRLNTTSLY VTHDQVEAMT LAHRMVVMYQ GVPEQIGTPM EVFEKPASTF VAGFIGSPPM
NLLEVAVGGD GIVHTSDGIA LDISPLAVPQ QVRGRKVVMG LRPEHMLLNA QGLAAEIEMI
ETLGSEQLVH GRCGKHMVVV RCSTRQFSET PARVGDTLTI GPDGRHPLHW FEADTGRRVE
GL