UGPC_SALTI
ID UGPC_SALTI Reviewed; 356 AA.
AC Q8Z245; Q7C5X8;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 149.
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};
GN OrderedLocusNames=STY4257, t3967;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(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; AL513382; CAD08075.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO71437.1; -; Genomic_DNA.
DR RefSeq; NP_458365.1; NC_003198.1.
DR RefSeq; WP_000907851.1; NZ_WSUR01000001.1.
DR AlphaFoldDB; Q8Z245; -.
DR SMR; Q8Z245; -.
DR STRING; 220341.16505054; -.
DR EnsemblBacteria; AAO71437; AAO71437; t3967.
DR KEGG; stt:t3967; -.
DR KEGG; sty:STY4257; -.
DR PATRIC; fig|220341.7.peg.4348; -.
DR eggNOG; COG3842; Bacteria.
DR HOGENOM; CLU_000604_1_1_6; -.
DR OMA; PRNMYDK; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IEA:UniProt.
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..356
FT /note="sn-glycerol-3-phosphate import ATP-binding protein
FT UgpC"
FT /id="PRO_0000289780"
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 356 AA; 39393 MW; 02A827D530DAD1C7 CRC64;
MAGLKLQAVT KSWGGKTQVI QPLTLDVADG EFIVMVGPSG CGKSTLLRMV AGLERVTSGD
IWIDRKRVTE MEPKDRGIAM VFQNYALYPH MSVEENMAWG LKIRGMSKAH IEERVREAAR
ILELDGLLKR RPRELSGGQR QRVAMGRAIV REPAVFLFDE PLSNLDAKLR VQMRLELQHL
HRRLRTTSLY VTHDQVEAMT LAQRVMVMNK GVAEQIGTPV EVYEKPASRF VASFIGSPAM
NLLDGVISAS GDRFELPGGL ALPIGAGYRG HAGRKMTLGI RPEHIALSSQ AEGGVPLTVD
TLEILGADNL AHGRWGDQKL VVRLAHQQRP AAGSTLWLRL PEHQRHLFDG ETGQRV
