UGPC_ECOLI
ID UGPC_ECOLI Reviewed; 356 AA.
AC P10907; P76696; Q2M7B3;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 3.
DT 03-AUG-2022, entry version 187.
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=b3450, JW3415;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=3062310; DOI=10.1111/j.1365-2958.1988.tb00088.x;
RA Overduin P., Boos W., Tommassen J.;
RT "Nucleotide sequence of the ugp genes of Escherichia coli K-12: homology to
RT the maltose system.";
RL Mol. Microbiol. 2:767-775(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION IN SN-GLYCEROL-3-PHOSPHATE TRANSPORT, AND ACTIVITY REGULATION.
RC STRAIN=K12;
RX PubMed=363686; DOI=10.1128/jb.136.3.1070-1083.1978;
RA Argast M., Ludtke D., Silhavy T.J., Boos W.;
RT "A second transport system for sn-glycerol-3-phosphate in Escherichia
RT coli.";
RL J. Bacteriol. 136:1070-1083(1978).
RN [6]
RP FUNCTION IN SN-GLYCEROL-3-PHOSPHATE TRANSPORT, AND INDUCTION BY PHOB.
RC STRAIN=K12;
RX PubMed=7042685; DOI=10.1128/jb.150.3.1154-1163.1982;
RA Schweizer H., Argast M., Boos W.;
RT "Characteristics of a binding protein-dependent transport system for sn-
RT glycerol-3-phosphate in Escherichia coli that is part of the pho regulon.";
RL J. Bacteriol. 150:1154-1163(1982).
RN [7]
RP FUNCTION IN SN-GLYCEROL-3-PHOSPHATE AND GLYCEROPHOSPHORYL DIESTERS
RP TRANSPORT, AND INDUCTION BY PHOB.
RC STRAIN=K12;
RX PubMed=2842304; DOI=10.1128/jb.170.9.4125-4135.1988;
RA Brzoska P., Boos W.;
RT "Characteristics of a ugp-encoded and phoB-dependent glycerophosphoryl
RT diester phosphodiesterase which is physically dependent on the ugp
RT transport system of Escherichia coli.";
RL J. Bacteriol. 170:4125-4135(1988).
RN [8]
RP INDUCTION BY PHOB, AND CRP.
RC STRAIN=K12;
RX PubMed=1987150; DOI=10.1128/jb.173.2.549-558.1991;
RA Kasahara M., Makino K., Amemura M., Nakata A., Shinagawa H.;
RT "Dual regulation of the ugp operon by phosphate and carbon starvation at
RT two interspaced promoters.";
RL J. Bacteriol. 173:549-558(1991).
RN [9]
RP FUNCTIONAL EXCHANGEABILITY OF UGPC AND MALK.
RC STRAIN=K12;
RX PubMed=8407831; DOI=10.1128/jb.175.20.6546-6552.1993;
RA Hekstra D., Tommassen J.;
RT "Functional exchangeability of the ABC proteins of the periplasmic binding
RT protein-dependent transport systems Ugp and Mal of Escherichia coli.";
RL J. Bacteriol. 175:6546-6552(1993).
RN [10]
RP FUNCTION IN SN-GLYCEROL-3-PHOSPHATE, AND INHIBITION BY INTERNAL PHOSPHATE.
RC STRAIN=K12;
RX PubMed=8282692; DOI=10.1128/jb.176.1.15-20.1994;
RA Brzoska P., Rimmele M., Brzostek K., Boos W.;
RT "The pho regulon-dependent Ugp uptake system for glycerol-3-phosphate in
RT Escherichia coli is trans inhibited by Pi.";
RL J. Bacteriol. 176:15-20(1994).
RN [11]
RP INHIBITION BY INTERNAL PHOSPHATE.
RC STRAIN=K12;
RX PubMed=7836304; DOI=10.1128/jb.177.3.699-704.1995;
RA Xavier K.B., Kossmann M., Santos H., Boos W.;
RT "Kinetic analysis by in vivo 31P nuclear magnetic resonance of internal Pi
RT during the uptake of sn-glycerol-3-phosphate by the pho regulon-dependent
RT Ugp system and the glp regulon-dependent GlpT system.";
RL J. Bacteriol. 177:699-704(1995).
RN [12]
RP REVIEW.
RX PubMed=9711545; DOI=10.1016/s0076-6879(98)92006-7;
RA Boos W.;
RT "Binding protein-dependent ABC transport system for glycerol 3-phosphate of
RT Escherichia coli.";
RL Methods Enzymol. 292:40-51(1998).
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 (Probable). Can also transport glycerophosphoryl
CC diesters. {ECO:0000255|HAMAP-Rule:MF_01727, ECO:0000269|PubMed:2842304,
CC ECO:0000269|PubMed:363686, ECO:0000269|PubMed:7042685,
CC ECO:0000269|PubMed:8282692, ECO:0000269|PubMed:8407831, ECO:0000305}.
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 -!- ACTIVITY REGULATION: Activated by gluconate, inhibited by fumarate and
CC internal phosphate. Internal phosphate may bind to UgpC and reduce its
CC affinity for UgpA and UgpE. {ECO:0000269|PubMed:363686}.
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; Peripheral membrane protein.
CC -!- INDUCTION: Induced by phosphate starvation, via PhoB. Also induced by
CC carbon starvation, via the cAMP receptor protein (CRP).
CC {ECO:0000269|PubMed:1987150, ECO:0000269|PubMed:2842304,
CC ECO:0000269|PubMed:7042685}.
CC -!- MISCELLANEOUS: Functional exchangeability of MalK and UgpC. But UgpC
CC does not complement the regulatory function of MalK.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB18425.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X13141; CAA31534.1; -; Genomic_DNA.
DR EMBL; U00039; AAB18425.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76475.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77843.1; -; Genomic_DNA.
DR PIR; S47669; QRECUC.
DR RefSeq; NP_417907.2; NC_000913.3.
DR RefSeq; WP_000907792.1; NZ_SSZK01000008.1.
DR AlphaFoldDB; P10907; -.
DR SMR; P10907; -.
DR BioGRID; 4262493; 216.
DR ComplexPortal; CPX-2150; sn-glycerol-3-phosphate ABC transporter complex.
DR DIP; DIP-11079N; -.
DR IntAct; P10907; 8.
DR STRING; 511145.b3450; -.
DR TCDB; 3.A.1.1.3; the atp-binding cassette (abc) superfamily.
DR jPOST; P10907; -.
DR PaxDb; P10907; -.
DR PRIDE; P10907; -.
DR EnsemblBacteria; AAC76475; AAC76475; b3450.
DR EnsemblBacteria; BAE77843; BAE77843; BAE77843.
DR GeneID; 947953; -.
DR KEGG; ecj:JW3415; -.
DR KEGG; eco:b3450; -.
DR PATRIC; fig|511145.12.peg.3547; -.
DR EchoBASE; EB1041; -.
DR eggNOG; COG3842; Bacteria.
DR HOGENOM; CLU_000604_1_1_6; -.
DR InParanoid; P10907; -.
DR OMA; PRNMYDK; -.
DR PhylomeDB; P10907; -.
DR BioCyc; EcoCyc:UGPC-MON; -.
DR BioCyc; MetaCyc:UGPC-MON; -.
DR PRO; PR:P10907; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IDA:EcoCyc.
DR GO; GO:1902517; C:glycerol-3-phosphate-transporting ATPase complex; IPI:ComplexPortal.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0015430; F:ABC-type glycerol-3-phosphate transporter activity; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; ISM:EcoCyc.
DR GO; GO:0015169; F:glycerol-3-phosphate transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0001406; F:glycerophosphodiester transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR GO; GO:0015794; P:glycerol-3-phosphate transmembrane transport; IDA:ComplexPortal.
DR GO; GO:0001407; P:glycerophosphodiester transmembrane transport; IDA:EcoCyc.
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 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Reference proteome; Sugar transport; Translocase;
KW Transport.
FT CHAIN 1..356
FT /note="sn-glycerol-3-phosphate import ATP-binding protein
FT UgpC"
FT /id="PRO_0000093026"
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; 39524 MW; 33D49B258D0C9AA8 CRC64;
MAGLKLQAVT KSWDGKTQVI KPLTLDVADG EFIVMVGPSG CGKSTLLRMV AGLERVTEGD
IWINDQRVTE MEPKDRGIAM VFQNYALYPH MSVEENMAWG LKIRGMGKQQ IAERVKEAAR
ILELDGLLKR RPRELSGGQR QRVAMGRAIV RDPAVFLFDE PLSNLDAKLR VQMRLELQQL
HRRLKTTSLY VTHDQVEAMT LAQRVMVMNG GVAEQIGTPV EVYEKPASLF VASFIGSPAM
NLLTGRVNNE GTHFELDGGI ELPLNGGYRQ YAGRKMTLGI RPEHIALSSQ AEGGVPMVMD
TLEILGADNL AHGRWGEQKL VVRLAHQERP TAGSTLWLHL AENQLHLFDG ETGQRV
