UGPC_ECO57
ID UGPC_ECO57 Reviewed; 356 AA.
AC Q8X6U5; Q7AA82;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 150.
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=Z4818, ECs4296;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG58556.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB37719.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE005174; AAG58556.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000007; BAB37719.1; ALT_INIT; Genomic_DNA.
DR PIR; H86011; H86011.
DR PIR; H91165; H91165.
DR RefSeq; NP_312323.2; NC_002695.1.
DR RefSeq; WP_000907770.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8X6U5; -.
DR SMR; Q8X6U5; -.
DR STRING; 155864.EDL933_4657; -.
DR EnsemblBacteria; AAG58556; AAG58556; Z4818.
DR EnsemblBacteria; BAB37719; BAB37719; ECs_4296.
DR GeneID; 915835; -.
DR KEGG; ece:Z4818; -.
DR KEGG; ecs:ECs_4296; -.
DR PATRIC; fig|386585.9.peg.4487; -.
DR eggNOG; COG3842; Bacteria.
DR HOGENOM; CLU_000604_1_1_6; -.
DR OMA; PRNMYDK; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; 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_0000289751"
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; 39391 MW; 50722869D4D49CD3 CRC64;
MAGLKLQAVT KSWDGKTQVI KPLTLDVADG EFIVMVGPSG CGKSTLLRMV AGLERVTEGD
ICINDQRVTE MEPKDRGIAM VFQNYALYPH MSVEENMAWG LKIRGMGKQQ IAERVKEAAR
ILELDGLLKR RPRELSGGQR QRVAMGRAIV RDPAVFLFDE PLSNLDAKLR VQMRLELQQL
HRRLKTTSLY VTHDQVEAMT LAQRVMVMNG GVAEQIGTPV EVYEKPASLF VASFIGSPAM
NLLTGRVNNE GTHFELDGGI ALPLNGGYRQ YAGRKMTLGI RPEHIALSSQ AEGGVPLVMD
TLEILGADNL AHGRWGEQKL VVRLAHQERP TAGSTLWLHL PENQLHLFDG ETGQRV
