UGPC_RHIME
ID UGPC_RHIME Reviewed; 349 AA.
AC Q92WD6;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
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=RB0405;
GN ORFNames=SMb20419;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OG Plasmid pSymB (megaplasmid 2).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481431; DOI=10.1073/pnas.161294698;
RA Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorhoelter F.J.,
RA Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puehler A.;
RT "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing
RT endosymbiont Sinorhizobium meliloti.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(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}.
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DR EMBL; AL591985; CAC48805.1; -; Genomic_DNA.
DR PIR; E95892; E95892.
DR RefSeq; NP_436945.1; NC_003078.1.
DR RefSeq; WP_010975293.1; NC_003078.1.
DR AlphaFoldDB; Q92WD6; -.
DR SMR; Q92WD6; -.
DR STRING; 266834.SM_b20419; -.
DR EnsemblBacteria; CAC48805; CAC48805; SM_b20419.
DR GeneID; 25012751; -.
DR GeneID; 61600412; -.
DR KEGG; sme:SM_b20419; -.
DR PATRIC; fig|266834.11.peg.5334; -.
DR eggNOG; COG3842; Bacteria.
DR HOGENOM; CLU_000604_1_1_5; -.
DR OMA; APPMNLM; -.
DR PRO; PR:Q92WD6; -.
DR Proteomes; UP000001976; Plasmid pSymB.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
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; IPR027417; P-loop_NTPase.
DR InterPro; IPR013611; Transp-assoc_OB_typ2.
DR InterPro; IPR017922; UgpC.
DR PANTHER; PTHR43875:SF12; PTHR43875:SF12; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF08402; TOBE_2; 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; Plasmid; Reference proteome; Sugar transport;
KW Translocase; Transport.
FT CHAIN 1..349
FT /note="sn-glycerol-3-phosphate import ATP-binding protein
FT UgpC"
FT /id="PRO_0000289769"
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 349 AA; 37854 MW; 06DB882EBABB820C CRC64;
MATITLKDVH KTYHGDIAAI RGVSLAIADG EFIVLVGPSG CGKSTLLRMI AGLESITSGE
ISIGDRVVNG LEPSERDIAM VFQNYALYPH MTVRQNLSYG LKNRNTPKEE IERRIAKAAK
SLEIEPFLDR KPRQLSGGQR QRVAMGRAIV REPAAFLFDE PLSNLDAKLR VQMRVEIKRL
QRALGTTSVY VTHDQLEAMT LADRLVVLNG GRIEQVGTPI ELYENPATAF VATFIGSPSM
NLLDLNTGNA AWSAPAALVG KPGLATIGIR PEDITLAGDT DGGERFRARV RVGAVELVGA
ESYVHGTLAN GEPLVFRVAG RSRMMIDEEV EVAAVAGSLH WFDAAGRRL
