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UGPC_RUEPO
ID   UGPC_RUEPO              Reviewed;         351 AA.
AC   Q5LX21;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 124.
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=SPO0237;
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS   pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA   Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT   environment.";
RL   Nature 432:910-913(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
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; CP000031; AAV93562.1; -; Genomic_DNA.
DR   RefSeq; WP_011046004.1; NC_003911.12.
DR   AlphaFoldDB; Q5LX21; -.
DR   SMR; Q5LX21; -.
DR   STRING; 246200.SPO0237; -.
DR   EnsemblBacteria; AAV93562; AAV93562; SPO0237.
DR   KEGG; sil:SPO0237; -.
DR   eggNOG; COG3842; Bacteria.
DR   HOGENOM; CLU_000604_1_1_5; -.
DR   OMA; APPMNLM; -.
DR   OrthoDB; 1200451at2; -.
DR   Proteomes; UP000001023; 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; Reference proteome; Sugar transport; Translocase;
KW   Transport.
FT   CHAIN           1..351
FT                   /note="sn-glycerol-3-phosphate import ATP-binding protein
FT                   UgpC"
FT                   /id="PRO_0000289784"
FT   DOMAIN          4..234
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01727"
FT   BINDING         36..43
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01727"
SQ   SEQUENCE   351 AA;  38140 MW;  293A77EBABC49319 CRC64;
     MASITLDNLV KAYGDTEVLH HVAGQIEDGE FIVIVGPSGC GKSTLLRMVA GLETVTAGQI
     SIGDRVVNQL EPADRDIAMV FQNYALYPHM SVRENMAYGL KIRKISKDEI ARRVEEAADI
     LELRPYLDRK PRQLSGGQRQ RVAMGRAIVR NPQVFLFDEP LSNLDAKLRV QMRLEIRKLQ
     QRLGVTSIYV THDQVEAMTL GDRLMVLNGG YVEQFGTPIE LYDRPATTFV AGFIGSPAMN
     FLPATAAEGS VTLANGARIA GSGTAHGTVT LGLRPEHLLP DEGGPVRVRV ELVEQLGANS
     LLHGQLEGTD TEMVVSMPGH MSAAADAVMA FTPTADSLHL FDPETGKRIA E
 
 
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