UGPC_CHRVO
ID UGPC_CHRVO Reviewed; 370 AA.
AC Q7NRX5;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 135.
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=CV_3653;
OS Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC
OS 12614 / NCIMB 9131 / NCTC 9757).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Chromobacterium.
OX NCBI_TaxID=243365;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC
RC 9757;
RX PubMed=14500782; DOI=10.1073/pnas.1832124100;
RA Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T.,
RA Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R.,
RA Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F.,
RA Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S.,
RA Belo A., van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M.,
RA Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P.,
RA Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S.,
RA Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N.,
RA Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P.,
RA Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R.,
RA Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B.,
RA Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J.,
RA Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F.,
RA Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z.,
RA de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F.,
RA Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A.,
RA Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C.,
RA Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M.,
RA Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C.,
RA Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R.,
RA Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M.,
RA Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R.,
RA Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.;
RT "The complete genome sequence of Chromobacterium violaceum reveals
RT remarkable and exploitable bacterial adaptability.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(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; AE016825; AAQ61315.1; -; Genomic_DNA.
DR RefSeq; WP_011137200.1; NC_005085.1.
DR AlphaFoldDB; Q7NRX5; -.
DR SMR; Q7NRX5; -.
DR STRING; 243365.CV_3653; -.
DR EnsemblBacteria; AAQ61315; AAQ61315; CV_3653.
DR KEGG; cvi:CV_3653; -.
DR eggNOG; COG3842; Bacteria.
DR HOGENOM; CLU_000604_1_1_4; -.
DR OMA; EPLICRC; -.
DR OrthoDB; 1200451at2; -.
DR Proteomes; UP000001424; Chromosome.
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; Reference proteome; Sugar transport; Translocase;
KW Transport.
FT CHAIN 1..370
FT /note="sn-glycerol-3-phosphate import ATP-binding protein
FT UgpC"
FT /id="PRO_0000289747"
FT DOMAIN 4..236
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01727"
FT BINDING 38..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01727"
SQ SEQUENCE 370 AA; 40490 MW; 594C7C9815FF4B57 CRC64;
MAKLSLKNIA KRYPGAERRV LEEISAEIAD GEFVVIVGPS GCGKSTLLRM VAGLESTEDG
EIRIGERLVN QLEPKDRDIA MVFQNYALYP HMTVAENMGY ALKLKGLKKV EIMERVLKVA
AVLELEQLLQ RKPRELSGGQ RQRVAMGRAI VREPAVFLFD EPLSNLDAKL RGQMRLEIQR
LHRRLATTSL YVTHDQVEAM TLADRVIVLN KGHIEQIGAP DEIYDRPATA FVAAFMGSPG
MNLFDAQADE SGERLLLGDG VSLALPAANP ALAGRRLKAG IRPEHLRAAG EGGETLSLRV
DSLEMLGADN YVYGLLAGQN VVARLAHGHR PEPGSRLEVA VRAESLHLFD AETQRRIEHA
AASQASLAVS
