ID   UGPC_SALPA              Reviewed;         356 AA.
AC   Q5PJL1;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 116.
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=SPA3406;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000026; AAV79217.1; -; Genomic_DNA.
DR   RefSeq; WP_000907834.1; NC_006511.1.
DR   AlphaFoldDB; Q5PJL1; -.
DR   SMR; Q5PJL1; -.
DR   EnsemblBacteria; AAV79217; AAV79217; SPA3406.
DR   KEGG; spt:SPA3406; -.
DR   HOGENOM; CLU_000604_1_1_6; -.
DR   OMA; PRNMYDK; -.
DR   Proteomes; UP000008185; 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; Sugar transport; Translocase; Transport.
FT   CHAIN           1..356
FT                   /note="sn-glycerol-3-phosphate import ATP-binding protein
FT                   UgpC"
FT                   /id="PRO_0000289779"
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;  39414 MW;  80782E8623E96746 CRC64;
     MAGLKLQAVT KSWDGKTQVI QPLTLDVADG EFIVMVGPSG CGKSTLLRMV AGLERVTSGD
     IWIDRKRVTE MEPKDRGIAI VFQNYALYPH MSVEENMAWG LKIRGMSKAH IEERVREAAR
     ILELDGLLKR RPRELSGGQR QRVAMGRAIV REPAVFLFDE PLSNLDAKLR VQMRLELQHL
     HRRLRTTSLY VTHDQVEAMT LAQRVMVMNK GVAEQIGTPV EVYEKPASRF VASFIGSPAM
     NLLDGVISAS GDRFELPGGL ALPIGAGYRG HAGRKMTLGI RPEHIALSSQ AEGGVPLTVD
     TLEILGADNL AHGRWGDQKL VVRLAHQQRP AAGSTLWLHL PEHQRHLFDG ETGQRV