TAUB_CUPPJ
ID TAUB_CUPPJ Reviewed; 258 AA.
AC Q471U2;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Taurine import ATP-binding protein TauB {ECO:0000255|HAMAP-Rule:MF_01714};
DE EC=7.6.2.7 {ECO:0000255|HAMAP-Rule:MF_01714};
GN Name=tauB {ECO:0000255|HAMAP-Rule:MF_01714}; OrderedLocusNames=Reut_A1471;
OS Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS (strain JMP 134)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=264198;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JMP134 / LMG 1197;
RX PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA Kyrpides N.C.;
RT "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT versatile pollutant degrader.";
RL PLoS ONE 5:E9729-E9729(2010).
CC -!- FUNCTION: Part of the ABC transporter complex TauABC involved in
CC taurine import. Responsible for energy coupling to the transport
CC system. {ECO:0000255|HAMAP-Rule:MF_01714}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + taurine(out) = ADP + H(+) + phosphate +
CC taurine(in); Xref=Rhea:RHEA:14613, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216, ChEBI:CHEBI:507393; EC=7.6.2.7;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01714};
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (TauB),
CC two transmembrane proteins (TauC) and a solute-binding protein (TauA).
CC {ECO:0000255|HAMAP-Rule:MF_01714}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01714}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01714}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Taurine
CC importer (TC 3.A.1.17.1) family. {ECO:0000255|HAMAP-Rule:MF_01714}.
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DR EMBL; CP000090; AAZ60841.1; -; Genomic_DNA.
DR RefSeq; WP_011297640.1; NC_007347.1.
DR AlphaFoldDB; Q471U2; -.
DR SMR; Q471U2; -.
DR STRING; 264198.Reut_A1471; -.
DR EnsemblBacteria; AAZ60841; AAZ60841; Reut_A1471.
DR KEGG; reu:Reut_A1471; -.
DR eggNOG; COG4525; Bacteria.
DR HOGENOM; CLU_000604_1_22_4; -.
DR OMA; KGFENHW; -.
DR OrthoDB; 1832232at2; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IPR015859; ABC_transpr_TauB.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR42788:SF18; PTHR42788:SF18; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS51250; TAUB; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Translocase; Transport.
FT CHAIN 1..258
FT /note="Taurine import ATP-binding protein TauB"
FT /id="PRO_0000275839"
FT DOMAIN 4..236
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01714"
FT BINDING 41..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01714"
SQ SEQUENCE 258 AA; 28300 MW; 49DB3FB4549ECE47 CRC64;
MSRLEIDKVS VNYGGRGGAQ TLALSQVNLT MERGDFVVAL GASGCGKTTL LSCIAGFMQP
SEGEIRLDGK PVLGPGAERG VVFQKHALMP WLNVADNVAL GLRLRGVNRA ERLRIAHEKL
AQVGLEKVAS KPVYQLSGGM QQRVGIARAL ANDPEVMLMD EPLGALDALT RESIQALILR
LWAREQKIVF FITHSVEEAL FLATRLIVMT PSPGRIAHSY DLPFARRYIE CGDARAVKSD
PEFIRYREEI VDLIHATP