ID   TAUB_PSEPU              Reviewed;         262 AA.
AC   Q8KZR4;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 82.
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};
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DS1;
RX   PubMed=12835925; DOI=10.1007/s00253-003-1233-7;
RA   Endoh T., Kasuga K., Horinouchi M., Yoshida T., Habe H., Nojiri H.,
RA   Omori T.;
RT   "Characterization and identification of genes essential for dimethyl
RT   sulfide utilization in Pseudomonas putida strain DS1.";
RL   Appl. Microbiol. Biotechnol. 62:83-91(2003).
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; AB086390; BAC00967.1; -; Genomic_DNA.
DR   RefSeq; WP_023660883.1; NZ_LKKS01000120.1.
DR   AlphaFoldDB; Q8KZR4; -.
DR   SMR; Q8KZR4; -.
DR   STRING; 1240350.AMZE01000010_gene3804; -.
DR   GeneID; 58533090; -.
DR   eggNOG; COG4525; Bacteria.
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..262
FT                   /note="Taurine import ATP-binding protein TauB"
FT                   /id="PRO_0000093013"
FT   DOMAIN          4..233
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01714"
FT   BINDING         38..45
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01714"
SQ   SEQUENCE   262 AA;  28477 MW;  1BEBACCA4BF892D8 CRC64;
     MALLELERIS AQYPGAETPV LADINLSLGP RQLLVALGPS GSGKTSLLNL IAGFVAPSGG
     RITLDGVPVQ GPGAERGVVF QDDALLPWQN VLGNVAFGLE LAGVPRAERE AKAREMLALV
     DLDGFGERRI WQLSGGQKQR VGLARALAAD PRVLLMDEPF GALDAFTREQ MQELLLQVWQ
     RTAKPVFLIT HDIEEAVFLA SELVLLAPNP GRVVERLQLD FGQRYAAGES ARAIKSDPAF
     IETREHVLAR VFSQRQSLQE RA