TAUB_PARPN
ID TAUB_PARPN Reviewed; 269 AA.
AC Q6RH47; Q6RH56;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 76.
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 Paracoccus pantotrophus (Thiosphaera pantotropha).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Paracoccus.
OX NCBI_TaxID=82367;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 17741 / DSM 65 / LMG 4218, and DSM 12449 / NKNCYSA;
RX PubMed=15073291; DOI=10.1099/mic.0.26795-0;
RA Brueggemann C., Denger K., Cook A.M., Ruff J.;
RT "Enzymes and genes of taurine and isethionate dissimilation in Paracoccus
RT denitrificans.";
RL Microbiology 150:805-816(2004).
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; AY498614; AAS78791.1; -; Genomic_DNA.
DR EMBL; AY498615; AAS78800.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6RH47; -.
DR SMR; Q6RH47; -.
DR STRING; 935565.JAEM01000047_gene683; -.
DR eggNOG; COG4525; Bacteria.
DR BRENDA; 1.4.99.2; 4531.
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..269
FT /note="Taurine import ATP-binding protein TauB"
FT /id="PRO_0000093010"
FT DOMAIN 4..237
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01714"
FT BINDING 42..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01714"
FT VARIANT 40
FT /note="A -> V (in strain: DSM 65)"
FT VARIANT 70
FT /note="D -> G (in strain: DSM 65)"
FT VARIANT 74
FT /note="A -> T (in strain: DSM 65)"
FT VARIANT 79
FT /note="E -> D (in strain: DSM 65)"
FT VARIANT 264
FT /note="Q -> R (in strain: DSM 65)"
SQ SEQUENCE 269 AA; 29674 MW; 3FDBC12E6C3A2420 CRC64;
MQTLKVSDVS LIYPGHHKGA PVTALKGVNL EVKSGDFVVA LGASGCGKTT LLNLMAGFMA
PSAGQITLGD RPVAGPGAER GVVFQKHALL PWLNVIDNVE FGLKLQGVDA RTRRERAVKN
LALVGLQDFH KHMIYHLSGG MQQRVGIARA LTCDPAMLLM DEPMAALDAL TRETVQELLL
QIWQQTDKMY FFITHSVEEA LFLGSRLIVM SPRPGRITHT YELDFNRRFL AEGNARAIKS
SPDFIEMREQ ILGIIYGDER AGEQEKIHA
