TAUB_SHIBS
ID TAUB_SHIBS Reviewed; 255 AA.
AC Q325N3;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=SBO_0260;
OS Shigella boydii serotype 4 (strain Sb227).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300268;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sb227;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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; CP000036; ABB64975.1; -; Genomic_DNA.
DR RefSeq; WP_000939377.1; NC_007613.1.
DR AlphaFoldDB; Q325N3; -.
DR SMR; Q325N3; -.
DR EnsemblBacteria; ABB64975; ABB64975; SBO_0260.
DR KEGG; sbo:SBO_0260; -.
DR HOGENOM; CLU_000604_1_22_6; -.
DR OMA; ALINCPK; -.
DR Proteomes; UP000007067; Chromosome.
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..255
FT /note="Taurine import ATP-binding protein TauB"
FT /id="PRO_0000275843"
FT DOMAIN 2..229
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01714"
FT BINDING 34..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01714"
SQ SEQUENCE 255 AA; 28265 MW; E277C7181CA6EB07 CRC64;
MLQISHLYAD YGGKPALEDI NLTLESGELL VVLGPSGCGK TTLLNLIAGF VPYQHGSIQL
AGKRIEGPGA ERGVVFQNEG LLPWRNVQDN VAFGLQLAGI EKMQRLEIAH QVLKKVGLEG
AEKRYIWQLS GGQRQRVGIA RALAANPQLL LLDEPFGALD AFTRDQMQTL LLKLWQETGK
QVLLITHDIE EAVFMATELV LLSSGPGRVL ERLPLNFARR FVAGESSRSI KSDPQFIAMR
EYVLSRVFEQ REAFS
