ID   SSUB_DELAC              Reviewed;         241 AA.
AC   Q8RLB6;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Aliphatic sulfonates import ATP-binding protein SsuB {ECO:0000255|HAMAP-Rule:MF_01724};
DE            EC=7.6.2.14 {ECO:0000255|HAMAP-Rule:MF_01724};
GN   Name=ssuB {ECO:0000255|HAMAP-Rule:MF_01724};
OS   Delftia acidovorans (Pseudomonas acidovorans) (Comamonas acidovorans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Delftia.
OX   NCBI_TaxID=80866;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 15668 / DSM 39 / BCRC 14819 / JCM 5833 / NBRC 14950 / NCIMB
RC   9681 / NCTC 10683 / 2167;
RX   PubMed=14622263; DOI=10.1046/j.1432-1033.2003.03875.x;
RA   Ivanov N.V., Hubalek F., Trani M., Edmondson D.E.;
RT   "Factors involved in the assembly of a functional molybdopyranopterin
RT   center in recombinant Comamonas acidovorans xanthine dehydrogenase.";
RL   Eur. J. Biochem. 270:4744-4754(2003).
CC   -!- FUNCTION: Part of the ABC transporter complex SsuABC involved in
CC       aliphatic sulfonates import. Responsible for energy coupling to the
CC       transport system. {ECO:0000255|HAMAP-Rule:MF_01724}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + aliphatic sulfonate-[sulfonate-binding
CC         protein]Side 1 = ADP + phosphate + aliphatic sulfonateSide 2 +
CC         [sulfonate-binding protein]Side 1.; EC=7.6.2.14;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01724};
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (SsuB),
CC       two transmembrane proteins (SsuC) and a solute-binding protein (SsuA).
CC       {ECO:0000255|HAMAP-Rule:MF_01724}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01724}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01724}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Aliphatic
CC       sulfonates importer (TC 3.A.1.17.2) family. {ECO:0000255|HAMAP-
CC       Rule:MF_01724}.
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DR   EMBL; AY082333; AAL92576.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8RLB6; -.
DR   SMR; Q8RLB6; -.
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; IPR027417; P-loop_NTPase.
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; PS51291; SSUB; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Translocase; Transport.
FT   CHAIN           1..241
FT                   /note="Aliphatic sulfonates import ATP-binding protein
FT                   SsuB"
FT                   /id="PRO_0000279909"
FT   DOMAIN          10..226
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01724"
FT   BINDING         42..49
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01724"
SQ   SEQUENCE   241 AA;  25984 MW;  AACEAE81970F2D2B CRC64;
     MNRPSLAGAV HLHGFSRSFH GKQVLDDLGL DIAPGQFVAL LGESGSGKTT LLRALAGLDV
     EARSSGTAVA HGNVSVLFQD SRLLPWLTVL DNLTLGLDAQ AVRPAAAQLL REVGLADKAA
     AWPASLSGGQ KQRAALARSL LREPHVLLAD EPFGALDALT RLRMQGLLRR MVERVRPTVI
     LVTHDVDESL LLADRILVLR DGKIAEDHAL DLAHPRRPDH PAFMQLRATL LRSLGVEAEF
     V