ID   SSUB_ECOUT              Reviewed;         255 AA.
AC   Q1RDS4;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
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}; OrderedLocusNames=UTI89_C1005;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC;
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
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; CP000243; ABE06490.1; -; Genomic_DNA.
DR   RefSeq; WP_001090487.1; NC_007946.1.
DR   AlphaFoldDB; Q1RDS4; -.
DR   SMR; Q1RDS4; -.
DR   EnsemblBacteria; ABE06490; ABE06490; UTI89_C1005.
DR   KEGG; eci:UTI89_C1005; -.
DR   HOGENOM; CLU_000604_1_22_6; -.
DR   OMA; ADRANDW; -.
DR   Proteomes; UP000001952; 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; 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..255
FT                   /note="Aliphatic sulfonates import ATP-binding protein
FT                   SsuB"
FT                   /id="PRO_0000279912"
FT   DOMAIN          12..233
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01724"
FT   BINDING         44..51
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01724"
SQ   SEQUENCE   255 AA;  27709 MW;  F960815A94DF9E85 CRC64;
     MNTARLNQGT PLLLNAVSKH YAENIVLNQL DLHIPAGQFV AVVGRSGGGK STLLRLLAGL
     ETPTAGDVLA GTTPLAEIQD DTRMMFQDAR LLPWKSVIDN VGLGLKGQWR DAARQALAAV
     GLENRAGEWP AALSGGQKQR VALARALIHR PGLLLLDEPL GALDALTRLE MQDLIVSLWQ
     EHGFTVLLVT HDVSEAVAMA DRVLLIEEGK IGLDLTVDIP RPRRLGSVRL AELEAEVLQR
     VMQRGHSEQP IRRHG