ID   SSUB_YERPS              Reviewed;         271 AA.
AC   Q665B6;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=YPTB3602;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BX936398; CAH22840.1; -; Genomic_DNA.
DR   RefSeq; WP_011193182.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q665B6; -.
DR   SMR; Q665B6; -.
DR   EnsemblBacteria; CAH22840; CAH22840; YPTB3602.
DR   GeneID; 66843980; -.
DR   KEGG; ypo:BZ17_2998; -.
DR   KEGG; yps:YPTB3602; -.
DR   PATRIC; fig|273123.14.peg.3136; -.
DR   OMA; ADRANDW; -.
DR   Proteomes; UP000001011; 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..271
FT                   /note="Aliphatic sulfonates import ATP-binding protein
FT                   SsuB"
FT                   /id="PRO_0000279970"
FT   DOMAIN          13..234
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01724"
FT   REGION          250..271
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        254..271
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         45..52
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01724"
SQ   SEQUENCE   271 AA;  29455 MW;  3FBADCC606ACCD3B CRC64;
     MTTLTHIPQG TPITLESIGK RYGNRTVLDN LQLRITAGQF VAVVGRSGCG KSTLLRLLAG
     LEAASDGTLL SGNALLSHAK DETRLMFQEA RLLPWKKVID NVGLGLRGHW RDDALQVLDT
     VGLADRANEW PAALSGGQKQ RVALARALIH RPRLLLLDEP LGALDALTRI EMQGLIERLW
     QQHGFTVLLV THDVSEAIAL ADRVLLIEEG RIGLDLAIDL PRPRRKGSAK LAALEAEVLE
     RVLSPPQGIE ASRQGIKASR QGTATSRRVA N