ID   SSUB_YERPA              Reviewed;         271 AA.
AC   Q1C1S0;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
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=YPA_3640;
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua;
RX   PubMed=16740952; DOI=10.1128/jb.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA   Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT   evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(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; CP000308; ABG15602.1; -; Genomic_DNA.
DR   RefSeq; WP_002210036.1; NZ_CP009906.1.
DR   AlphaFoldDB; Q1C1S0; -.
DR   SMR; Q1C1S0; -.
DR   EnsemblBacteria; ABG15602; ABG15602; YPA_3640.
DR   GeneID; 57975053; -.
DR   KEGG; ypa:YPA_3640; -.
DR   OMA; ADRANDW; -.
DR   Proteomes; UP000001971; 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_0000279968"
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;  29469 MW;  31B4C6760707D730 CRC64;
     MTTLTHIPQG TPITLESIGK RYGNRTVLDN LQLRITAGQF VAVVGRSGCG KSTLLRLLAG
     LEAASDGTLL SGNALLSHAK DETRLMFQEA RLLPWKKVID NVGLGLRGHW RDEALQVLDT
     VGLADRANEW PAALSGGQKQ RVALARALIH RPRLLLLDEP LGALDALTRI EMQGLIERLW
     QQHGFTVLLV THDVSEAIAL ADRVLLIEEG RIGLDLAIDL PRPRRKGSAK LAALEAEVLE
     RVLSPPQGIE ASRQGIKASR QGTATSRRVA N