SSUB_BURTA
ID SSUB_BURTA Reviewed; 335 AA.
AC Q2SVN0;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=BTH_I2499;
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS E264).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
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; CP000086; ABC39266.1; -; Genomic_DNA.
DR RefSeq; WP_009909606.1; NZ_CP008785.1.
DR AlphaFoldDB; Q2SVN0; -.
DR SMR; Q2SVN0; -.
DR PRIDE; Q2SVN0; -.
DR EnsemblBacteria; ABC39266; ABC39266; BTH_I2499.
DR KEGG; bte:BTH_I2499; -.
DR HOGENOM; CLU_000604_1_22_4; -.
DR OMA; ADRANDW; -.
DR OrthoDB; 1200451at2; -.
DR Proteomes; UP000001930; Chromosome I.
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..335
FT /note="Aliphatic sulfonates import ATP-binding protein
FT SsuB"
FT /id="PRO_0000279905"
FT DOMAIN 74..293
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01724"
FT REGION 48..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 106..113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01724"
SQ SEQUENCE 335 AA; 35642 MW; AFB849E32A27A27E CRC64;
MTGTSLAATY GPIAGADLEA ELAQPRTADG DAQDAAVLER DGGAHALPFA SGGAFGRAPR
DDDDDRRGAG DASVRLTRVS KRYGERTVLA DVDLAIERGG FVSIVGRSGC GKSTLLRLVA
ELETPSAGTL VKRGDGGGVL DTRIMYQDAR LLPWKTVLQN VMLGLGRRAK DDARAVLDEV
GLLARAHDWP AQLSGGQRQR VALARALVHR PQLLLLDEPL GALDALTRIE MHELIERLWR
EHRFTALLVT HDVQEAVSLA DRILLIEAGR IAFDQPVPLE RPRARASAAF AELEDRVLQR
VLTGSDPAGA TSAAASAGGA ARGRAAQANG LRWAV