SSUB2_PSEAB
ID SSUB2_PSEAB Reviewed; 274 AA.
AC Q02QT1;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Aliphatic sulfonates import ATP-binding protein SsuB 2 {ECO:0000255|HAMAP-Rule:MF_01724};
DE EC=7.6.2.14 {ECO:0000255|HAMAP-Rule:MF_01724};
GN Name=ssuB2 {ECO:0000255|HAMAP-Rule:MF_01724}; OrderedLocusNames=PA14_19580;
OS Pseudomonas aeruginosa (strain UCBPP-PA14).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCBPP-PA14;
RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT combinatorial.";
RL Genome Biol. 7:R90.1-R90.14(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; CP000438; ABJ12698.1; -; Genomic_DNA.
DR RefSeq; WP_003117544.1; NZ_CP034244.1.
DR AlphaFoldDB; Q02QT1; -.
DR SMR; Q02QT1; -.
DR PRIDE; Q02QT1; -.
DR EnsemblBacteria; ABJ12698; ABJ12698; PA14_19580.
DR KEGG; pau:PA14_19580; -.
DR HOGENOM; CLU_000604_1_22_6; -.
DR OMA; ADRANDW; -.
DR BioCyc; PAER208963:G1G74-1612-MON; -.
DR Proteomes; UP000000653; 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..274
FT /note="Aliphatic sulfonates import ATP-binding protein SsuB
FT 2"
FT /id="PRO_0000279930"
FT DOMAIN 21..242
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01724"
FT BINDING 53..60
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01724"
SQ SEQUENCE 274 AA; 29855 MW; 61DB567248209B02 CRC64;
MNAHNAALGG TPQRLKRGIP LALRGVARRF GEREVLKDID LLVPAGQFVA IVGRSGCGKS
TLLRLLAGLD QPSRGELLAG SAALAEARED TRLMFQDSRL LPWKRVIDNV GLGLRGDWRA
KARQALRAVG LAERANEWPA ALSGGQKQRV ALARALIHEP RLLLLDEPLG ALDALTRIEM
QQLIEGLWRE HGFTVLLVTH DVSEAVAVAD RVILIEDGEI GLDLPVELPR PRSRGSARLA
ALEAEVLNRV LAQPELPPQP EPVSPLPTQL RWAL
