SSUB1_PSEAB
ID SSUB1_PSEAB Reviewed; 249 AA.
AC Q02QT6;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Aliphatic sulfonates import ATP-binding protein SsuB 1 {ECO:0000255|HAMAP-Rule:MF_01724};
DE EC=7.6.2.14 {ECO:0000255|HAMAP-Rule:MF_01724};
GN Name=ssuB1 {ECO:0000255|HAMAP-Rule:MF_01724}; OrderedLocusNames=PA14_19520;
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; ABJ12703.1; -; Genomic_DNA.
DR RefSeq; WP_003091922.1; NZ_CP034244.1.
DR AlphaFoldDB; Q02QT6; -.
DR SMR; Q02QT6; -.
DR EnsemblBacteria; ABJ12703; ABJ12703; PA14_19520.
DR KEGG; pau:PA14_19520; -.
DR HOGENOM; CLU_000604_1_22_6; -.
DR OMA; QSIVTFP; -.
DR BioCyc; PAER208963:G1G74-1607-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..249
FT /note="Aliphatic sulfonates import ATP-binding protein SsuB
FT 1"
FT /id="PRO_0000279929"
FT DOMAIN 5..233
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01724"
FT BINDING 37..44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01724"
SQ SEQUENCE 249 AA; 27144 MW; 9CF98D127BBA881D CRC64;
MSGLLDLLEI RKAYGDTRVL EGVALSLAPG EVVSLLGPSG CGKSTLLRIA AGLDDDFQGT
VERNPILGFG PDGENGRSGG IGVVFQEPRL LPWLTVAQNV GFADGWLEDE HWVERLLADV
GLAGCGGLLP KQLSGGMAQR AAIARGLYGR PQVLLLDEPF SAVDAFTRMR LQDLLQDVVQ
NYEISVLLVT HDLDEAFYLA DRVLLMGGRP GHIRREFHVP LARPRDRRAV ELAYLRGEAL
TEMQRAHVL
