ID SSUB_PSEPU Reviewed; 270 AA.
AC Q8KZQ6; O85766;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 24-JAN-2024, entry version 100.
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};
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 6884 / S-313;
RX PubMed=10361295; DOI=10.1046/j.1365-2958.1999.01398.x;
RA Vermeij P., Wietek C., Kahnert A., Wueest T., Kertesz M.A.;
RT "Genetic organization of sulphur-controlled aryl desulphonation in
RT Pseudomonas putida S-313.";
RL Mol. Microbiol. 32:913-926(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN ALIPHATIC SULFONATES
RP TRANSPORT.
RC STRAIN=DS1;
RX PubMed=12835925; DOI=10.1007/s00253-003-1233-7;
RA Endoh T., Kasuga K., Horinouchi M., Yoshida T., Habe H., Nojiri H.,
RA Omori T.;
RT "Characterization and identification of genes essential for dimethyl
RT sulfide utilization in Pseudomonas putida strain DS1.";
RL Appl. Microbiol. Biotechnol. 62:83-91(2003).
RN [3]
RP FUNCTION IN ALIPHATIC SULFONATES TRANSPORT.
RC STRAIN=DSM 6884 / S-313;
RX PubMed=10781557; DOI=10.1128/jb.182.10.2869-2878.2000;
RA Kahnert A., Vermeij P., Wietek C., James P., Leisinger T., Kertesz M.A.;
RT "The ssu locus plays a key role in organosulfur metabolism in Pseudomonas
RT putida S-313.";
RL J. Bacteriol. 182:2869-2878(2000).
CC -!- FUNCTION: Part of the ABC transporter complex SsuABC involved in
CC aliphatic sulfonates import. Responsible for energy coupling to the
CC transport system (Probable). {ECO:0000305|PubMed:10781557,
CC ECO:0000305|PubMed:12835925}.
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; AF075709; AAC31907.1; -; Genomic_DNA.
DR EMBL; AB086390; BAC00975.1; -; Genomic_DNA.
DR RefSeq; WP_013970450.1; NZ_RJAI01000049.1.
DR AlphaFoldDB; Q8KZQ6; -.
DR SMR; Q8KZQ6; -.
DR TCDB; 3.A.1.17.2; the atp-binding cassette (abc) superfamily.
DR GeneID; 58533098; -.
DR eggNOG; COG1116; Bacteria.
DR OrthoDB; 9802264at2; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd03293; ABC_NrtD_SsuB_transporters; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 PANTHER; PTHR42788:SF17; ALIPHATIC SULFONATES IMPORT ATP-BINDING PROTEIN SSUB; 1.
DR PANTHER; PTHR42788; TAURINE IMPORT ATP-BINDING PROTEIN-RELATED; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS51291; SSUB; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Translocase; Transport.
FT CHAIN 1..270
FT /note="Aliphatic sulfonates import ATP-binding protein
FT SsuB"
FT /id="PRO_0000279935"
FT DOMAIN 17..238
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01724"
FT REGION 249..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 49..56
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01724"
FT CONFLICT 20
FT /note="S -> N (in Ref. 1; AAC31907)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="K -> R (in Ref. 1; AAC31907)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="E -> D (in Ref. 1; AAC31907)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="Q -> E (in Ref. 1; AAC31907)"
FT /evidence="ECO:0000305"
FT CONFLICT 81..82
FT /note="EQ -> AE (in Ref. 1; AAC31907)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="S -> K (in Ref. 1; AAC31907)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="P -> Q (in Ref. 1; AAC31907)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="E -> D (in Ref. 1; AAC31907)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="S -> A (in Ref. 1; AAC31907)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="S -> N (in Ref. 1; AAC31907)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="T -> N (in Ref. 1; AAC31907)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="A -> V (in Ref. 1; AAC31907)"
FT /evidence="ECO:0000305"
FT CONFLICT 252..253
FT /note="AA -> TP (in Ref. 1; AAC31907)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="D -> E (in Ref. 1; AAC31907)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 270 AA; 29324 MW; 74CBC7B36EB4045D CRC64;
MTVLKEQPPR LLRGIPLASS GLRKTFGQRE VLKGIELHIP AGQFVAIVGR SGCGKSTLLR
LLAGLDQPTA GQLLAGAAPL EQAREETRLM FQDARLLPWK KVIDNVGLGL SGDWRPRALE
ALESVGLADR ANEWPAALSG GQKQRVALAR ALIHQPRLLL LDEPLGALDA LTRIEMQQLI
ERLWRQHGFT VLLVTHDVSE AVAVADRVIL IEDGEVGLDL TVDLARPRAR GSHRLAALES
EVLNRVLSAP GAAPEPDPVA PLPTQLRWAH
//
