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SSUB3_ALKCK
ID   SSUB3_ALKCK             Reviewed;         247 AA.
AC   Q5WBL0;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Aliphatic sulfonates import ATP-binding protein SsuB 3 {ECO:0000255|HAMAP-Rule:MF_01724};
DE            EC=7.6.2.14 {ECO:0000255|HAMAP-Rule:MF_01724};
GN   Name=ssuB3 {ECO:0000255|HAMAP-Rule:MF_01724}; OrderedLocusNames=ABC3717;
OS   Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=66692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16;
RA   Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA   Kawai S., Ito S., Horikoshi K.;
RT   "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT   K16.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
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 membrane {ECO:0000255|HAMAP-Rule:MF_01724};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-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; AP006627; BAD66250.1; -; Genomic_DNA.
DR   RefSeq; WP_011248555.1; NC_006582.1.
DR   AlphaFoldDB; Q5WBL0; -.
DR   SMR; Q5WBL0; -.
DR   STRING; 66692.ABC3717; -.
DR   EnsemblBacteria; BAD66250; BAD66250; ABC3717.
DR   KEGG; bcl:ABC3717; -.
DR   eggNOG; COG1116; Bacteria.
DR   HOGENOM; CLU_000604_1_22_9; -.
DR   OMA; DHDANEA; -.
DR   OrthoDB; 1200451at2; -.
DR   Proteomes; UP000001168; 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 membrane; Membrane; Nucleotide-binding;
KW   Reference proteome; Translocase; Transport.
FT   CHAIN           1..247
FT                   /note="Aliphatic sulfonates import ATP-binding protein SsuB
FT                   3"
FT                   /id="PRO_0000279890"
FT   DOMAIN          14..235
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01724"
FT   BINDING         46..53
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01724"
SQ   SEQUENCE   247 AA;  27279 MW;  34580C5539900F07 CRC64;
     MAIAKQTTKR GVEIRIAQLQ KTFGDQNVIK DITLTIEAGQ FVAIVGKSGS GKSTLLRLVA
     GLEQPSSGDL LFNGATLKKS QASITMMYQD SRLLPWKKVI DNVGLGLKGN WQQKGESVLH
     AVGLSAFSNE WPSTLSGGQQ QRVALARALI REPDLLMLDE PLSALDALTR SEMQDLIETI
     WQENQFTALL VTHDVREAVK LADRIILIEE GVIALDVENP LSRPRDVTNK QLIELEKQVT
     SRILEKE
 
 
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