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SSUB_TRIV2
ID   SSUB_TRIV2              Reviewed;         255 AA.
AC   Q3M5J9;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=Ava_4138;
OS   Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29413 / PCC 7937;
RX   PubMed=25197444; DOI=10.4056/sigs.3899418;
RA   Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA   Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT   "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL   Stand. Genomic Sci. 9:562-573(2014).
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; CP000117; ABA23737.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3M5J9; -.
DR   SMR; Q3M5J9; -.
DR   STRING; 240292.Ava_4138; -.
DR   EnsemblBacteria; ABA23737; ABA23737; Ava_4138.
DR   KEGG; ava:Ava_4138; -.
DR   eggNOG; COG1116; Bacteria.
DR   HOGENOM; CLU_000604_1_22_3; -.
DR   OMA; HDMSLAR; -.
DR   Proteomes; UP000002533; 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..255
FT                   /note="Aliphatic sulfonates import ATP-binding protein
FT                   SsuB"
FT                   /id="PRO_0000279883"
FT   DOMAIN          10..231
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01724"
FT   BINDING         42..49
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01724"
SQ   SEQUENCE   255 AA;  28577 MW;  B50CC528AB7CEE9F CRC64;
     MVANLKGSRI NILDLTKAFG HKTVLNSLNL EVAPGEFIAI VGRSGCGKST LLRLVSGLDK
     PTTGGILLDG EPLRKLSHSV RVMFQEPRLL PWKRVIDNVG LGLQENWQSK ATWVLEQVGL
     KDRAGEWPHV LSGGQRQRVA LARALVSQPH LLLLDEPLGA LDALTRLEMQ YLIEDLWRER
     GFTAFLVTHD VEEAVALADR VIVIEEGRIM LDLPVRLPRP RDRASELFIN IREAVLEQVM
     NNESNNKNQL LQMSH
 
 
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