SSUB_ECOK1
ID SSUB_ECOK1 Reviewed; 255 AA.
AC A1A9L0;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=Ecok1_08560;
GN ORFNames=APECO1_45;
OS Escherichia coli O1:K1 / APEC.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=405955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17293413; DOI=10.1128/jb.01726-06;
RA Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J.,
RA Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.;
RT "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7
RT shares strong similarities with human extraintestinal pathogenic E. coli
RT genomes.";
RL J. Bacteriol. 189:3228-3236(2007).
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; CP000468; ABJ00350.1; -; Genomic_DNA.
DR RefSeq; WP_001090487.1; NC_008563.1.
DR AlphaFoldDB; A1A9L0; -.
DR SMR; A1A9L0; -.
DR EnsemblBacteria; ABJ00350; ABJ00350; APECO1_45.
DR KEGG; ecv:APECO1_45; -.
DR HOGENOM; CLU_000604_1_22_6; -.
DR OMA; ADRANDW; -.
DR Proteomes; UP000008216; 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_0000279913"
FT DOMAIN 12..233
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01724"
FT BINDING 44..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01724"
SQ SEQUENCE 255 AA; 27709 MW; F960815A94DF9E85 CRC64;
MNTARLNQGT PLLLNAVSKH YAENIVLNQL DLHIPAGQFV AVVGRSGGGK STLLRLLAGL
ETPTAGDVLA GTTPLAEIQD DTRMMFQDAR LLPWKSVIDN VGLGLKGQWR DAARQALAAV
GLENRAGEWP AALSGGQKQR VALARALIHR PGLLLLDEPL GALDALTRLE MQDLIVSLWQ
EHGFTVLLVT HDVSEAVAMA DRVLLIEEGK IGLDLTVDIP RPRRLGSVRL AELEAEVLQR
VMQRGHSEQP IRRHG
