SSUB_SHIF8
ID SSUB_SHIF8 Reviewed; 255 AA.
AC Q0T6A8;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=SFV_0935;
OS Shigella flexneri serotype 5b (strain 8401).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=373384;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8401;
RX PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT "Complete genome sequence of Shigella flexneri 5b and comparison with
RT Shigella flexneri 2a.";
RL BMC Genomics 7:173-173(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; CP000266; ABF03157.1; -; Genomic_DNA.
DR RefSeq; WP_001090477.1; NC_008258.1.
DR AlphaFoldDB; Q0T6A8; -.
DR SMR; Q0T6A8; -.
DR EnsemblBacteria; ABF03157; ABF03157; SFV_0935.
DR GeneID; 58391194; -.
DR KEGG; sfv:SFV_0935; -.
DR HOGENOM; CLU_000604_1_22_6; -.
DR OMA; ADRANDW; -.
DR BioCyc; SFLE373384:SFV_RS05185-MON; -.
DR Proteomes; UP000000659; 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_0000279961"
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; 27791 MW; 6F340C4AA5A28E12 CRC64;
MNTARLNQGT PLLLNAVSKH YAENIVLNQL DLHIPAGQFV AVVGRSGGGK STLLHLLAGL
ETPTAGDVLA GTTPLAEIQD DTRMMFQDAR LLPWKSVIDN VGLGLKGQWR DAARRALAAV
GLENRAGEWP AALSGGQKQR VALARALIHR PGLLLLDEPL GALDALTRLE MQDLIVSLWQ
QHGFTVLLVT HDVSEAVAMA DRVLLIEEGK ISLDLTVDIP RPRRLGSVRL AELEAEVLQR
VMRRGHSEQL IRRHG
