SSUB_ECOLI
ID SSUB_ECOLI Reviewed; 255 AA.
AC P0AAI1; P38053; P75850;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 127.
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, ECO:0000305|PubMed:10506196};
GN Name=ssuB {ECO:0000255|HAMAP-Rule:MF_01724}; Synonyms=ycbE;
GN OrderedLocusNames=b0933, JW0916;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN ALIPHATIC SULFONATES
RP TRANSPORT, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=10506196; DOI=10.1074/jbc.274.41.29358;
RA Van der Ploeg J.R., Iwanicka-Nowicka R., Bykowski T., Hryniewicz M.M.,
RA Leisinger T.;
RT "The Escherichia coli ssuEADCB gene cluster is required for the utilization
RT of sulfur from aliphatic sulfonates and is regulated by the transcriptional
RT activator Cbl.";
RL J. Biol. Chem. 274:29358-29365(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 161-255.
RC STRAIN=K12;
RX PubMed=3549459; DOI=10.1016/0378-1119(86)90360-4;
RA McCaman M.T., Gabe J.D.;
RT "The nucleotide sequence of the pepN gene and its over-expression in
RT Escherichia coli.";
RL Gene 48:145-153(1986).
RN [6]
RP IDENTIFICATION.
RX PubMed=7984428; DOI=10.1093/nar/22.22.4756;
RA Borodovsky M., Rudd K.E., Koonin E.V.;
RT "Intrinsic and extrinsic approaches for detecting genes in a bacterial
RT genome.";
RL Nucleic Acids Res. 22:4756-4767(1994).
RN [7]
RP FUNCTION IN ALIPHATIC SULFONATES TRANSPORT.
RC STRAIN=K12;
RX PubMed=10781534; DOI=10.1128/jb.182.10.2687-2695.2000;
RA Eichhorn E., van der Ploeg J.R., Leisinger T.;
RT "Deletion analysis of the Escherichia coli taurine and alkanesulfonate
RT transport systems.";
RL J. Bacteriol. 182:2687-2695(2000).
RN [8]
RP REVIEW.
RX PubMed=11479697; DOI=10.1007/s002030100298;
RA van der Ploeg J.R., Eichhorn E., Leisinger T.;
RT "Sulfonate-sulfur metabolism and its regulation in Escherichia coli.";
RL Arch. Microbiol. 176:1-8(2001).
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:10506196,
CC ECO:0000305|PubMed:10781534}.
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 ECO:0000305|PubMed:10506196};
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 -!- INDUCTION: Repressed by sulfate and cystine. Transcriptionally
CC regulated by cbl. {ECO:0000269|PubMed:10506196}.
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; AJ237695; CAB40393.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74019.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35685.1; -; Genomic_DNA.
DR EMBL; M15273; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; D64833; D64833.
DR RefSeq; NP_415453.1; NC_000913.3.
DR RefSeq; WP_001090506.1; NZ_SSZK01000002.1.
DR AlphaFoldDB; P0AAI1; -.
DR SMR; P0AAI1; -.
DR BioGRID; 4261879; 14.
DR BioGRID; 851552; 1.
DR ComplexPortal; CPX-4313; Aliphatic sulfonate ABC transporter complex.
DR IntAct; P0AAI1; 7.
DR STRING; 511145.b0933; -.
DR PaxDb; P0AAI1; -.
DR PRIDE; P0AAI1; -.
DR EnsemblBacteria; AAC74019; AAC74019; b0933.
DR EnsemblBacteria; BAA35685; BAA35685; BAA35685.
DR GeneID; 60899829; -.
DR GeneID; 947220; -.
DR KEGG; ecj:JW0916; -.
DR KEGG; eco:b0933; -.
DR PATRIC; fig|1411691.4.peg.1341; -.
DR EchoBASE; EB2261; -.
DR eggNOG; COG1116; Bacteria.
DR HOGENOM; CLU_000604_1_22_6; -.
DR InParanoid; P0AAI1; -.
DR OMA; ADRANDW; -.
DR PhylomeDB; P0AAI1; -.
DR BioCyc; EcoCyc:YCBE-MON; -.
DR BioCyc; MetaCyc:YCBE-MON; -.
DR PRO; PR:P0AAI1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC:ComplexPortal.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0042959; F:alkanesulfonate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISM:EcoCyc.
DR GO; GO:0010438; P:cellular response to sulfur starvation; IC:ComplexPortal.
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 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Reference proteome; Translocase; Transport.
FT CHAIN 1..255
FT /note="Aliphatic sulfonates import ATP-binding protein
FT SsuB"
FT /id="PRO_0000092976"
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"
FT CONFLICT 161..165
FT /note="GALDA -> RGAGR (in Ref. 5; M15273)"
FT /evidence="ECO:0000305"
FT CONFLICT 232..233
FT /note="EL -> DV (in Ref. 5; M15273)"
FT /evidence="ECO:0000305"
FT CONFLICT 236..237
FT /note="EV -> RS (in Ref. 5; M15273)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 255 AA; 27738 MW; 6FA276AD6E7FACE1 CRC64;
MNTARLNQGT PLLLNAVSKH YAENIVLNQL DLHIPAGQFV AVVGRSGGGK STLLRLLAGL
ETPTAGDVLA GTTPLAEIQE DTRMMFQDAR LLPWKSVIDN VGLGLKGQWR DAARRALAAV
GLENRAGEWP AALSGGQKQR VALARALIHR PGLLLLDEPL GALDALTRLE MQDLIVSLWQ
EHGFTVLLVT HDVSEAVAMA DRVLLIEEGK IGLDLTVDIP RPRRLGSVRL AELEAEVLQR
VMQRGESETR LRKQG
