SSUC_ECOLI
ID SSUC_ECOLI Reviewed; 263 AA.
AC P75851;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Putative aliphatic sulfonates transport permease protein SsuC;
GN Name=ssuC; Synonyms=ycbM; OrderedLocusNames=b0934, JW5121;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 TOPOLOGY.
RC STRAIN=K12 / JM109 / ATCC 53323;
RX PubMed=11867724; DOI=10.1073/pnas.052018199;
RA Drew D., Sjoestrand D., Nilsson J., Urbig T., Chin C.-N., de Gier J.-W.,
RA von Heijne G.;
RT "Rapid topology mapping of Escherichia coli inner-membrane proteins by
RT prediction and PhoA/GFP fusion analysis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:2690-2695(2002).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- FUNCTION: Part of a binding-protein-dependent transport system for
CC aliphatic sulfonates. Probably responsible for the translocation of the
CC substrate across the membrane.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. CysTW subfamily. {ECO:0000305}.
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DR EMBL; AJ237695; CAB40392.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74020.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA35689.2; -; Genomic_DNA.
DR PIR; E64833; E64833.
DR RefSeq; NP_415454.4; NC_000913.3.
DR RefSeq; WP_000235203.1; NZ_STEB01000006.1.
DR AlphaFoldDB; P75851; -.
DR SMR; P75851; -.
DR BioGRID; 4260017; 16.
DR ComplexPortal; CPX-4313; Aliphatic sulfonate ABC transporter complex.
DR STRING; 511145.b0934; -.
DR TCDB; 3.A.1.17.10; the atp-binding cassette (abc) superfamily.
DR PaxDb; P75851; -.
DR EnsemblBacteria; AAC74020; AAC74020; b0934.
DR EnsemblBacteria; BAA35689; BAA35689; BAA35689.
DR GeneID; 66670790; -.
DR GeneID; 947216; -.
DR KEGG; ecj:JW5121; -.
DR KEGG; eco:b0934; -.
DR PATRIC; fig|1411691.4.peg.1340; -.
DR EchoBASE; EB3469; -.
DR eggNOG; COG0600; Bacteria.
DR HOGENOM; CLU_046113_1_2_6; -.
DR InParanoid; P75851; -.
DR OMA; LRWHPGY; -.
DR PhylomeDB; P75851; -.
DR BioCyc; EcoCyc:YCBM-MON; -.
DR BioCyc; MetaCyc:YCBM-MON; -.
DR PRO; PR:P75851; -.
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:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0042959; F:alkanesulfonate transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042918; P:alkanesulfonate transport; IBA:GO_Central.
DR GO; GO:0010438; P:cellular response to sulfur starvation; IC:ComplexPortal.
DR GO; GO:0006790; P:sulfur compound metabolic process; IGI:EcoliWiki.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; -; 1.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR Pfam; PF00528; BPD_transp_1; 1.
DR SUPFAM; SSF161098; SSF161098; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..263
FT /note="Putative aliphatic sulfonates transport permease
FT protein SsuC"
FT /id="PRO_0000060228"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 35..43
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 65..68
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 90..102
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..122
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 123..125
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..148
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 149..164
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 186..187
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 209..217
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 239..263
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 58..242
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 263 AA; 28925 MW; DF84985E95116FA2 CRC64;
MATPVKKWLL RVAPWFLPVG IVAVWQLASS VGWLSTRILP SPEGVVTAFW TLSASGELWQ
HLAISSWRAL IGFSIGGSLG LILGLISGLS RWGERLLDTS IQMLRNVPHL ALIPLVILWF
GIDESAKIFL VALGTLFPIY INTWHGIRNI DRGLVEMARS YGLSGIPLFI HVILPGALPS
IMVGVRFALG LMWLTLIVAE TISANSGIGY LAMNAREFLQ TDVVVVAIIL YALLGKLADV
SAQLLERLWL RWNPAYHLKE ATV
