ID   SFSA_ECOLI              Reviewed;         234 AA.
AC   P0A823; P18273;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Sugar fermentation stimulation protein A {ECO:0000255|HAMAP-Rule:MF_00095};
GN   Name=sfsA {ECO:0000255|HAMAP-Rule:MF_00095}; Synonyms=sfs1;
GN   OrderedLocusNames=b0146, JW0142;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2180916; DOI=10.1128/jb.172.4.2055-2064.1990;
RA   Kang P.J., Craig E.A.;
RT   "Identification and characterization of a new Escherichia coli gene that is
RT   a dosage-dependent suppressor of a dnaK deletion mutation.";
RL   J. Bacteriol. 172:2055-2064(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=2013578; DOI=10.1128/jb.173.8.2644-2648.1991;
RA   Kawamukai M., Utsumi R., Takeda K., Higashi A., Matsuda H., Choi Y.-L.,
RA   Komano T.;
RT   "Nucleotide sequence and characterization of the sfs1 gene: sfs1 is
RT   involved in CRP*-dependent mal gene expression in Escherichia coli.";
RL   J. Bacteriol. 173:2644-2648(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8202364; DOI=10.1093/nar/22.9.1637;
RA   Fujita N., Mori H., Yura T., Ishihama A.;
RT   "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-
RT   4.1 min (110,917-193,643 bp) region.";
RL   Nucleic Acids Res. 22:1637-1639(1994).
RN   [4]
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   [5]
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   [6]
RP   FUNCTION, DNA-BINDING, AND DISRUPTION PHENOTYPE.
RX   PubMed=11272834; DOI=10.1271/bbb.65.213;
RA   Takeda K., Akimoto C., Kawamukai M.;
RT   "Effects of the Escherichia coli sfsA gene on mal genes expression and a
RT   DNA binding activity of SfsA.";
RL   Biosci. Biotechnol. Biochem. 65:213-217(2001).
CC   -!- FUNCTION: Binds to DNA non-specifically. Could be a regulatory factor
CC       involved in maltose metabolism. {ECO:0000255|HAMAP-Rule:MF_00095,
CC       ECO:0000269|PubMed:11272834, ECO:0000269|PubMed:2013578}.
CC   -!- INTERACTION:
CC       P0A823; P0AFT5: btsR; NbExp=2; IntAct=EBI-556413, EBI-556431;
CC       P0A823; P07004: proA; NbExp=4; IntAct=EBI-556413, EBI-548584;
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC       {ECO:0000269|PubMed:11272834}.
CC   -!- SIMILARITY: Belongs to the SfsA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00095}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=M34945; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; M34945; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; M60726; AAA72977.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73257.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAB96723.1; -; Genomic_DNA.
DR   PIR; A43671; A43671.
DR   RefSeq; NP_414688.1; NC_000913.3.
DR   RefSeq; WP_000396036.1; NZ_STEB01000010.1.
DR   PDB; 4DAP; X-ray; 2.20 A; A=1-234.
DR   PDBsum; 4DAP; -.
DR   AlphaFoldDB; P0A823; -.
DR   SMR; P0A823; -.
DR   BioGRID; 4259743; 19.
DR   BioGRID; 849255; 2.
DR   DIP; DIP-48084N; -.
DR   IntAct; P0A823; 7.
DR   STRING; 511145.b0146; -.
DR   jPOST; P0A823; -.
DR   PaxDb; P0A823; -.
DR   PRIDE; P0A823; -.
DR   EnsemblBacteria; AAC73257; AAC73257; b0146.
DR   EnsemblBacteria; BAB96723; BAB96723; BAB96723.
DR   GeneID; 944855; -.
DR   KEGG; ecj:JW0142; -.
DR   KEGG; eco:b0146; -.
DR   PATRIC; fig|1411691.4.peg.2135; -.
DR   EchoBASE; EB0942; -.
DR   eggNOG; COG1489; Bacteria.
DR   HOGENOM; CLU_052299_2_0_6; -.
DR   InParanoid; P0A823; -.
DR   OMA; VTAHCPN; -.
DR   PhylomeDB; P0A823; -.
DR   BioCyc; EcoCyc:EG10949-MON; -.
DR   PRO; PR:P0A823; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IDA:EcoCyc.
DR   GO; GO:0009891; P:positive regulation of biosynthetic process; IMP:EcoCyc.
DR   HAMAP; MF_00095; SfsA; 1.
DR   InterPro; IPR005224; SfsA.
DR   InterPro; IPR040452; SfsA_C.
DR   InterPro; IPR041465; SfsA_N.
DR   PANTHER; PTHR30545; PTHR30545; 1.
DR   Pfam; PF03749; SfsA; 1.
DR   Pfam; PF17746; SfsA_N; 1.
DR   TIGRFAMs; TIGR00230; sfsA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA-binding; Reference proteome.
FT   CHAIN           1..234
FT                   /note="Sugar fermentation stimulation protein A"
FT                   /id="PRO_0000152282"
FT   DNA_BIND        201..220
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00095"
FT   STRAND          8..16
FT                   /evidence="ECO:0007829|PDB:4DAP"
FT   TURN            17..19
FT                   /evidence="ECO:0007829|PDB:4DAP"
FT   STRAND          20..24
FT                   /evidence="ECO:0007829|PDB:4DAP"
FT   STRAND          30..34
FT                   /evidence="ECO:0007829|PDB:4DAP"
FT   TURN            42..44
FT                   /evidence="ECO:0007829|PDB:4DAP"
FT   STRAND          50..55
FT                   /evidence="ECO:0007829|PDB:4DAP"
FT   STRAND          65..71
FT                   /evidence="ECO:0007829|PDB:4DAP"
FT   STRAND          77..79
FT                   /evidence="ECO:0007829|PDB:4DAP"
FT   HELIX           82..84
FT                   /evidence="ECO:0007829|PDB:4DAP"
FT   HELIX           85..94
FT                   /evidence="ECO:0007829|PDB:4DAP"
FT   HELIX           99..101
FT                   /evidence="ECO:0007829|PDB:4DAP"
FT   STRAND          105..112
FT                   /evidence="ECO:0007829|PDB:4DAP"
FT   STRAND          119..126
FT                   /evidence="ECO:0007829|PDB:4DAP"
FT   STRAND          129..139
FT                   /evidence="ECO:0007829|PDB:4DAP"
FT   STRAND          141..143
FT                   /evidence="ECO:0007829|PDB:4DAP"
FT   STRAND          146..149
FT                   /evidence="ECO:0007829|PDB:4DAP"
FT   HELIX           155..169
FT                   /evidence="ECO:0007829|PDB:4DAP"
FT   STRAND          173..180
FT                   /evidence="ECO:0007829|PDB:4DAP"
FT   STRAND          187..190
FT                   /evidence="ECO:0007829|PDB:4DAP"
FT   TURN            192..194
FT                   /evidence="ECO:0007829|PDB:4DAP"
FT   HELIX           196..207
FT                   /evidence="ECO:0007829|PDB:4DAP"
FT   STRAND          211..220
FT                   /evidence="ECO:0007829|PDB:4DAP"
FT   STRAND          223..229
FT                   /evidence="ECO:0007829|PDB:4DAP"
SQ   SEQUENCE   234 AA;  26229 MW;  8AF528989FE78DCD CRC64;
     MEFSPPLQRA TLIQRYKRFL ADVITPDGRE LTLHCPNTGA MTGCATPGDT VWYSTSDNTK
     RKYPHTWELT QSQSGAFICV NTLWANRLTK EAILNESISE LSGYSSLKSE VKYGAERSRI
     DFMLQADSRP DCYIEVKSVT LAENEQGYFP DAVTERGQKH LRELMSVAAE GQRAVIFFAV
     LHSAITRFSP ARHIDEKYAQ LLSEAQQRGV EILAYKAEIS AEGMALKKSL PVTL