SSB_ECOLI
ID SSB_ECOLI Reviewed; 178 AA.
AC P0AGE0; P02339; Q2M6P5;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Single-stranded DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_00984};
DE Short=SSB {ECO:0000255|HAMAP-Rule:MF_00984};
DE AltName: Full=Helix-destabilizing protein;
GN Name=ssb; Synonyms=exrB, lexC; OrderedLocusNames=b4059, JW4020;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-53.
RX PubMed=6270666; DOI=10.1073/pnas.78.7.4274;
RA Sancar A., Williams K.R., Chase J.W., Rupp W.D.;
RT "Sequences of the ssb gene and protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:4274-4278(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6351061; DOI=10.1073/pnas.80.18.5480;
RA Chase J.W., Merrill B.M., Williams K.R.;
RT "F sex factor encodes a single-stranded DNA binding protein (SSB) with
RT extensive sequence homology to Escherichia coli SSB.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:5480-5484(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
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 PROTEIN SEQUENCE OF 2-41.
RX PubMed=7042342; DOI=10.1111/j.1432-1033.1982.tb19784.x;
RA Beyreuther K., Berthold-Schmidt V., Geider K.;
RT "Biological activity and a partial amino-acid sequence of Escherichia coli
RT DNA-binding protein I isolated from overproducing cells.";
RL Eur. J. Biochem. 123:415-420(1982).
RN [7]
RP CHARACTERIZATION, AND SEQUENCE REVISION TO 134.
RX PubMed=6363409; DOI=10.1016/s0021-9258(17)43529-0;
RA Chase J.W., L'Italien J.J., Murphy J.B., Spicer E.K., Williams K.R.;
RT "Characterization of the Escherichia coli SSB-113 mutant single-stranded
RT DNA-binding protein. Cloning of the gene, DNA and protein sequence
RT analysis, high pressure liquid chromatography peptide mapping, and DNA-
RT binding studies.";
RL J. Biol. Chem. 259:805-814(1984).
RN [8]
RP MUTANT SSB-1.
RX PubMed=6384214; DOI=10.1016/s0021-9258(20)71283-4;
RA Williams K.R., Murphy J.B., Chase J.W.;
RT "Characterization of the structural and functional defect in the
RT Escherichia coli single-stranded DNA binding protein encoded by the ssb-1
RT mutant gene. Expression of the ssb-1 gene under lambda pL regulation.";
RL J. Biol. Chem. 259:11804-11811(1984).
RN [9]
RP MUTAGENESIS, AND DNA-BINDING.
RX PubMed=3301414; DOI=10.1016/0014-5793(87)80844-x;
RA Casas-Finet J.R., Khamis M.I., Maki A.W., Chase J.W.;
RT "Tryptophan 54 and phenylalanine 60 are involved synergistically in the
RT binding of E. coli SSB protein to single-stranded polynucleotides.";
RL FEBS Lett. 220:347-352(1987).
RN [10]
RP REVIEW.
RX PubMed=2087220; DOI=10.1128/mr.54.4.342-380.1990;
RA Meyer R.R., Laine P.S.;
RT "The single-stranded DNA-binding protein of Escherichia coli.";
RL Microbiol. Rev. 54:342-380(1990).
RN [11]
RP MUTANT SSB-1, AND DNA-BINDING.
RX PubMed=1988680; DOI=10.1016/0022-2836(91)90611-9;
RA Bujalowski W., Lohman T.M.;
RT "Monomers of the Escherichia coli SSB-1 mutant protein bind single-stranded
RT DNA.";
RL J. Mol. Biol. 217:63-74(1991).
RN [12]
RP INTERACTION WITH RECO.
RX PubMed=7962001; DOI=10.1016/s0021-9258(18)43981-6;
RA Umezu K., Kolodner R.D.;
RT "Protein interactions in genetic recombination in Escherichia coli.
RT Interactions involving RecO and RecR overcome the inhibition of RecA by
RT single-stranded DNA-binding protein.";
RL J. Biol. Chem. 269:30005-30013(1994).
RN [13]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [14]
RP MUTANTS SSB-200; SSB-201 AND SSB-202.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9139905; DOI=10.1128/jb.179.9.2892-2899.1997;
RA Reddy M., Gowrishankar J.;
RT "Identification and characterization of ssb and uup mutants with increased
RT frequency of precise excision of transposon Tn10 derivatives: nucleotide
RT sequence of uup in Escherichia coli.";
RL J. Bacteriol. 179:2892-2899(1997).
RN [15]
RP INTERACTION WITH HOLC.
RX PubMed=9545254; DOI=10.1093/emboj/17.8.2436;
RA Kelman Z., Yuzhakov A., Andjelkovic J., O'Donnell M.;
RT "Devoted to the lagging strand-the subunit of DNA polymerase III holoenzyme
RT contacts SSB to promote processive elongation and sliding clamp assembly.";
RL EMBO J. 17:2436-2449(1998).
RN [16]
RP INTERACTION WITH EXONUCLEASE I (SBCB).
RX PubMed=10782989; DOI=10.1515/bc.2000.025;
RA Genschel J., Curth U., Urbanke C.;
RT "Interaction of E. coli single-stranded DNA binding protein (SSB) with
RT exonuclease I. The carboxy-terminus of SSB is the recognition site for the
RT nuclease.";
RL Biol. Chem. 381:183-192(2000).
RN [17]
RP DNA-BINDING, AND INTERACTION WITH PRIA.
RX PubMed=15576682; DOI=10.1093/nar/gkh980;
RA Cadman C.J., McGlynn P.;
RT "PriA helicase and SSB interact physically and functionally.";
RL Nucleic Acids Res. 32:6378-6387(2004).
RN [18]
RP PHOSPHORYLATION.
RX PubMed=16549871; DOI=10.1093/nar/gkj514;
RA Mijakovic I., Petranovic D., Macek B., Cepo T., Mann M., Davies J.,
RA Jensen P.R., Vujaklija D.;
RT "Bacterial single-stranded DNA-binding proteins are phosphorylated on
RT tyrosine.";
RL Nucleic Acids Res. 34:1588-1596(2006).
RN [19]
RP INTERACTION WITH RECQ.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=17483090; DOI=10.1074/jbc.m608011200;
RA Shereda R.D., Bernstein D.A., Keck J.L.;
RT "A central role for SSB in Escherichia coli RecQ DNA helicase function.";
RL J. Biol. Chem. 282:19247-19258(2007).
RN [20]
RP REVIEW, AND FUNCTION.
RX PubMed=18937104; DOI=10.1080/10409230802341296;
RA Shereda R.D., Kozlov A.G., Lohman T.M., Cox M.M., Keck J.L.;
RT "SSB as an organizer/mobilizer of genome maintenance complexes.";
RL Crit. Rev. Biochem. Mol. Biol. 43:289-318(2008).
RN [21]
RP INTERACTION WITH EXONUCLEASE I (SBCB), AND MUTAGENESIS OF PRO-177.
RX PubMed=18591666; DOI=10.1073/pnas.0800741105;
RA Lu D., Keck J.L.;
RT "Structural basis of Escherichia coli single-stranded DNA-binding protein
RT stimulation of exonuclease I.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:9169-9174(2008).
RN [22]
RP FUNCTION, DNA-BINDING, AND ACTIVITY REGULATION.
RX PubMed=20360609; DOI=10.1074/jbc.m110.118273;
RA Kozlov A.G., Cox M.M., Lohman T.M.;
RT "Regulation of single-stranded DNA binding by the C termini of Escherichia
RT coli single-stranded DNA-binding (SSB) protein.";
RL J. Biol. Chem. 285:17246-17252(2010).
RN [23]
RP INTERACTION WITH EXONUCLEASE I (SBCB).
RX PubMed=20018747; DOI=10.1073/pnas.0909191107;
RA Lu D., Bernstein D.A., Satyshur K.A., Keck J.L.;
RT "Small-molecule tools for dissecting the roles of SSB/protein interactions
RT in genome maintenance.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:633-638(2010).
RN [24]
RP FUNCTION.
RX PubMed=21784244; DOI=10.1016/j.cell.2011.06.036;
RA Zhou R., Kozlov A.G., Roy R., Zhang J., Korolev S., Lohman T.M., Ha T.;
RT "SSB functions as a sliding platform that migrates on DNA via reptation.";
RL Cell 146:222-232(2011).
RN [25]
RP INTERACTION WITH DNAG.
RX PubMed=23430154; DOI=10.1093/nar/gkt107;
RA Naue N., Beerbaum M., Bogutzki A., Schmieder P., Curth U.;
RT "The helicase-binding domain of Escherichia coli DnaG primase interacts
RT with the highly conserved C-terminal region of single-stranded DNA-binding
RT protein.";
RL Nucleic Acids Res. 41:4507-4517(2013).
RN [26]
RP INTERACTION WITH PRIB.
RX PubMed=23963891; DOI=10.1007/s10930-013-9509-y;
RA Huang Y.H., Lin M.J., Huang C.Y.;
RT "Yeast two-hybrid analysis of PriB-interacting proteins in replication
RT restart primosome: a proposed PriB-SSB interaction model.";
RL Protein J. 32:477-483(2013).
RN [27]
RP FUNCTION, INTERACTION WITH RADD, AND MUTAGENESIS OF 171-ASP--PHE-178.
RC STRAIN=K12 / MG1655 (DE3);
RX PubMed=27519413; DOI=10.1074/jbc.m116.736223;
RA Chen S.H., Byrne-Nash R.T., Cox M.M.;
RT "Escherichia coli RadD Protein Functionally Interacts with the Single-
RT stranded DNA-binding Protein.";
RL J. Biol. Chem. 291:20779-20786(2016).
RN [28]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-136, AND SUBUNIT.
RX PubMed=9192620; DOI=10.1073/pnas.94.13.6652;
RA Raghunathan S., Ricard C.S., Lohman T.M., Waksman G.;
RT "Crystal structure of the homo-tetrameric DNA binding domain of Escherichia
RT coli single-stranded DNA-binding protein determined by multiwavelength X-
RT ray diffraction on the selenomethionyl protein at 2.9-A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:6652-6657(1997).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-136, DNA-BINDING, AND SUBUNIT.
RX PubMed=10932248; DOI=10.1038/77943;
RA Raghunathan S., Kozlov A.G., Lohman T.M., Waksman G.;
RT "Structure of the DNA binding domain of E. coli SSB bound to ssDNA.";
RL Nat. Struct. Biol. 7:648-652(2000).
CC -!- FUNCTION: Plays an important role in DNA replication, recombination and
CC repair. Binds to ssDNA and to an array of partner proteins to recruit
CC them to their sites of action during DNA metabolism. Acts as a sliding
CC platform that migrates on DNA via reptation. SSB or its 10 C-terminal
CC amino acids stimulates the ATPase activity of RadD (PubMed:27519413).
CC {ECO:0000255|HAMAP-Rule:MF_00984, ECO:0000269|PubMed:18937104,
CC ECO:0000269|PubMed:20360609, ECO:0000269|PubMed:21784244,
CC ECO:0000269|PubMed:27519413}.
CC -!- ACTIVITY REGULATION: The C-terminal tail exerts an inhibitory effect on
CC ssDNA binding. {ECO:0000269|PubMed:20360609}.
CC -!- SUBUNIT: Homotetramer. Interacts, via its C-terminus, with several
CC proteins involved in DNA metabolism such as DnaG, HolC, PriA, PriB,
CC RecO, RecQ and SbcB. Interacts with RadD (PubMed:27519413).
CC {ECO:0000255|HAMAP-Rule:MF_00984, ECO:0000269|PubMed:10782989,
CC ECO:0000269|PubMed:10932248, ECO:0000269|PubMed:15576682,
CC ECO:0000269|PubMed:17483090, ECO:0000269|PubMed:18591666,
CC ECO:0000269|PubMed:20018747, ECO:0000269|PubMed:23430154,
CC ECO:0000269|PubMed:23963891, ECO:0000269|PubMed:27519413,
CC ECO:0000269|PubMed:7962001, ECO:0000269|PubMed:9192620,
CC ECO:0000269|PubMed:9545254}.
CC -!- INTERACTION:
CC P0AGE0; P27296: dinG; NbExp=2; IntAct=EBI-1118620, EBI-1114590;
CC P0AGE0; P0ABS5: dnaG; NbExp=2; IntAct=EBI-1118620, EBI-549259;
CC P0AGE0; P06710: dnaX; NbExp=2; IntAct=EBI-1118620, EBI-549140;
CC P0AGE0; P28905: holC; NbExp=10; IntAct=EBI-1118620, EBI-549169;
CC P0AGE0; P17888: priA; NbExp=3; IntAct=EBI-1118620, EBI-552050;
CC P0AGE0; P0A7H3: recO; NbExp=3; IntAct=EBI-1118620, EBI-1129540;
CC P0AGE0; P0AGE0: ssb; NbExp=2; IntAct=EBI-1118620, EBI-1118620;
CC -!- PTM: Phosphorylated on tyrosine residue(s).
CC {ECO:0000269|PubMed:16549871}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J01704; AAA24649.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43153.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77029.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78061.1; -; Genomic_DNA.
DR PIR; B65214; DDEC.
DR RefSeq; NP_418483.1; NC_000913.3.
DR RefSeq; WP_000168305.1; NZ_STEB01000022.1.
DR PDB; 1EQQ; X-ray; 3.20 A; A/B/C/D=1-178.
DR PDB; 1EYG; X-ray; 2.80 A; A/B/C/D=1-116.
DR PDB; 1KAW; X-ray; 2.90 A; A/B/C/D=2-136.
DR PDB; 1QVC; X-ray; 2.20 A; A/B/C/D=2-146.
DR PDB; 1SRU; X-ray; 3.30 A; A/B/C/D=1-113.
DR PDB; 3C94; X-ray; 2.70 A; B/C=170-178.
DR PDB; 3SXU; X-ray; 1.85 A; C=175-178.
DR PDB; 3UF7; X-ray; 1.20 A; B/C=170-178.
DR PDB; 4MZ9; X-ray; 2.20 A; A/B/C/D=1-178.
DR PDB; 4Z0U; X-ray; 2.00 A; D/E=170-178.
DR PDBsum; 1EQQ; -.
DR PDBsum; 1EYG; -.
DR PDBsum; 1KAW; -.
DR PDBsum; 1QVC; -.
DR PDBsum; 1SRU; -.
DR PDBsum; 3C94; -.
DR PDBsum; 3SXU; -.
DR PDBsum; 3UF7; -.
DR PDBsum; 4MZ9; -.
DR PDBsum; 4Z0U; -.
DR AlphaFoldDB; P0AGE0; -.
DR BMRB; P0AGE0; -.
DR SMR; P0AGE0; -.
DR BioGRID; 4262671; 106.
DR BioGRID; 852864; 1.
DR ComplexPortal; CPX-1928; SSB single-stranded DNA binding complex.
DR DIP; DIP-35980N; -.
DR IntAct; P0AGE0; 57.
DR MINT; P0AGE0; -.
DR STRING; 511145.b4059; -.
DR DrugBank; DB04243; TMP.
DR SWISS-2DPAGE; P0AGE0; -.
DR jPOST; P0AGE0; -.
DR PaxDb; P0AGE0; -.
DR PRIDE; P0AGE0; -.
DR EnsemblBacteria; AAC77029; AAC77029; b4059.
DR EnsemblBacteria; BAE78061; BAE78061; BAE78061.
DR GeneID; 66672025; -.
DR GeneID; 948570; -.
DR KEGG; ecj:JW4020; -.
DR KEGG; eco:b4059; -.
DR PATRIC; fig|511145.12.peg.4180; -.
DR EchoBASE; EB0969; -.
DR eggNOG; COG0629; Bacteria.
DR HOGENOM; CLU_078758_0_2_6; -.
DR InParanoid; P0AGE0; -.
DR OMA; GQMQERT; -.
DR PhylomeDB; P0AGE0; -.
DR BioCyc; EcoCyc:EG10976-MON; -.
DR BioCyc; MetaCyc:EG10976-MON; -.
DR EvolutionaryTrace; P0AGE0; -.
DR PRO; PR:P0AGE0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0009295; C:nucleoid; IBA:GO_Central.
DR GO; GO:0030894; C:replisome; IC:ComplexPortal.
DR GO; GO:0044777; C:single-stranded DNA-binding protein complex; IPI:ComplexPortal.
DR GO; GO:0008047; F:enzyme activator activity; IMP:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:EcoCyc.
DR GO; GO:0006261; P:DNA-templated DNA replication; IC:ComplexPortal.
DR GO; GO:0006298; P:mismatch repair; TAS:EcoCyc.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IMP:UniProtKB.
DR GO; GO:0051096; P:positive regulation of helicase activity; IBA:GO_Central.
DR GO; GO:0000725; P:recombinational repair; TAS:EcoCyc.
DR GO; GO:0009432; P:SOS response; TAS:EcoCyc.
DR CDD; cd04496; SSB_OBF; 1.
DR DisProt; DP02137; -.
DR Gene3D; 2.40.50.140; -; 1.
DR HAMAP; MF_00984; SSB; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR000424; Primosome_PriB/ssb.
DR InterPro; IPR011344; ssDNA-bd.
DR PANTHER; PTHR10302; PTHR10302; 1.
DR Pfam; PF00436; SSB; 1.
DR PIRSF; PIRSF002070; SSB; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00621; ssb; 1.
DR PROSITE; PS50935; SSB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA damage; DNA recombination;
KW DNA repair; DNA replication; DNA-binding; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6270666,
FT ECO:0000269|PubMed:7042342"
FT CHAIN 2..178
FT /note="Single-stranded DNA-binding protein"
FT /id="PRO_0000096036"
FT DOMAIN 6..111
FT /note="SSB"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT DNA_BIND 55..61
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT REGION 113..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 173..178
FT /note="Important for interaction with partner proteins"
FT COMPBIAS 133..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 5
FT /note="G->D: Increased frequency of precise excision of
FT transposon Tn10 derivatives (mutant SSB-200)."
FT /evidence="ECO:0000269|PubMed:3301414"
FT MUTAGEN 11
FT /note="L->F: Increased frequency of precise excision of
FT transposon Tn10 derivatives (mutant SSB-202)."
FT /evidence="ECO:0000269|PubMed:3301414"
FT MUTAGEN 25
FT /note="P->S: Increased frequency of precise excision of
FT transposon Tn10 derivatives (mutant SSB-202)."
FT /evidence="ECO:0000269|PubMed:3301414"
FT MUTAGEN 56
FT /note="H->L: Reduces DNA-binding affinity."
FT /evidence="ECO:0000269|PubMed:3301414"
FT MUTAGEN 56
FT /note="H->Y: Destabilizes the tetramer (mutant SSB-1)."
FT /evidence="ECO:0000269|PubMed:3301414"
FT MUTAGEN 61
FT /note="F->A: Reduces DNA-binding affinity."
FT /evidence="ECO:0000269|PubMed:3301414"
FT MUTAGEN 103
FT /note="V->M: Increased frequency of precise excision of
FT transposon Tn10 derivatives (mutant SSB-201)."
FT /evidence="ECO:0000269|PubMed:3301414"
FT MUTAGEN 171..178
FT /note="Missing: No longer interacts with RadD."
FT /evidence="ECO:0000269|PubMed:27519413"
FT MUTAGEN 177
FT /note="P->S: Strongly reduced exonuclease I (sbcB)
FT stimulation."
FT /evidence="ECO:0000269|PubMed:18591666"
FT CONFLICT 121
FT /note="A -> AQ (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="G -> S (in Ref. 1; AAA24649)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="D -> DG (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT STRAND 6..17
FT /evidence="ECO:0007829|PDB:1QVC"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:1QVC"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:1QVC"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:1QVC"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:1QVC"
FT STRAND 54..61
FT /evidence="ECO:0007829|PDB:1QVC"
FT HELIX 63..71
FT /evidence="ECO:0007829|PDB:1QVC"
FT STRAND 77..89
FT /evidence="ECO:0007829|PDB:1QVC"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:1QVC"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:1QVC"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:1EQQ"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:1QVC"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:1QVC"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:1QVC"
SQ SEQUENCE 178 AA; 18975 MW; F0AF43B6DC8D02FC CRC64;
MASRGVNKVI LVGNLGQDPE VRYMPNGGAV ANITLATSES WRDKATGEMK EQTEWHRVVL
FGKLAEVASE YLRKGSQVYI EGQLRTRKWT DQSGQDRYTT EVVVNVGGTM QMLGGRQGGG
APAGGNIGGG QPQGGWGQPQ QPQGGNQFSG GAQSRPQQSA PAAPSNEPPM DFDDDIPF
