SSPB_ECOLI
ID SSPB_ECOLI Reviewed; 165 AA.
AC P0AFZ3; P25663; Q2M8Y5;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Stringent starvation protein B;
DE AltName: Full=Adapter protein SspB;
DE AltName: Full=Specificity-enhancing factor SspB;
GN Name=sspB; OrderedLocusNames=b3228, JW3197;
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=1721886; DOI=10.1016/0378-1119(91)90584-x;
RA Williams M.D., Fuchs J.A., Flickinger M.C.;
RT "Null mutation in the stringent starvation protein of Escherichia coli
RT disrupts lytic development of bacteriophage P1.";
RL Gene 109:21-30(1991).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-139.
RX PubMed=3029697; DOI=10.1093/nar/15.3.1153;
RA Serizawa H., Fukuda R.;
RT "Structure of the gene for the stringent starvation protein of Escherichia
RT coli.";
RL Nucleic Acids Res. 15:1153-1163(1987).
RN [5]
RP PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, INTERACTION WITH SSRA-TAGGED
RP PROTEINS, AND DISRUPTION PHENOTYPE.
RX PubMed=11009422; DOI=10.1126/science.289.5488.2354;
RA Levchenko I., Seidel M., Sauer R.T., Baker T.A.;
RT "A specificity-enhancing factor for the ClpXP degradation machine.";
RL Science 289:2354-2356(2000).
RN [6]
RP CHARACTERIZATION, AND INDUCTION.
RX PubMed=8022275; DOI=10.1111/j.1365-2958.1994.tb00381.x;
RA Williams M.D., Ouyang T.X., Flickinger M.C.;
RT "Starvation-induced expression of SspA and SspB: the effects of a null
RT mutation in sspA on Escherichia coli protein synthesis and survival during
RT growth and prolonged starvation.";
RL Mol. Microbiol. 11:1029-1043(1994).
RN [7]
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 [8]
RP FUNCTION, INTERACTION WITH RPOE AND RSEA, INTERACTION WITH SSRA TAG, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=15371343; DOI=10.1101/gad.1240104;
RA Flynn J.M., Levchenko I., Sauer R.T., Baker T.A.;
RT "Modulating substrate choice: the SspB adaptor delivers a regulator of the
RT extracytoplasmic-stress response to the AAA+ protease ClpXP for
RT degradation.";
RL Genes Dev. 18:2292-2301(2004).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 4-111 IN COMPLEX WITH SSRA TAG,
RP FUNCTION IN ACTIVATING CLPX, SUBUNIT, AND DOMAIN.
RX PubMed=12887894; DOI=10.1016/s1097-2765(03)00271-5;
RA Song H.K., Eck M.J.;
RT "Structural basis of degradation signal recognition by SspB, a specificity-
RT enhancing factor for the ClpXP proteolytic machine.";
RL Mol. Cell 12:75-86(2003).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-118 IN COMPLEX WITH RSEA
RP N-TERMINAL FRAGMENT, SUBUNIT, AND MUTAGENESIS OF VAL-52; ALA-59 AND ALA-74.
RX PubMed=15880122; DOI=10.1038/nsmb934;
RA Levchenko I., Grant R.A., Flynn J.M., Sauer R.T., Baker T.A.;
RT "Versatile modes of peptide recognition by the AAA+ adaptor protein SspB.";
RL Nat. Struct. Mol. Biol. 12:520-525(2005).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 159-165 IN COMPLEX WITH CLPX
RP N-TERMINAL FRAGMENT.
RX PubMed=17258768; DOI=10.1016/j.jmb.2007.01.003;
RA Park E.Y., Lee B.G., Hong S.B., Kim H.W., Jeon H., Song H.K.;
RT "Structural basis of SspB-tail recognition by the zinc binding domain of
RT ClpX.";
RL J. Mol. Biol. 367:514-526(2007).
CC -!- FUNCTION: Enhances recognition of ssrA-tagged proteins by the ClpX-ClpP
CC protease; the ssrA degradation tag (AANDENYALAA) is added trans-
CC translationally to proteins that are stalled on the ribosome, freeing
CC the ribosome and targeting stalled peptides for degradation. SspB
CC activates the ATPase activity of ClpX. Seems to act in concert with
CC SspA in the regulation of several proteins during exponential and
CC stationary-phase growth.
CC -!- FUNCTION: Also stimulates degradation of the N-terminus of RseA
CC (residues 1-108, alone or in complex with sigma-E) by ClpX-ClpP in a
CC non-ssrA-mediated fashion.
CC -!- SUBUNIT: Homodimer. Binds 1 ssrA-tag per monomer; if the first Asn
CC residue of the ssrA tag is mutated to Ala, SspB no longer binds the
CC protein or stimulates ClpX-ClpP degradation (PubMed:11009422). Binds
CC the N-terminus (residues 1-108) of RseA with and without sigma-E
CC (PubMed:15371343); although ssrA and the N-terminal fragment of RseA
CC both bind to SspB competitively they bind in opposite directions in its
CC peptide-binding groove. {ECO:0000269|PubMed:11009422,
CC ECO:0000269|PubMed:12887894, ECO:0000269|PubMed:15371343,
CC ECO:0000269|PubMed:15880122, ECO:0000269|PubMed:17258768}.
CC -!- INDUCTION: By amino acid starvation. {ECO:0000269|PubMed:8022275}.
CC -!- DISRUPTION PHENOTYPE: Decreased degradation of ssrA-tagged proteins by
CC ClpX-ClpP, no effect on degradation by ClpA-ClpP protease. Delayed and
CC decreased induction of the extracytoplasmic-stress response.
CC {ECO:0000269|PubMed:11009422, ECO:0000269|PubMed:15371343}.
CC -!- SIMILARITY: Belongs to the SspB family. {ECO:0000305}.
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DR EMBL; M69028; AAA24650.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58030.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76260.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77271.1; -; Genomic_DNA.
DR EMBL; X05088; CAA28741.1; -; Genomic_DNA.
DR PIR; JS0666; JS0666.
DR RefSeq; NP_417695.1; NC_000913.3.
DR RefSeq; WP_000366129.1; NZ_STEB01000012.1.
DR PDB; 1OX8; X-ray; 2.20 A; A/B=5-111.
DR PDB; 1OX9; X-ray; 2.90 A; A/B/C/D/E/F/G/H=4-111.
DR PDB; 1YFN; X-ray; 1.80 A; A/B/C/D=1-118.
DR PDB; 2DS8; X-ray; 1.60 A; P/Q=159-165.
DR PDBsum; 1OX8; -.
DR PDBsum; 1OX9; -.
DR PDBsum; 1YFN; -.
DR PDBsum; 2DS8; -.
DR AlphaFoldDB; P0AFZ3; -.
DR SMR; P0AFZ3; -.
DR BioGRID; 4262444; 119.
DR BioGRID; 849176; 1.
DR DIP; DIP-29563N; -.
DR IntAct; P0AFZ3; 31.
DR STRING; 511145.b3228; -.
DR SWISS-2DPAGE; P0AFZ3; -.
DR jPOST; P0AFZ3; -.
DR PaxDb; P0AFZ3; -.
DR PRIDE; P0AFZ3; -.
DR EnsemblBacteria; AAC76260; AAC76260; b3228.
DR EnsemblBacteria; BAE77271; BAE77271; BAE77271.
DR GeneID; 66672876; -.
DR GeneID; 944774; -.
DR KEGG; ecj:JW3197; -.
DR KEGG; eco:b3228; -.
DR PATRIC; fig|1411691.4.peg.3500; -.
DR EchoBASE; EB0971; -.
DR eggNOG; COG2969; Bacteria.
DR HOGENOM; CLU_118425_0_0_6; -.
DR InParanoid; P0AFZ3; -.
DR OMA; FQARFGG; -.
DR PhylomeDB; P0AFZ3; -.
DR BioCyc; EcoCyc:EG10978-MON; -.
DR EvolutionaryTrace; P0AFZ3; -.
DR PRO; PR:P0AFZ3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0009376; C:HslUV protease complex; IMP:CAFA.
DR GO; GO:0005840; C:ribosome; IDA:EcoCyc.
DR GO; GO:0051117; F:ATPase binding; IPI:CAFA.
DR GO; GO:0042803; F:protein homodimerization activity; IMP:CAFA.
DR GO; GO:0003723; F:RNA binding; IMP:CAFA.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; IMP:CAFA.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:EcoCyc.
DR DisProt; DP00194; -.
DR Gene3D; 2.30.30.220; -; 1.
DR InterPro; IPR007481; SspB.
DR InterPro; IPR036760; SspB-like_sf.
DR PANTHER; PTHR37486; PTHR37486; 1.
DR Pfam; PF04386; SspB; 1.
DR PIRSF; PIRSF005276; SspB; 1.
DR SUPFAM; SSF101738; SSF101738; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Reference proteome;
KW Stress response.
FT CHAIN 1..165
FT /note="Stringent starvation protein B"
FT /id="PRO_0000072218"
FT REGION 73..95
FT /note="Binds SspB"
FT REGION 119..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..165
FT /note="Required for interaction with ClpX, not required for
FT ssrA tag recognition or dimerization"
FT COMPBIAS 132..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 52
FT /note="V->D,M,Q: No folded protein."
FT /evidence="ECO:0000269|PubMed:15880122"
FT MUTAGEN 52
FT /note="V->I: 2.5-fold reduction in binding of RseA, no
FT effect on ssrA-tag binding."
FT /evidence="ECO:0000269|PubMed:15880122"
FT MUTAGEN 59
FT /note="A->T: 10-fold reduction in binding of ssrA tag and
FT RseA."
FT /evidence="ECO:0000269|PubMed:15880122"
FT MUTAGEN 74
FT /note="A->Q: Severe reduction in binding of ssrA tag (40-
FT fold) and RseA (100-fold)."
FT /evidence="ECO:0000269|PubMed:15880122"
FT HELIX 10..23
FT /evidence="ECO:0007829|PDB:1YFN"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:1YFN"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:1YFN"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:1YFN"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:1YFN"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:1YFN"
FT STRAND 67..76
FT /evidence="ECO:0007829|PDB:1YFN"
FT STRAND 79..86
FT /evidence="ECO:0007829|PDB:1YFN"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:1YFN"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:1YFN"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:1YFN"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:1YFN"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:1YFN"
SQ SEQUENCE 165 AA; 18262 MW; 363ECEB430AE5A18 CRC64;
MDLSQLTPRR PYLLRAFYEW LLDNQLTPHL VVDVTLPGVQ VPMEYARDGQ IVLNIAPRAV
GNLELANDEV RFNARFGGIP RQVSVPLAAV LAIYARENGA GTMFEPEAAY DEDTSIMNDE
EASADNETVM SVIDGDKPDH DDDTHPDDEP PQPPRGGRPA LRVVK
