ID   SSPB_SHIFL              Reviewed;         165 AA.
AC   Q83Q08;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Stringent starvation protein B;
DE   AltName: Full=Adapter protein SspB;
DE   AltName: Full=Specificity-enhancing factor SspB;
GN   Name=sspB; OrderedLocusNames=SF3268, S3483;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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 (By similarity). {ECO:0000250}.
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. {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SspB family. {ECO:0000305}.
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DR   EMBL; AE005674; AAN44732.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP18543.1; -; Genomic_DNA.
DR   RefSeq; NP_709025.1; NC_004337.2.
DR   AlphaFoldDB; Q83Q08; -.
DR   SMR; Q83Q08; -.
DR   STRING; 198214.SF3268; -.
DR   EnsemblBacteria; AAN44732; AAN44732; SF3268.
DR   EnsemblBacteria; AAP18543; AAP18543; S3483.
DR   GeneID; 1027107; -.
DR   KEGG; sfl:SF3268; -.
DR   KEGG; sfx:S3483; -.
DR   PATRIC; fig|198214.7.peg.3871; -.
DR   HOGENOM; CLU_118425_0_0_6; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
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   3: Inferred from homology;
KW   Reference proteome.
FT   CHAIN           1..165
FT                   /note="Stringent starvation protein B"
FT                   /id="PRO_0000072221"
FT   REGION          119..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..152
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        29
FT                   /note="L -> H (in Ref. 2; AAP18543)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   165 AA;  18238 MW;  34470BA030AE5F0C CRC64;
     MDLSQLTPRR PYLLRAFYEW LLDNQLTPLL VVDVTLPGVQ VPMEYARDGQ IVLNIAPRAV
     GNLELANDEV RFNARFGGIP RQVSVPLAAV LAIYARENGA GTMFEPEAAY DEDTSIMNDE
     EASADNETVM SVIDGDKPDH DDDTHPDDEP PQPPRGGRPA LRVVK